anti pcna mouse mab  (Vector Laboratories)


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    Name:
    Biotinylated Rabbit Anti Goat IgG Antibody
    Description:
    Biotinylated Rabbit Anti Goat IgG Antibody is prepared using proprietary immunization schedules that produce high affinity antibodies The antibodies are then purified by affinity chromatography and cross reactivities that are likely to interfere with specific labeling are removed by solid phase adsorption techniques The biotinylated secondary antibodies are conjugated to ensure the maximum degree of labeling without compromising the specificity or affinity of the antibody These antibodies are subjected to rigorous quality control assays and can be used for tissue and cell staining ELISAs and blots Biotinylated Rabbit Anti Goat IgG H L is supplied in liquid format With some exceptions the recommended dilution for most applications is 1 200 H L indicates the antibody recognizes both heavy and light chains The use of bovine products such as casein serum albumin or non fat dry milk as blocking agents in ELISA or blot assays may produce a high background due to cross reactivity of this antibody with bovine immunoglobulins that may be present If this antibody is to be used in these applications blocking with Animal Free Blocker solution Cat No SP 5030 is recommended This antibody is included in the VECTASTAIN ABC kits This antibody is suitable for use with goat sheep and bovine IgG primary antibodies
    Catalog Number:
    ba-5000
    Price:
    None
    Host:
    Rabbit
    Size:
    1 5 mg
    Category:
    Antibodies
    Reactivity:
    Goat
    Buy from Supplier


    Structured Review

    Vector Laboratories anti pcna mouse mab
    Biotinylated Rabbit Anti Goat IgG Antibody
    Biotinylated Rabbit Anti Goat IgG Antibody is prepared using proprietary immunization schedules that produce high affinity antibodies The antibodies are then purified by affinity chromatography and cross reactivities that are likely to interfere with specific labeling are removed by solid phase adsorption techniques The biotinylated secondary antibodies are conjugated to ensure the maximum degree of labeling without compromising the specificity or affinity of the antibody These antibodies are subjected to rigorous quality control assays and can be used for tissue and cell staining ELISAs and blots Biotinylated Rabbit Anti Goat IgG H L is supplied in liquid format With some exceptions the recommended dilution for most applications is 1 200 H L indicates the antibody recognizes both heavy and light chains The use of bovine products such as casein serum albumin or non fat dry milk as blocking agents in ELISA or blot assays may produce a high background due to cross reactivity of this antibody with bovine immunoglobulins that may be present If this antibody is to be used in these applications blocking with Animal Free Blocker solution Cat No SP 5030 is recommended This antibody is included in the VECTASTAIN ABC kits This antibody is suitable for use with goat sheep and bovine IgG primary antibodies
    https://www.bioz.com/result/anti pcna mouse mab/product/Vector Laboratories
    Average 85 stars, based on 2334 article reviews
    Price from $9.99 to $1999.99
    anti pcna mouse mab - by Bioz Stars, 2020-09
    85/100 stars

    Images

    1) Product Images from "Depletion of CD8+ T cells enhances airway remodelling in a rodent model of asthma"

    Article Title: Depletion of CD8+ T cells enhances airway remodelling in a rodent model of asthma

    Journal: Immunology

    doi: 10.1111/j.1365-2567.2008.02876.x

    Histological sections of airways from rats chronically challenged with phosphate-buffered saline (PBS), treated with control ascites (PBS/Cont group), rats chronically challenged with ovalbumin (OVA), treated with control ascites (OVA/Cont group) and rats chronically challenged with OVA, treated with OX-8 monoclonal antibody (OVA/OX-8 group). Periodic acid–Schiff staining for the detection of mucus-containing cells (a–c), proliferating cell nuclear antigen immunohistochemistry for the detection of proliferating epithelial cells (d–f), and α-smooth muscle actin immunohistochemistry for the detection of airway smooth muscle (g–i) in rat airways.
    Figure Legend Snippet: Histological sections of airways from rats chronically challenged with phosphate-buffered saline (PBS), treated with control ascites (PBS/Cont group), rats chronically challenged with ovalbumin (OVA), treated with control ascites (OVA/Cont group) and rats chronically challenged with OVA, treated with OX-8 monoclonal antibody (OVA/OX-8 group). Periodic acid–Schiff staining for the detection of mucus-containing cells (a–c), proliferating cell nuclear antigen immunohistochemistry for the detection of proliferating epithelial cells (d–f), and α-smooth muscle actin immunohistochemistry for the detection of airway smooth muscle (g–i) in rat airways.

    Techniques Used: Staining, Immunohistochemistry

    Morphometric quantification of proliferating cell nuclear antigen (PCNA)-positive proliferating epithelial cells by PCNA immunohistochemistry. The number of positive cells per unit length of the basement membrane perimeter ( P BM ) in small ( P BM
    Figure Legend Snippet: Morphometric quantification of proliferating cell nuclear antigen (PCNA)-positive proliferating epithelial cells by PCNA immunohistochemistry. The number of positive cells per unit length of the basement membrane perimeter ( P BM ) in small ( P BM

    Techniques Used: Immunohistochemistry

    2) Product Images from "Sox-2 Positive Neural Progenitors in the Primate Striatum Undergo Dynamic Changes after Dopamine Denervation"

    Article Title: Sox-2 Positive Neural Progenitors in the Primate Striatum Undergo Dynamic Changes after Dopamine Denervation

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0066377

    Ultra-structural analysis of Sox-2 expression. A. Sox-2 immuno-gold label is observed in the nucleus (arrowheads) in ependymal cells and astrocytes in ultra-thin sections of the SVZ. Boxed areas show an ependymal cell (E) and an astrocyte (As). Ependymal layer (EL), gap layer (HL), astrocyte ribbon layer (R). Scale bar = 20 um; Scale bar in boxed areas = 1 um. a1. Magnification shows a Sox-2 + astrocyte and lack of immunoreactivity in an oligodendrocyte (O) and a microglial cell (Mi). Astrocytes are recognized by the presence of dense bundles of intermediate filaments (arrows). Scale bar = 2 um. B. Sox-2 immuno-gold staining in a group of neuroblasts (type A cells). Scale bar = 20 um. b1. Magnification of three neuroblasts showing the nuclear staining. Neuroblasts form chain-like structures with characteristic intercellular spaces (arrows). Scale bar = 2 um. C. Light microscopy image of a semi-thin section showing the distribution and characterization of cells expressing Sox-2 in the dentate gyrus. Sox-2 + cells are visualized by the nuclear dark brown DAB precipitate. The section was counterstained with toluidine blue. The line marks the boundary between the granular layer (GrL) and the hilus (H) where most labeled cells were located. Scale bar = 100 um. c1 ) Neurons in the granular layer were not Sox-2 + . Scale bar = 10 um; Insert = 1 um. D. Microphotograph of a striatal field of a control monkey showing a Sox-2 + astrocyte and unlabeled neuron (Neu) and microglial cells (Mi). Scale bar = 5 um. d1. Boxed area of the astrocyte (As) nucleus shows the gold particles (arrowheads). Scale bar = 1 um. E. A representative Sox-2 + neuron in the striatum of a control monkey. Scale bar = 2 um. e1. Boxed area shows deposition of gold particles over the nucleus (arrowheads) close to a synapse (arrow), which identifies this cell as a neuron. Scale bar = 1 um. F. Sox-2 + astrocyte in the substantia nigra pars compacta. Scale bar = 10 µm. f1. Boxed area shows a dense bundle of intermediate filaments (arrows) that characterizes astrocytes. Arrowheads indicate gold particles in the nucleus. Scale bar = 1 µm. Abbreviations: subventricular zone: (SVZ); 3′, 3′-diaminobenzidine: (DAB).
    Figure Legend Snippet: Ultra-structural analysis of Sox-2 expression. A. Sox-2 immuno-gold label is observed in the nucleus (arrowheads) in ependymal cells and astrocytes in ultra-thin sections of the SVZ. Boxed areas show an ependymal cell (E) and an astrocyte (As). Ependymal layer (EL), gap layer (HL), astrocyte ribbon layer (R). Scale bar = 20 um; Scale bar in boxed areas = 1 um. a1. Magnification shows a Sox-2 + astrocyte and lack of immunoreactivity in an oligodendrocyte (O) and a microglial cell (Mi). Astrocytes are recognized by the presence of dense bundles of intermediate filaments (arrows). Scale bar = 2 um. B. Sox-2 immuno-gold staining in a group of neuroblasts (type A cells). Scale bar = 20 um. b1. Magnification of three neuroblasts showing the nuclear staining. Neuroblasts form chain-like structures with characteristic intercellular spaces (arrows). Scale bar = 2 um. C. Light microscopy image of a semi-thin section showing the distribution and characterization of cells expressing Sox-2 in the dentate gyrus. Sox-2 + cells are visualized by the nuclear dark brown DAB precipitate. The section was counterstained with toluidine blue. The line marks the boundary between the granular layer (GrL) and the hilus (H) where most labeled cells were located. Scale bar = 100 um. c1 ) Neurons in the granular layer were not Sox-2 + . Scale bar = 10 um; Insert = 1 um. D. Microphotograph of a striatal field of a control monkey showing a Sox-2 + astrocyte and unlabeled neuron (Neu) and microglial cells (Mi). Scale bar = 5 um. d1. Boxed area of the astrocyte (As) nucleus shows the gold particles (arrowheads). Scale bar = 1 um. E. A representative Sox-2 + neuron in the striatum of a control monkey. Scale bar = 2 um. e1. Boxed area shows deposition of gold particles over the nucleus (arrowheads) close to a synapse (arrow), which identifies this cell as a neuron. Scale bar = 1 um. F. Sox-2 + astrocyte in the substantia nigra pars compacta. Scale bar = 10 µm. f1. Boxed area shows a dense bundle of intermediate filaments (arrows) that characterizes astrocytes. Arrowheads indicate gold particles in the nucleus. Scale bar = 1 µm. Abbreviations: subventricular zone: (SVZ); 3′, 3′-diaminobenzidine: (DAB).

    Techniques Used: Expressing, Staining, Light Microscopy, Labeling

    3) Product Images from "Biochemical Characterization and Functional Studies of Acanthamoeba Mannose-Binding Protein "

    Article Title: Biochemical Characterization and Functional Studies of Acanthamoeba Mannose-Binding Protein

    Journal: Infection and Immunity

    doi: 10.1128/IAI.73.9.5775-5781.2005

    Polyclonal anti-MBP IgY inhibits (i) adhesion of Acanthamoeba to Man-BSA and to epithelial cells and (ii) amoeba-induced cytopathic effect. Wells of microtiter plates coated with Man-BSA (A) or monolayer cultures of epithelial cells (B) were incubated with 35 S-labeled amoebae that had been pretreated with medium alone (Media), anti-MBP IgY (Anti-MBP), preimmune IgY (PI), or 100 mM α-Man. After being washed with PBS, the numbers of bound parasites were estimated as the radioactivity recovered from the wells. The means plus standard deviations of three experiments are shown ( n = 12 for each group). (C) Anti- Acanthamoeba MBP inhibits amoeba-induced CPE. Epithelial cells were cultured to confluence on 96-well plates and then incubated for 18 h with acanthamoebae that had been preincubated with either anti-MBP IgY, preimmune IgY, or 100 mM α-Man. After being washed, the cells were fixed, stained with Giemsa, and photographed (left). The approximate cell density in each well was estimated by using the Plot Density tool of Quantity One software (Bio-Rad, Hercules, CA). Clear, unstained regions indicate loss of cells (i and iii). Dark, stained areas indicate the presence of cells (ii and iv). Note that the amoeba-induced CPE of host cells was completely inhibited when the assays were performed using anti-MBP IgY-treated parasites (ii). Similar results were obtained regardless of whether the experiments were performed with rabbit corneal epithelial cells or Caco-2 cells.
    Figure Legend Snippet: Polyclonal anti-MBP IgY inhibits (i) adhesion of Acanthamoeba to Man-BSA and to epithelial cells and (ii) amoeba-induced cytopathic effect. Wells of microtiter plates coated with Man-BSA (A) or monolayer cultures of epithelial cells (B) were incubated with 35 S-labeled amoebae that had been pretreated with medium alone (Media), anti-MBP IgY (Anti-MBP), preimmune IgY (PI), or 100 mM α-Man. After being washed with PBS, the numbers of bound parasites were estimated as the radioactivity recovered from the wells. The means plus standard deviations of three experiments are shown ( n = 12 for each group). (C) Anti- Acanthamoeba MBP inhibits amoeba-induced CPE. Epithelial cells were cultured to confluence on 96-well plates and then incubated for 18 h with acanthamoebae that had been preincubated with either anti-MBP IgY, preimmune IgY, or 100 mM α-Man. After being washed, the cells were fixed, stained with Giemsa, and photographed (left). The approximate cell density in each well was estimated by using the Plot Density tool of Quantity One software (Bio-Rad, Hercules, CA). Clear, unstained regions indicate loss of cells (i and iii). Dark, stained areas indicate the presence of cells (ii and iv). Note that the amoeba-induced CPE of host cells was completely inhibited when the assays were performed using anti-MBP IgY-treated parasites (ii). Similar results were obtained regardless of whether the experiments were performed with rabbit corneal epithelial cells or Caco-2 cells.

    Techniques Used: Incubation, Labeling, Radioactivity, Cell Culture, Staining, Software

    4) Product Images from "Expression of orexin A and its receptor 1 in the human prostate"

    Article Title: Expression of orexin A and its receptor 1 in the human prostate

    Journal: Journal of Anatomy

    doi: 10.1111/joa.12030

    OXA- (A and B) and OX1R- (C and D) immunoreactivity in the human normal prostate. (A) Positive cells scattered along the monolayered epithelium of a prostatic follicle. (B) The majority of positive cells visible in this micrograph contain differently stained granular material in the apical portion of their cytoplasm. (C and D) Positive cells lined along the stratified epithelium of three follicles. Some of them are elongated in shape and completely filled with clusters of immunoreactive granules. Avidin–biotin immunohistochemical method. Scale bars: 20 μm.
    Figure Legend Snippet: OXA- (A and B) and OX1R- (C and D) immunoreactivity in the human normal prostate. (A) Positive cells scattered along the monolayered epithelium of a prostatic follicle. (B) The majority of positive cells visible in this micrograph contain differently stained granular material in the apical portion of their cytoplasm. (C and D) Positive cells lined along the stratified epithelium of three follicles. Some of them are elongated in shape and completely filled with clusters of immunoreactive granules. Avidin–biotin immunohistochemical method. Scale bars: 20 μm.

    Techniques Used: Staining, Avidin-Biotin Assay, Immunohistochemistry

    OXA- (A and B) and OX1R- (C and D) immunoreactivity in the human hyperplastic prostate. (A) The basal membrane of an intrafollicular, papillar-like structure is lined by a continuous row of intensely stained cells. (B) A peculiarity often shown by positive basal cells is the presence of a slender cytoplasmic extension (arrows) directed towards the follicular lumen and intermingled between the negative apical cells. (C) Almost all basal cells of the follicular epithelium contain OX1R-immunoreactive material, which completely fills their cytoplasm. (D) Invagination of a prostatic follicle completely lined by positive basal cells. The arrow points to a small cluster of low intensely stained apical cells close in contact with the follicular fluid. Avidin–biotin immunohistochemical method. Scale bars: 20 μm.
    Figure Legend Snippet: OXA- (A and B) and OX1R- (C and D) immunoreactivity in the human hyperplastic prostate. (A) The basal membrane of an intrafollicular, papillar-like structure is lined by a continuous row of intensely stained cells. (B) A peculiarity often shown by positive basal cells is the presence of a slender cytoplasmic extension (arrows) directed towards the follicular lumen and intermingled between the negative apical cells. (C) Almost all basal cells of the follicular epithelium contain OX1R-immunoreactive material, which completely fills their cytoplasm. (D) Invagination of a prostatic follicle completely lined by positive basal cells. The arrow points to a small cluster of low intensely stained apical cells close in contact with the follicular fluid. Avidin–biotin immunohistochemical method. Scale bars: 20 μm.

    Techniques Used: Staining, Avidin-Biotin Assay, Immunohistochemistry

    5) Product Images from "Establishment of Monoclonal Anti-Retroviral gp70 Autoantibodies from MRL/lpr Lupus Mice and Induction of Glomerular gp70 Deposition and Pathology by Transfer into Non-Autoimmune Mice"

    Article Title: Establishment of Monoclonal Anti-Retroviral gp70 Autoantibodies from MRL/lpr Lupus Mice and Induction of Glomerular gp70 Deposition and Pathology by Transfer into Non-Autoimmune Mice

    Journal: Journal of Virology

    doi:

    Differences in serum gp70 expression and glomerular pathology induced after injection of purified 12H5.1 IgG3 in NZW, (BALB/c × MRL/+)F 1 , and B6 mice. (a) Results of Western blotting assays showing the expression of serum gp70 in three different strains of mice. Sera were diluted 1:20 into SDS sample buffer without a reducing reagent and boiled for 5 min; 10 μl of each boiled mixture was loaded into a well of 7.5% polyacrylamide gel. Plasma from a 4 month-old female MRL/ lpr ), NZW mice expressed a high level of serum gp85 (gp70 plus p15E), gp70, and a degradation product gp45 (arrowheads), while their expression in B6 mice was low. (BALB/c × MRL/+)F 1 mice (F 1 ) expressed an intermediate level of serum gp70. Mr, biotinylated markers, with positions indicated in kilodaltons at the left. (b to d) Representative photomicrographs taken from kidney sections of NZW (b), (BALB/c × MRL/+)F 1 (c), and B6 (d) mice injected with purified anti-gp70 IgG3, 12H5.1; hematoxylin and eosin staining, ×300. Note apparent thickening of the capillary walls (arrowheads) and inflammatory cell infiltration (arrow) in panel b and marked increase in glomerular cellularity and evident neutrophilic infiltration in panel c.
    Figure Legend Snippet: Differences in serum gp70 expression and glomerular pathology induced after injection of purified 12H5.1 IgG3 in NZW, (BALB/c × MRL/+)F 1 , and B6 mice. (a) Results of Western blotting assays showing the expression of serum gp70 in three different strains of mice. Sera were diluted 1:20 into SDS sample buffer without a reducing reagent and boiled for 5 min; 10 μl of each boiled mixture was loaded into a well of 7.5% polyacrylamide gel. Plasma from a 4 month-old female MRL/ lpr ), NZW mice expressed a high level of serum gp85 (gp70 plus p15E), gp70, and a degradation product gp45 (arrowheads), while their expression in B6 mice was low. (BALB/c × MRL/+)F 1 mice (F 1 ) expressed an intermediate level of serum gp70. Mr, biotinylated markers, with positions indicated in kilodaltons at the left. (b to d) Representative photomicrographs taken from kidney sections of NZW (b), (BALB/c × MRL/+)F 1 (c), and B6 (d) mice injected with purified anti-gp70 IgG3, 12H5.1; hematoxylin and eosin staining, ×300. Note apparent thickening of the capillary walls (arrowheads) and inflammatory cell infiltration (arrow) in panel b and marked increase in glomerular cellularity and evident neutrophilic infiltration in panel c.

    Techniques Used: Expressing, Injection, Purification, Mouse Assay, Western Blot, Staining

    Representative kidney pathology of hybridoma-transplanted mice. (a) (BALB/c × MRL/+)F 1 mouse transplanted with 8.653 fusion partner cells. PAS staining, ×70. (b) (BALB/c × MRL/+)F 1 mouse transplanted with hybridoma cells 12H5.1. PAS staining, ×70. Note the extreme expansion of the glomeruli compared to those in panel a, which shows normal glomeruli at the same magnification. Sizes of tubules and of the nuclei of tubular epithelial cells are not different in panels a and b, but glomeruli are markedly enlarged in panel b. Granular deposition of fibrin in the affected glomeruli was also shown when phosphotungstenic acid-hematoxylin staining was applied (not shown). (c) Immunofluorescence staining with FITC-conjugated anti-mouse IgG of a fresh-frozen section taken from a representative (BALB/c × MRL/+)F 1 mouse transplanted with hybridoma cells 12H5.1. Use of FITC-conjugated anti-mouse C3 resulted in a similar pattern of staining. (d) Electron micrograph showing an affected glomerulus of a representative (BALB/c × MRL/+)F 1 ) was biotinylated to detect the presence of xenotropic viral env gene products. (g) (BALB/c × MRL/+)F 1 mouse transplanted with hybridoma cells 37C4.1 showing typical wire loop lesions. PAS staining, ×175. (h) Electron micrograph of the kidney from a (BALB/c × MRL/+)F 1 mouse transplanted with hybridoma cells 37C4.1. Bar = 2 μm. Note the dense subendothelial deposits consistent with light microscopic wire loops along the basement membrane. (i) SCID mouse transplanted with hybridoma cells 37C4.1. PAS staining, ×140. (j) Dense linear deposition of mouse C3 in a representative glomerulus from a SCID mouse transplanted with hybridoma 37C4.1. Similar deposition of mouse IgG and xenotropic viral gp70 in the affected glomeruli was also demonstrated in fresh-frozen sections of the transplanted SCID mice. (k and l) (BALB/c × MRL/+)F 1 mice transplanted with one clone of hybridomas 51D1.1 and 59C4.1, respectively. PAS staining, ×140. Note PAS-positive deposition and expansion of the mesangial areas in panel k and cell proliferation (arrowheads) and occlusive changes (arrow) of capillaries in panel l. Lesions similar to those in panel l were observed in the mice transplanted with hybridoma 60A5.1 (not shown).
    Figure Legend Snippet: Representative kidney pathology of hybridoma-transplanted mice. (a) (BALB/c × MRL/+)F 1 mouse transplanted with 8.653 fusion partner cells. PAS staining, ×70. (b) (BALB/c × MRL/+)F 1 mouse transplanted with hybridoma cells 12H5.1. PAS staining, ×70. Note the extreme expansion of the glomeruli compared to those in panel a, which shows normal glomeruli at the same magnification. Sizes of tubules and of the nuclei of tubular epithelial cells are not different in panels a and b, but glomeruli are markedly enlarged in panel b. Granular deposition of fibrin in the affected glomeruli was also shown when phosphotungstenic acid-hematoxylin staining was applied (not shown). (c) Immunofluorescence staining with FITC-conjugated anti-mouse IgG of a fresh-frozen section taken from a representative (BALB/c × MRL/+)F 1 mouse transplanted with hybridoma cells 12H5.1. Use of FITC-conjugated anti-mouse C3 resulted in a similar pattern of staining. (d) Electron micrograph showing an affected glomerulus of a representative (BALB/c × MRL/+)F 1 ) was biotinylated to detect the presence of xenotropic viral env gene products. (g) (BALB/c × MRL/+)F 1 mouse transplanted with hybridoma cells 37C4.1 showing typical wire loop lesions. PAS staining, ×175. (h) Electron micrograph of the kidney from a (BALB/c × MRL/+)F 1 mouse transplanted with hybridoma cells 37C4.1. Bar = 2 μm. Note the dense subendothelial deposits consistent with light microscopic wire loops along the basement membrane. (i) SCID mouse transplanted with hybridoma cells 37C4.1. PAS staining, ×140. (j) Dense linear deposition of mouse C3 in a representative glomerulus from a SCID mouse transplanted with hybridoma 37C4.1. Similar deposition of mouse IgG and xenotropic viral gp70 in the affected glomeruli was also demonstrated in fresh-frozen sections of the transplanted SCID mice. (k and l) (BALB/c × MRL/+)F 1 mice transplanted with one clone of hybridomas 51D1.1 and 59C4.1, respectively. PAS staining, ×140. Note PAS-positive deposition and expansion of the mesangial areas in panel k and cell proliferation (arrowheads) and occlusive changes (arrow) of capillaries in panel l. Lesions similar to those in panel l were observed in the mice transplanted with hybridoma 60A5.1 (not shown).

    Techniques Used: Mouse Assay, Staining, Immunofluorescence

    6) Product Images from "SARS Unique Domain (SUD) of Severe Acute Respiratory Syndrome Coronavirus Induces NLRP3 Inflammasome-Dependent CXCL10-Mediated Pulmonary Inflammation"

    Article Title: SARS Unique Domain (SUD) of Severe Acute Respiratory Syndrome Coronavirus Induces NLRP3 Inflammasome-Dependent CXCL10-Mediated Pulmonary Inflammation

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms21093179

    Histopathological changes in the lung tissues of the wild type mice intratracheally instilled with pSUD-FL, pSUD-NM, and pSUD-MC. The sections of the lung tissues from the instilled mice were performed using immunohistochemistry staining with anti-SARS-CoV SUD (( A ), first and second rows), or anti-mouse CD11b (( A ), third and fourth rows), and biotinylated universal antibodies from a VECTASTAIN ® Elite ® ABC Universal Kit ( A ). The sections were also assessed with H E staining, which the wide range of lung tissues was observed by a light microscope at 40× and 200× magnification (( B ), first and second rows); inflammatory cells infiltrated around the peribranchial and perivascular, and cell accumulation in alveolar space were examined using a light microscope at 400× magnification (( B ), third and fourth rows). The indices of histopathological changes in aggregation ( C ), perivascular cuffing ( D ), inflammation ( E ), and pathological index ( F ) were scored based on the degree of lesions ranged from one to five depending on severity: 1 = minimal (
    Figure Legend Snippet: Histopathological changes in the lung tissues of the wild type mice intratracheally instilled with pSUD-FL, pSUD-NM, and pSUD-MC. The sections of the lung tissues from the instilled mice were performed using immunohistochemistry staining with anti-SARS-CoV SUD (( A ), first and second rows), or anti-mouse CD11b (( A ), third and fourth rows), and biotinylated universal antibodies from a VECTASTAIN ® Elite ® ABC Universal Kit ( A ). The sections were also assessed with H E staining, which the wide range of lung tissues was observed by a light microscope at 40× and 200× magnification (( B ), first and second rows); inflammatory cells infiltrated around the peribranchial and perivascular, and cell accumulation in alveolar space were examined using a light microscope at 400× magnification (( B ), third and fourth rows). The indices of histopathological changes in aggregation ( C ), perivascular cuffing ( D ), inflammation ( E ), and pathological index ( F ) were scored based on the degree of lesions ranged from one to five depending on severity: 1 = minimal (

    Techniques Used: Mouse Assay, Immunohistochemistry, Staining, Light Microscopy

    7) Product Images from "Apolipoprotein E Inhibits Neointimal Hyperplasia after Arterial Injury in Mice"

    Article Title: Apolipoprotein E Inhibits Neointimal Hyperplasia after Arterial Injury in Mice

    Journal: The American Journal of Pathology

    doi:

    Von Willebrand Factor immunohistochemical staining of control ( a ) and injured ( b ) carotid arteries. Paraffin sections were obtained from a C57BL/6 mouse 1 hour after mechanically induced injury of the left carotid artery. The sections were incubated with a polyclonal antibody against Von Willebrand Factor at a dilution of 1:100. Immunoreactivity was detected by incubation with 0.5% biotinylated anti-rabbit IgG, followed by incubation with avidin-peroxidase complex and visualized with 3,3′-diaminobenzidine. Scale bar, 50 μm.
    Figure Legend Snippet: Von Willebrand Factor immunohistochemical staining of control ( a ) and injured ( b ) carotid arteries. Paraffin sections were obtained from a C57BL/6 mouse 1 hour after mechanically induced injury of the left carotid artery. The sections were incubated with a polyclonal antibody against Von Willebrand Factor at a dilution of 1:100. Immunoreactivity was detected by incubation with 0.5% biotinylated anti-rabbit IgG, followed by incubation with avidin-peroxidase complex and visualized with 3,3′-diaminobenzidine. Scale bar, 50 μm.

    Techniques Used: Immunohistochemistry, Staining, Incubation, Avidin-Biotin Assay

    Immunohistochemical staining of smooth muscle α-actin in control ( a ) and injured carotid arteries ( b ) of an apoE(−/−) mouse. Paraffin sections were obtained 14 days after mechanically induced injury of the mouse carotid artery. The sections were incubated with a monoclonal antibody against α-smooth muscle cell α-actin at a dilution of 1:3,000. Immunoreactivity was detected by incubation with 0.5% biotinylated anti-mouse IgG, followed by incubation with avidin-peroxidase complex and visualized with 3,3′-diaminobenzidine. Scale bar, 50 μm.
    Figure Legend Snippet: Immunohistochemical staining of smooth muscle α-actin in control ( a ) and injured carotid arteries ( b ) of an apoE(−/−) mouse. Paraffin sections were obtained 14 days after mechanically induced injury of the mouse carotid artery. The sections were incubated with a monoclonal antibody against α-smooth muscle cell α-actin at a dilution of 1:3,000. Immunoreactivity was detected by incubation with 0.5% biotinylated anti-mouse IgG, followed by incubation with avidin-peroxidase complex and visualized with 3,3′-diaminobenzidine. Scale bar, 50 μm.

    Techniques Used: Immunohistochemistry, Staining, Incubation, Avidin-Biotin Assay

    8) Product Images from "Depletion of CD8+ T cells enhances airway remodelling in a rodent model of asthma"

    Article Title: Depletion of CD8+ T cells enhances airway remodelling in a rodent model of asthma

    Journal: Immunology

    doi: 10.1111/j.1365-2567.2008.02876.x

    Histological sections of airways from rats chronically challenged with phosphate-buffered saline (PBS), treated with control ascites (PBS/Cont group), rats chronically challenged with ovalbumin (OVA), treated with control ascites (OVA/Cont group) and rats chronically challenged with OVA, treated with OX-8 monoclonal antibody (OVA/OX-8 group). Periodic acid–Schiff staining for the detection of mucus-containing cells (a–c), proliferating cell nuclear antigen immunohistochemistry for the detection of proliferating epithelial cells (d–f), and α-smooth muscle actin immunohistochemistry for the detection of airway smooth muscle (g–i) in rat airways.
    Figure Legend Snippet: Histological sections of airways from rats chronically challenged with phosphate-buffered saline (PBS), treated with control ascites (PBS/Cont group), rats chronically challenged with ovalbumin (OVA), treated with control ascites (OVA/Cont group) and rats chronically challenged with OVA, treated with OX-8 monoclonal antibody (OVA/OX-8 group). Periodic acid–Schiff staining for the detection of mucus-containing cells (a–c), proliferating cell nuclear antigen immunohistochemistry for the detection of proliferating epithelial cells (d–f), and α-smooth muscle actin immunohistochemistry for the detection of airway smooth muscle (g–i) in rat airways.

    Techniques Used: Staining, Immunohistochemistry

    Morphometric quantification of proliferating cell nuclear antigen (PCNA)-positive proliferating epithelial cells by PCNA immunohistochemistry. The number of positive cells per unit length of the basement membrane perimeter ( P BM ) in small ( P BM
    Figure Legend Snippet: Morphometric quantification of proliferating cell nuclear antigen (PCNA)-positive proliferating epithelial cells by PCNA immunohistochemistry. The number of positive cells per unit length of the basement membrane perimeter ( P BM ) in small ( P BM

    Techniques Used: Immunohistochemistry

    9) Product Images from "Heparan Sulfate Proteoglycan Is an Important Attachment Factor for Cell Entry of Akabane and Schmallenberg Viruses"

    Article Title: Heparan Sulfate Proteoglycan Is an Important Attachment Factor for Cell Entry of Akabane and Schmallenberg Viruses

    Journal: Journal of Virology

    doi: 10.1128/JVI.00503-17

    AKAV and SBV binding assays in HSPG-KO cells. (A) Real-time RT-PCR for the quantification of cell surface-attached viruses. AKAV(OBE-1) or SBV was incubated with HSPG-KO cells at 4°C. After a washing step, total RNAs were extracted. AKAV or SBV S RNAs were quantified by one-step real-time RT-PCR. For relative quantification, standard curves of AKAV or SBV S RNA and GAPDH were prepared by serial dilution of a mixture of total RNA from uninfected HmLu-1 cells and RNA extracted from AKAV(OBE-1) or SBV-containing supernatants. Results are expressed as the percentages relative to the levels in random-KO cells. The results are representative of three different experiments. (B) Sandwich ELISA for the detection of N proteins of AKAV attached to cell surfaces. AKAV(OBE-1) was inoculated onto HSPG-KO or random-KO HmLu-1 cells and left for 1 h at 4°C. After a washing step, the cells were lysed, and the lysates were added to the anti-AKAV N monoclonal antibody (5E8)-coated wells of 96-well ELISA plates (Maxisorp, Nunc), followed by incubation with biotinylated anti-AKAV mouse polyclonal antibody. Subsequently, the wells were incubated with avidin-biotinylated horseradish peroxidase (HRP) complex (Vectastain ABC kit; Vector Laboratories). A 3,3′,5,5′-tetramethylbenzidine (TMB) substrate solution was used for detection, and optical density values were measured. Results are expressed as percentages relative to the number of positive random-KO cells. The results are representative of three independent experiments.
    Figure Legend Snippet: AKAV and SBV binding assays in HSPG-KO cells. (A) Real-time RT-PCR for the quantification of cell surface-attached viruses. AKAV(OBE-1) or SBV was incubated with HSPG-KO cells at 4°C. After a washing step, total RNAs were extracted. AKAV or SBV S RNAs were quantified by one-step real-time RT-PCR. For relative quantification, standard curves of AKAV or SBV S RNA and GAPDH were prepared by serial dilution of a mixture of total RNA from uninfected HmLu-1 cells and RNA extracted from AKAV(OBE-1) or SBV-containing supernatants. Results are expressed as the percentages relative to the levels in random-KO cells. The results are representative of three different experiments. (B) Sandwich ELISA for the detection of N proteins of AKAV attached to cell surfaces. AKAV(OBE-1) was inoculated onto HSPG-KO or random-KO HmLu-1 cells and left for 1 h at 4°C. After a washing step, the cells were lysed, and the lysates were added to the anti-AKAV N monoclonal antibody (5E8)-coated wells of 96-well ELISA plates (Maxisorp, Nunc), followed by incubation with biotinylated anti-AKAV mouse polyclonal antibody. Subsequently, the wells were incubated with avidin-biotinylated horseradish peroxidase (HRP) complex (Vectastain ABC kit; Vector Laboratories). A 3,3′,5,5′-tetramethylbenzidine (TMB) substrate solution was used for detection, and optical density values were measured. Results are expressed as percentages relative to the number of positive random-KO cells. The results are representative of three independent experiments.

    Techniques Used: Binding Assay, Quantitative RT-PCR, Incubation, Serial Dilution, Sandwich ELISA, Enzyme-linked Immunosorbent Assay, Avidin-Biotin Assay, Plasmid Preparation

    10) Product Images from "Calretinin and calbindin architecture of the midline thalamus associated with prefrontal-hippocampal circuitry"

    Article Title: Calretinin and calbindin architecture of the midline thalamus associated with prefrontal-hippocampal circuitry

    Journal: bioRxiv

    doi: 10.1101/2020.07.21.214973

    Distribution of DAB CR + and DAB CB + cells is not the same across all RE internal subdivisions A: Brightfield images showing the distribution of DAB CR + cells in RE across the rostro-caudal axis of the thalamus. CR + cell area density varied depending on the subdivision of RE in which they were located. B: Distribution of DAB CB + cells. When compared, CR + and CB + cell distribution in all RE’s subregions and across the rostral to caudal levels did not appear to be the same. Overlay shown adapted from Swanson (2018) to highlight all RE internal subdivisions. Scale bar = 100μm. C: Comparison of DAB CR + and DAB CB + cell area density (cells/0.01mm 2 ) in all subdivisions of RE across the rostro-caudal axis. CB + cell densities were higher than CR + cell densities (except REm). Additionally, REl, REv and REcd subdivisions exhibited large CB + cell densities compared to other RE subregions. A moderate size effect was found for CB + cell area density across all levels and RE subdivisions (Hedges’ d=0.32). Abbreviations: β, bregma; CB, calbindin; CR, calretinin; DAB, 3,3’-Diaminobenzidine; PRe, perireuniens, RE, nucleus reuniens of the thalamus, REa, reuniens rostral division anterior part; REd, reuniens rostral division dorsal part; REl, reuniens rostral division lateral part; REm, reuniens rostral division median part; REv, reuniens rostral division ventral part; REcm, reuniens caudal division median part; REcd, reuniens caudal division dorsal part; REcp, reuniens caudal division posterior part.
    Figure Legend Snippet: Distribution of DAB CR + and DAB CB + cells is not the same across all RE internal subdivisions A: Brightfield images showing the distribution of DAB CR + cells in RE across the rostro-caudal axis of the thalamus. CR + cell area density varied depending on the subdivision of RE in which they were located. B: Distribution of DAB CB + cells. When compared, CR + and CB + cell distribution in all RE’s subregions and across the rostral to caudal levels did not appear to be the same. Overlay shown adapted from Swanson (2018) to highlight all RE internal subdivisions. Scale bar = 100μm. C: Comparison of DAB CR + and DAB CB + cell area density (cells/0.01mm 2 ) in all subdivisions of RE across the rostro-caudal axis. CB + cell densities were higher than CR + cell densities (except REm). Additionally, REl, REv and REcd subdivisions exhibited large CB + cell densities compared to other RE subregions. A moderate size effect was found for CB + cell area density across all levels and RE subdivisions (Hedges’ d=0.32). Abbreviations: β, bregma; CB, calbindin; CR, calretinin; DAB, 3,3’-Diaminobenzidine; PRe, perireuniens, RE, nucleus reuniens of the thalamus, REa, reuniens rostral division anterior part; REd, reuniens rostral division dorsal part; REl, reuniens rostral division lateral part; REm, reuniens rostral division median part; REv, reuniens rostral division ventral part; REcm, reuniens caudal division median part; REcd, reuniens caudal division dorsal part; REcp, reuniens caudal division posterior part.

    Techniques Used:

    11) Product Images from "Organotypic vibrosections: Novel whole sagittal brain cultures"

    Article Title: Organotypic vibrosections: Novel whole sagittal brain cultures

    Journal: Journal of Neuroscience Methods

    doi: 10.1016/j.jneumeth.2011.07.021

    Mini-Ruby neurotracing (red) of 2-week old vibrosections. Mini-Ruby was applied (*) either onto the striatum (A–C), or the cortex (D) or the ventral mesencephalon (vMes, E–H) and slices were analyzed after 3 h. (A) shows a co-staining of Mini-Ruby labelled cells in the striatum (red) and TH+ neurons in the vMes (green). (B) shows Mini-Ruby positive striatal nerve fibers growing caudal. (C) shows a large Mini-Ruby positive cortico-striatal neuron (arrows) and (D) shows a large Mini-Ruby labelled cortico-hippocampal neuron (arrows). (E)–(H) show mesencephalic Mini-Ruby positive cells and nerve fibers (E). The box in E shows co-localization of Mini-Ruby with tyrosine hydroxylase (TH) (see F–H). Note a TH+ nerve fiber (F, green, arrow), which co-localizes (H) with a Mini-Ruby labelled nerve fiber (G, red). Scale bar in A = 1170 μm (A), 290 μm (B), 185 μm (C), 160 μm (D), 200 μm (E–H).
    Figure Legend Snippet: Mini-Ruby neurotracing (red) of 2-week old vibrosections. Mini-Ruby was applied (*) either onto the striatum (A–C), or the cortex (D) or the ventral mesencephalon (vMes, E–H) and slices were analyzed after 3 h. (A) shows a co-staining of Mini-Ruby labelled cells in the striatum (red) and TH+ neurons in the vMes (green). (B) shows Mini-Ruby positive striatal nerve fibers growing caudal. (C) shows a large Mini-Ruby positive cortico-striatal neuron (arrows) and (D) shows a large Mini-Ruby labelled cortico-hippocampal neuron (arrows). (E)–(H) show mesencephalic Mini-Ruby positive cells and nerve fibers (E). The box in E shows co-localization of Mini-Ruby with tyrosine hydroxylase (TH) (see F–H). Note a TH+ nerve fiber (F, green, arrow), which co-localizes (H) with a Mini-Ruby labelled nerve fiber (G, red). Scale bar in A = 1170 μm (A), 290 μm (B), 185 μm (C), 160 μm (D), 200 μm (E–H).

    Techniques Used: Staining

    Schematic of the preparation of whole brain sagittal organotypic vibrosections. Postnatal day 8 rats were dissected sagittally (A) and fixed at the vibratome close to a razor knife (B). A semipermeable 0.4 μm pore membrane was prepared (C, arrow) and a sectioned organotypic vibrosection was carefully placed on this membrane and put into a semipermeable membrane insert (D), and incubated in a 6-well plate at 37 °C and 5% CO 2 (E). (F) shows a cresyl violet stained overview of a whole sagittal brain organotypic vibrosection cultured for 2 weeks. Scale bar = 2600 μm.
    Figure Legend Snippet: Schematic of the preparation of whole brain sagittal organotypic vibrosections. Postnatal day 8 rats were dissected sagittally (A) and fixed at the vibratome close to a razor knife (B). A semipermeable 0.4 μm pore membrane was prepared (C, arrow) and a sectioned organotypic vibrosection was carefully placed on this membrane and put into a semipermeable membrane insert (D), and incubated in a 6-well plate at 37 °C and 5% CO 2 (E). (F) shows a cresyl violet stained overview of a whole sagittal brain organotypic vibrosection cultured for 2 weeks. Scale bar = 2600 μm.

    Techniques Used: Incubation, Staining, Cell Culture

    Co-localization of dopaminergic and cholinergic neurons and capillaries in organotypic sagittal vibrosections using chromogenic substrate (A and B) or fluorescence labelling (C–I). (A) shows a triple immunohistochemical staining for cholinergic neurons (DAB-nickel, black), dopaminergic neurons (SG, grey) and calbindin (VIP, violet). (B) shows TH+ nerve fibers (arrows, blue) crossing ChAT+ neurons (brown) in the basal nucleus of Meynert. (C)–(F) show co-localization of cholinergic ChAT+ neurons (arrow, C) with laminin+ capillaries (D). (G)–(I) show cytoplasmic staining of TH+ dopaminergic neurons (arrow, G). Nuclei were stained with DAPI (E, H). (F) and (I) show the merged pictures. Scale bar in (A) = 1200 μm, 30 μm (B) and 60 μm (C–I).
    Figure Legend Snippet: Co-localization of dopaminergic and cholinergic neurons and capillaries in organotypic sagittal vibrosections using chromogenic substrate (A and B) or fluorescence labelling (C–I). (A) shows a triple immunohistochemical staining for cholinergic neurons (DAB-nickel, black), dopaminergic neurons (SG, grey) and calbindin (VIP, violet). (B) shows TH+ nerve fibers (arrows, blue) crossing ChAT+ neurons (brown) in the basal nucleus of Meynert. (C)–(F) show co-localization of cholinergic ChAT+ neurons (arrow, C) with laminin+ capillaries (D). (G)–(I) show cytoplasmic staining of TH+ dopaminergic neurons (arrow, G). Nuclei were stained with DAPI (E, H). (F) and (I) show the merged pictures. Scale bar in (A) = 1200 μm, 30 μm (B) and 60 μm (C–I).

    Techniques Used: Fluorescence, Immunohistochemistry, Staining

    H 2 O 2 -induced (450 mM for 3 days) alterations in the hippocampus of organotypic sagittal vibrosections stained for DAPI (A and D), propidiumiodide (B and E; PI) and calbindin (C and F). Note enhanced PI staining and reduced calbindin staining after hydrogen peroxide. DG, dentate gyrus; CA1, pyramidal cell layer CA1. Scale bar in (F) = 500 μm.
    Figure Legend Snippet: H 2 O 2 -induced (450 mM for 3 days) alterations in the hippocampus of organotypic sagittal vibrosections stained for DAPI (A and D), propidiumiodide (B and E; PI) and calbindin (C and F). Note enhanced PI staining and reduced calbindin staining after hydrogen peroxide. DG, dentate gyrus; CA1, pyramidal cell layer CA1. Scale bar in (F) = 500 μm.

    Techniques Used: Staining

    In situ hybridization for cholinergic neurons (ChAT mRNA) in adult brains (A, B, and D) and in 2-week old organotypic vibrosections incubated with NGF (C). (A) and (C) show X-ray films exposed for 1 week, and (B) shows a dipped slide at dark-field and (D) at bright field. Note black silver grains over cresyl violet counterstained cells (D). Str, striatum; nBM, basal nucleus of Meynert. Scale bar in (A) = 2000 μm, 700 μm (B), 3000 μm (C), 85 μm (D).
    Figure Legend Snippet: In situ hybridization for cholinergic neurons (ChAT mRNA) in adult brains (A, B, and D) and in 2-week old organotypic vibrosections incubated with NGF (C). (A) and (C) show X-ray films exposed for 1 week, and (B) shows a dipped slide at dark-field and (D) at bright field. Note black silver grains over cresyl violet counterstained cells (D). Str, striatum; nBM, basal nucleus of Meynert. Scale bar in (A) = 2000 μm, 700 μm (B), 3000 μm (C), 85 μm (D).

    Techniques Used: In Situ Hybridization, Incubation

    12) Product Images from "Cannabinoid modulation of limbic forebrain noradrenergic circuitry"

    Article Title: Cannabinoid modulation of limbic forebrain noradrenergic circuitry

    Journal: The European Journal of Neuroscience

    doi: 10.1111/j.1460-9568.2009.07054.x

    Confocal fluorescence photomicrographs showing dual-labeling for CB1R and DBH in coronal sections of the nucleus accumbens (Acb, A–C) and the nucleus of the solitary tract (NTS, D) or CB1R and MAP2 in the Acb (E). CB1R was detected using a rhodamine
    Figure Legend Snippet: Confocal fluorescence photomicrographs showing dual-labeling for CB1R and DBH in coronal sections of the nucleus accumbens (Acb, A–C) and the nucleus of the solitary tract (NTS, D) or CB1R and MAP2 in the Acb (E). CB1R was detected using a rhodamine

    Techniques Used: Fluorescence, Labeling

    13) Product Images from "Cystic fibrosis remodels the regulation of purinergic signaling by NTPDase1 (CD39) and NTPDase3"

    Article Title: Cystic fibrosis remodels the regulation of purinergic signaling by NTPDase1 (CD39) and NTPDase3

    Journal: American Journal of Physiology - Lung Cellular and Molecular Physiology

    doi: 10.1152/ajplung.00019.2010

    Expression of NTPDase1 and NTPDase3 in human airway epithelia. A : both azide-sensitive NTPDases were detected at the mRNA level by RT-PCR in nasal epithelial cultures (NC), bronchial epithelial cultures (BC), nasal excised epithelia (NE), and bronchial
    Figure Legend Snippet: Expression of NTPDase1 and NTPDase3 in human airway epithelia. A : both azide-sensitive NTPDases were detected at the mRNA level by RT-PCR in nasal epithelial cultures (NC), bronchial epithelial cultures (BC), nasal excised epithelia (NE), and bronchial

    Techniques Used: Expressing, Reverse Transcription Polymerase Chain Reaction

    Impact of CF on the airway distribution of NTPDase3 dominated by mucus secretion. Immunolabeling of NTPDase3 in frozen airway tissue sections photographed at ×10 ( left ) and ×40 ( right ). NTPDase3 remains restricted to the epithelia, which
    Figure Legend Snippet: Impact of CF on the airway distribution of NTPDase3 dominated by mucus secretion. Immunolabeling of NTPDase3 in frozen airway tissue sections photographed at ×10 ( left ) and ×40 ( right ). NTPDase3 remains restricted to the epithelia, which

    Techniques Used: Immunolabeling

    Restricted distribution of NTPDase3 to epithelial cells in the airways. Immunolabeling of NTPDase3 in frozen airway tissue sections photographed at ×10 ( left ) and ×40 ( right ). Note the absence of NTPDase3 signal in the interstitium in
    Figure Legend Snippet: Restricted distribution of NTPDase3 to epithelial cells in the airways. Immunolabeling of NTPDase3 in frozen airway tissue sections photographed at ×10 ( left ) and ×40 ( right ). Note the absence of NTPDase3 signal in the interstitium in

    Techniques Used: Immunolabeling

    14) Product Images from "CD4+ T Cells Have a Permissive Effect on Enriched Environment-Induced Hippocampus Synaptic Plasticity"

    Article Title: CD4+ T Cells Have a Permissive Effect on Enriched Environment-Induced Hippocampus Synaptic Plasticity

    Journal: Frontiers in Synaptic Neuroscience

    doi: 10.3389/fnsyn.2018.00014

    CD4 + T cell depletion affects EE-induced neurogenesis in dentate gyrus of the hippocampus from SE and EE mice. (A) Chromogenic immunodetection of newborn BrdU + cells measured in the DG 24 h after BrdU injection (left) or 21 days after the first BrdU injection (right) in mice raised in SE (white) or EE (gray). Mice were treated either with the depleting anti-CD4 or the control isotype antibodies ( n = 4–6 mice per group). (B) Right Panel: confocal micrographs of the DG from control (left) or CD4 + T cell-depleted (right) mice housed in SE (top) or EE (bottom) showing the labeling of BrdU + (green) and NeuN + (red) cells. Left Panel: Histogram showing the mean number per slice (two slices labeled per hippocampus, n = 4 mice per group) of BrdU + cells and BrdU + NeuN + cells.
    Figure Legend Snippet: CD4 + T cell depletion affects EE-induced neurogenesis in dentate gyrus of the hippocampus from SE and EE mice. (A) Chromogenic immunodetection of newborn BrdU + cells measured in the DG 24 h after BrdU injection (left) or 21 days after the first BrdU injection (right) in mice raised in SE (white) or EE (gray). Mice were treated either with the depleting anti-CD4 or the control isotype antibodies ( n = 4–6 mice per group). (B) Right Panel: confocal micrographs of the DG from control (left) or CD4 + T cell-depleted (right) mice housed in SE (top) or EE (bottom) showing the labeling of BrdU + (green) and NeuN + (red) cells. Left Panel: Histogram showing the mean number per slice (two slices labeled per hippocampus, n = 4 mice per group) of BrdU + cells and BrdU + NeuN + cells.

    Techniques Used: Mouse Assay, Immunodetection, Injection, Labeling

    15) Product Images from "Differential regulation of human and murine P-selectin expression and function in vivo"

    Article Title: Differential regulation of human and murine P-selectin expression and function in vivo

    Journal: The Journal of Experimental Medicine

    doi: 10.1084/jem.20101545

    Transgenic mice express human P-selectin in endothelial cells. (A) Sections of heart or lung from TghSelp +/− or WT mice were incubated with biotinylated sheep anti–human P-selectin IgG (anti–hP-sel, which does not crossreact with murine P-selectin) or control sheep IgG, followed by a streptavidin–horseradish peroxidase complex. The slides were developed with a peroxidase substrate. Brown reaction product marks sites of antibody binding. Arrows mark endothelial cells lining venules. (B) Cultured lung endothelial cells from WT or TghSelp +/− mice were fixed, permeabilized, and stained with antibodies to P-selectin (green) and von Willebrand factor (VWF, red). Fluorescent images were visualized with a confocal microscope. Shown are representative images of cells from TghSelp +/− mice. Yellow staining indicates overlapping distribution of human P-selectin and murine VWF in the merged images. Colocalization of VWF and P-selectin fluorescence was quantified with an Imaris colocalization module. The bar graph depicts the mean ± SEM of the percentage of colocalized VWF and P-selectin pixels from three representative images of cells from WT and TghSelp +/− mice. The images in A and B are representative of at least three experiments.
    Figure Legend Snippet: Transgenic mice express human P-selectin in endothelial cells. (A) Sections of heart or lung from TghSelp +/− or WT mice were incubated with biotinylated sheep anti–human P-selectin IgG (anti–hP-sel, which does not crossreact with murine P-selectin) or control sheep IgG, followed by a streptavidin–horseradish peroxidase complex. The slides were developed with a peroxidase substrate. Brown reaction product marks sites of antibody binding. Arrows mark endothelial cells lining venules. (B) Cultured lung endothelial cells from WT or TghSelp +/− mice were fixed, permeabilized, and stained with antibodies to P-selectin (green) and von Willebrand factor (VWF, red). Fluorescent images were visualized with a confocal microscope. Shown are representative images of cells from TghSelp +/− mice. Yellow staining indicates overlapping distribution of human P-selectin and murine VWF in the merged images. Colocalization of VWF and P-selectin fluorescence was quantified with an Imaris colocalization module. The bar graph depicts the mean ± SEM of the percentage of colocalized VWF and P-selectin pixels from three representative images of cells from WT and TghSelp +/− mice. The images in A and B are representative of at least three experiments.

    Techniques Used: Transgenic Assay, Mouse Assay, Incubation, Binding Assay, Cell Culture, Staining, Microscopy, Fluorescence

    16) Product Images from "Sox-2 Positive Neural Progenitors in the Primate Striatum Undergo Dynamic Changes after Dopamine Denervation"

    Article Title: Sox-2 Positive Neural Progenitors in the Primate Striatum Undergo Dynamic Changes after Dopamine Denervation

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0066377

    Ultra-structural analysis of Sox-2 expression. A. Sox-2 immuno-gold label is observed in the nucleus (arrowheads) in ependymal cells and astrocytes in ultra-thin sections of the SVZ. Boxed areas show an ependymal cell (E) and an astrocyte (As). Ependymal layer (EL), gap layer (HL), astrocyte ribbon layer (R). Scale bar = 20 um; Scale bar in boxed areas = 1 um. a1. Magnification shows a Sox-2 + astrocyte and lack of immunoreactivity in an oligodendrocyte (O) and a microglial cell (Mi). Astrocytes are recognized by the presence of dense bundles of intermediate filaments (arrows). Scale bar = 2 um. B. Sox-2 immuno-gold staining in a group of neuroblasts (type A cells). Scale bar = 20 um. b1. Magnification of three neuroblasts showing the nuclear staining. Neuroblasts form chain-like structures with characteristic intercellular spaces (arrows). Scale bar = 2 um. C. Light microscopy image of a semi-thin section showing the distribution and characterization of cells expressing Sox-2 in the dentate gyrus. Sox-2 + cells are visualized by the nuclear dark brown DAB precipitate. The section was counterstained with toluidine blue. The line marks the boundary between the granular layer (GrL) and the hilus (H) where most labeled cells were located. Scale bar = 100 um. c1 ) Neurons in the granular layer were not Sox-2 + . Scale bar = 10 um; Insert = 1 um. D. Microphotograph of a striatal field of a control monkey showing a Sox-2 + astrocyte and unlabeled neuron (Neu) and microglial cells (Mi). Scale bar = 5 um. d1. Boxed area of the astrocyte (As) nucleus shows the gold particles (arrowheads). Scale bar = 1 um. E. A representative Sox-2 + neuron in the striatum of a control monkey. Scale bar = 2 um. e1. Boxed area shows deposition of gold particles over the nucleus (arrowheads) close to a synapse (arrow), which identifies this cell as a neuron. Scale bar = 1 um. F. Sox-2 + astrocyte in the substantia nigra pars compacta. Scale bar = 10 µm. f1. Boxed area shows a dense bundle of intermediate filaments (arrows) that characterizes astrocytes. Arrowheads indicate gold particles in the nucleus. Scale bar = 1 µm. Abbreviations: subventricular zone: (SVZ); 3′, 3′-diaminobenzidine: (DAB).
    Figure Legend Snippet: Ultra-structural analysis of Sox-2 expression. A. Sox-2 immuno-gold label is observed in the nucleus (arrowheads) in ependymal cells and astrocytes in ultra-thin sections of the SVZ. Boxed areas show an ependymal cell (E) and an astrocyte (As). Ependymal layer (EL), gap layer (HL), astrocyte ribbon layer (R). Scale bar = 20 um; Scale bar in boxed areas = 1 um. a1. Magnification shows a Sox-2 + astrocyte and lack of immunoreactivity in an oligodendrocyte (O) and a microglial cell (Mi). Astrocytes are recognized by the presence of dense bundles of intermediate filaments (arrows). Scale bar = 2 um. B. Sox-2 immuno-gold staining in a group of neuroblasts (type A cells). Scale bar = 20 um. b1. Magnification of three neuroblasts showing the nuclear staining. Neuroblasts form chain-like structures with characteristic intercellular spaces (arrows). Scale bar = 2 um. C. Light microscopy image of a semi-thin section showing the distribution and characterization of cells expressing Sox-2 in the dentate gyrus. Sox-2 + cells are visualized by the nuclear dark brown DAB precipitate. The section was counterstained with toluidine blue. The line marks the boundary between the granular layer (GrL) and the hilus (H) where most labeled cells were located. Scale bar = 100 um. c1 ) Neurons in the granular layer were not Sox-2 + . Scale bar = 10 um; Insert = 1 um. D. Microphotograph of a striatal field of a control monkey showing a Sox-2 + astrocyte and unlabeled neuron (Neu) and microglial cells (Mi). Scale bar = 5 um. d1. Boxed area of the astrocyte (As) nucleus shows the gold particles (arrowheads). Scale bar = 1 um. E. A representative Sox-2 + neuron in the striatum of a control monkey. Scale bar = 2 um. e1. Boxed area shows deposition of gold particles over the nucleus (arrowheads) close to a synapse (arrow), which identifies this cell as a neuron. Scale bar = 1 um. F. Sox-2 + astrocyte in the substantia nigra pars compacta. Scale bar = 10 µm. f1. Boxed area shows a dense bundle of intermediate filaments (arrows) that characterizes astrocytes. Arrowheads indicate gold particles in the nucleus. Scale bar = 1 µm. Abbreviations: subventricular zone: (SVZ); 3′, 3′-diaminobenzidine: (DAB).

    Techniques Used: Expressing, Staining, Light Microscopy, Labeling

    17) Product Images from "Cytokine profiles of tumor supernatants in invasive ductal cancer and fibroadenoma of the breast and its relationship with VEGF-A expression in the tumors"

    Article Title: Cytokine profiles of tumor supernatants in invasive ductal cancer and fibroadenoma of the breast and its relationship with VEGF-A expression in the tumors

    Journal: International Journal of Immunopathology and Pharmacology

    doi: 10.1177/0394632016681306

    Expression of VEGF-A in breast IDC and breast FA. Expression of VEGF-A in IDC samples before (a) and after (b) incubation with polyclonal activator (PA). Expression of VEGF-A in FA samples before (c) and after (d) incubation with PA. Immunohistochemical staining with 3,3′-diaminobenzidine (DAB; brown) as a substrate and additional staining with H E (400× magnification).
    Figure Legend Snippet: Expression of VEGF-A in breast IDC and breast FA. Expression of VEGF-A in IDC samples before (a) and after (b) incubation with polyclonal activator (PA). Expression of VEGF-A in FA samples before (c) and after (d) incubation with PA. Immunohistochemical staining with 3,3′-diaminobenzidine (DAB; brown) as a substrate and additional staining with H E (400× magnification).

    Techniques Used: Expressing, Incubation, Immunohistochemistry, Staining

    18) Product Images from "Morpho-physiological Characteristics of Dorsal Subicular Network in Mice after Pilocarpine Induced Status Epilepticus"

    Article Title: Morpho-physiological Characteristics of Dorsal Subicular Network in Mice after Pilocarpine Induced Status Epilepticus

    Journal: Brain pathology (Zurich, Switzerland)

    doi: 10.1111/j.1750-3639.2009.00243.x

    PHA-L single and PHA-L with PV, CB, or CR double-labeling in Dsub of control and SE mice. A1-A 3. PHA-L labelling in control ( A1 ) and SE mice ( A2 ) shows increased number of PHA-L immunopositive en passant and terminal boutons in SE mice when compared to
    Figure Legend Snippet: PHA-L single and PHA-L with PV, CB, or CR double-labeling in Dsub of control and SE mice. A1-A 3. PHA-L labelling in control ( A1 ) and SE mice ( A2 ) shows increased number of PHA-L immunopositive en passant and terminal boutons in SE mice when compared to

    Techniques Used: Labeling, Mouse Assay

    19) Product Images from "A novel multiplex assay for simultaneous quantification of total and S129 phosphorylated human alpha-synuclein"

    Article Title: A novel multiplex assay for simultaneous quantification of total and S129 phosphorylated human alpha-synuclein

    Journal: Molecular Neurodegeneration

    doi: 10.1186/s13024-016-0125-0

    Characterization of total and phosphorylated S129 human alpha-synuclein duplex assay . The hook-point for biotinylated 4B12 antibody was determined simultaneously in a mix of Europium Acceptor-bead coupled 11A5 antibody and Terbium Acceptor-bead coupled LB509 antibody ( a ). Arrows indicate optimal 4B12 concentrations for both Acceptor-bead variants. Equivalency of the signal obtained in the total h-asyn assay was demonstrated for pS129 h-asyn and h-asyn proteins in the duplex assay in two consecutive experiments and data plotted in panel ( b ). All protein standards were spiked in naïve rat brain lysate. Lower detection limit (LDL) was 450 pg/ml and is indicated with a dashed line. Intra assay variation was calculated based on three standard curves which were measured on the same day but on separate plates for each emission signal separately ( c and d ). Inter assay variation data was calculated based on six pairs of standard curves performed on separate days ( e and f ). AU arbitrary units
    Figure Legend Snippet: Characterization of total and phosphorylated S129 human alpha-synuclein duplex assay . The hook-point for biotinylated 4B12 antibody was determined simultaneously in a mix of Europium Acceptor-bead coupled 11A5 antibody and Terbium Acceptor-bead coupled LB509 antibody ( a ). Arrows indicate optimal 4B12 concentrations for both Acceptor-bead variants. Equivalency of the signal obtained in the total h-asyn assay was demonstrated for pS129 h-asyn and h-asyn proteins in the duplex assay in two consecutive experiments and data plotted in panel ( b ). All protein standards were spiked in naïve rat brain lysate. Lower detection limit (LDL) was 450 pg/ml and is indicated with a dashed line. Intra assay variation was calculated based on three standard curves which were measured on the same day but on separate plates for each emission signal separately ( c and d ). Inter assay variation data was calculated based on six pairs of standard curves performed on separate days ( e and f ). AU arbitrary units

    Techniques Used: Intra Assay, Inter Assay

    Characterization of total human alpha-synuclein AlphaLISA. The hook-point analysis was evaluated for serial dilutions of biotinylated 4B12 in combination with Europium Acceptor-beads coupled to either LB509 (LB509-Eu) or syn211 (syn211-Eu) using a 19 ng/ml of recombinant GST-tagged h-asyn protein diluted in 10 μg/ml of Tris wild-type rat brain lysate ( a ). Arrow indicates the highest signal obtained and therefore optimal 4B12-biotin concentration to use. Standard curve was established for biotinylated 4B12 and Europium Acceptor-bead coupled LB509 by serial dilution of either GST-tagged h-asyn or mouse asyn (m-asyn) protein spiked in Tris brain lysate obtained from a naïve rat (10 μg/ml) ( b ). The lower detection limit (LDL) was 3.7 pg/ml and is indicated by a dashed line . Intra assay variation was calculated based on two standard curves which were measured on the same day but on separate plates ( c ). Inter assay variation data was calculated based on two pairs of standard curves performed on separate days ( d ). AU arbitrary units
    Figure Legend Snippet: Characterization of total human alpha-synuclein AlphaLISA. The hook-point analysis was evaluated for serial dilutions of biotinylated 4B12 in combination with Europium Acceptor-beads coupled to either LB509 (LB509-Eu) or syn211 (syn211-Eu) using a 19 ng/ml of recombinant GST-tagged h-asyn protein diluted in 10 μg/ml of Tris wild-type rat brain lysate ( a ). Arrow indicates the highest signal obtained and therefore optimal 4B12-biotin concentration to use. Standard curve was established for biotinylated 4B12 and Europium Acceptor-bead coupled LB509 by serial dilution of either GST-tagged h-asyn or mouse asyn (m-asyn) protein spiked in Tris brain lysate obtained from a naïve rat (10 μg/ml) ( b ). The lower detection limit (LDL) was 3.7 pg/ml and is indicated by a dashed line . Intra assay variation was calculated based on two standard curves which were measured on the same day but on separate plates ( c ). Inter assay variation data was calculated based on two pairs of standard curves performed on separate days ( d ). AU arbitrary units

    Techniques Used: Recombinant, Concentration Assay, Serial Dilution, Intra Assay, Inter Assay

    Evaluation of the duplex AlphaLISA performance. Assessment of the Acceptor-bead performance and comparison between Europium and Terbium based beads was carried out once for both the LB509 ( a ) and the 11A5 ( b ) antibodies. In both instances the biotinylated 4B12 antibody was used and signal to background ratio calculated against serial dilutions of h-asyn proteins spiked in naïve rat brain lysate. Presence of any hindrance of Acceptor-bead coupled antibodies against each other was assessed for LB509-Terbium ( c ) and 11A5-Europium beads ( d ). Cross-talk between the channels was assessed using the Resorufine/Amplex Red FP535 Terbium filter ( e ) and the Europium 615 filter ( f ). For these experiments the relevant analyte, Acceptor- and Donor-bead information is given under the x-axis. Both the hindrance of Acceptor-bead coupled antibodies and the channel cross talk were run twice. See Additional file 2 : Figure S2 for a theoretical explanation of the phenomena. AU arbitrary units
    Figure Legend Snippet: Evaluation of the duplex AlphaLISA performance. Assessment of the Acceptor-bead performance and comparison between Europium and Terbium based beads was carried out once for both the LB509 ( a ) and the 11A5 ( b ) antibodies. In both instances the biotinylated 4B12 antibody was used and signal to background ratio calculated against serial dilutions of h-asyn proteins spiked in naïve rat brain lysate. Presence of any hindrance of Acceptor-bead coupled antibodies against each other was assessed for LB509-Terbium ( c ) and 11A5-Europium beads ( d ). Cross-talk between the channels was assessed using the Resorufine/Amplex Red FP535 Terbium filter ( e ) and the Europium 615 filter ( f ). For these experiments the relevant analyte, Acceptor- and Donor-bead information is given under the x-axis. Both the hindrance of Acceptor-bead coupled antibodies and the channel cross talk were run twice. See Additional file 2 : Figure S2 for a theoretical explanation of the phenomena. AU arbitrary units

    Techniques Used:

    Characterization of S129 phosphorylated human alpha-synuclein specific AlphaLISA. The hook-point analysis was evaluated for biotinylated 4B12 and Europium Acceptor-bead conjugated 11A5 ( a ). Pair was tested using 14 ng/ml of pS129 h-asyn protein diluted in 10 μg/ml of Tris brain lysate obtained from an asyn knockout mouse. Arrow indicates the optimal biotinylated antibody concentration to use. Standard curve was established for biotinylated 4B12 and Europium Acceptor-bead coupled 11A5 by serial dilution of either pS129 h-asyn or S129A h-asyn protein spiked in wild-type rodent brain lysate (10 μg/ml) ( b ). The lower detection limit (LDL) was 1.1 pg/ml and is indicated by a dashed line. Intra assay variation was calculated based on two standard curves which were measured on the same day but on separate plates ( c ) while the inter assay variation was calculated based on two pairs of standard curves performed on separate days ( d ). AU arbitrary units
    Figure Legend Snippet: Characterization of S129 phosphorylated human alpha-synuclein specific AlphaLISA. The hook-point analysis was evaluated for biotinylated 4B12 and Europium Acceptor-bead conjugated 11A5 ( a ). Pair was tested using 14 ng/ml of pS129 h-asyn protein diluted in 10 μg/ml of Tris brain lysate obtained from an asyn knockout mouse. Arrow indicates the optimal biotinylated antibody concentration to use. Standard curve was established for biotinylated 4B12 and Europium Acceptor-bead coupled 11A5 by serial dilution of either pS129 h-asyn or S129A h-asyn protein spiked in wild-type rodent brain lysate (10 μg/ml) ( b ). The lower detection limit (LDL) was 1.1 pg/ml and is indicated by a dashed line. Intra assay variation was calculated based on two standard curves which were measured on the same day but on separate plates ( c ) while the inter assay variation was calculated based on two pairs of standard curves performed on separate days ( d ). AU arbitrary units

    Techniques Used: Knock-Out, Concentration Assay, Serial Dilution, Intra Assay, Inter Assay

    20) Product Images from "Hot Water Extract of Wheat Bran Attenuates White Matter Injury in a Rat Model of Vascular Dementia"

    Article Title: Hot Water Extract of Wheat Bran Attenuates White Matter Injury in a Rat Model of Vascular Dementia

    Journal: Preventive Nutrition and Food Science

    doi: 10.3746/pnf.2014.19.3.145

    Immunochemical staining of microglia for Iba1. (A) Photomicrographs of white matter sections showing immunochemical staining of microglia for Iba1 (200×): (a) sham group; (b) control group; (c) WBE-treated group; (a)–(c) depict the optic tract region (opt). (B) Quantitative analysis of Iba1-positive cells. The relative numbers of Iba1-positive cells in the opt region were determined by normalization to the number of Iba1-positive cells detected in the sham group (n=6 rats per group). * P
    Figure Legend Snippet: Immunochemical staining of microglia for Iba1. (A) Photomicrographs of white matter sections showing immunochemical staining of microglia for Iba1 (200×): (a) sham group; (b) control group; (c) WBE-treated group; (a)–(c) depict the optic tract region (opt). (B) Quantitative analysis of Iba1-positive cells. The relative numbers of Iba1-positive cells in the opt region were determined by normalization to the number of Iba1-positive cells detected in the sham group (n=6 rats per group). * P

    Techniques Used: Staining

    21) Product Images from "Loss of connexin43 in murine Sertoli cells and its effect on blood-testis barrier formation and dynamics"

    Article Title: Loss of connexin43 in murine Sertoli cells and its effect on blood-testis barrier formation and dynamics

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0198100

    Claudin-11 immunohistochemistry in adult WT and SCCx43KO -/- mice. (A) WT tubule showing a fine linear immunopositive reaction in the basal part of the seminiferous epithelium. Scale bar: 50 μm. (B) SCCx43KO -/- tubules with SCO showing an apparently increased immunoreaction and a diffuse cytoplasmic distribution pattern. Scale bar: 100 μm. (C) SCCx43KO -/- tubule containing round spermatids showing a finer staining pattern and localisation towards the BTB (arrows). Scale bar: 50 μm. (D) SCCx43KO -/- tubule with qualitative normal spermatogenesis showing the same staining pattern as adult WT mice (arrows). Scale bar: 100 μm.
    Figure Legend Snippet: Claudin-11 immunohistochemistry in adult WT and SCCx43KO -/- mice. (A) WT tubule showing a fine linear immunopositive reaction in the basal part of the seminiferous epithelium. Scale bar: 50 μm. (B) SCCx43KO -/- tubules with SCO showing an apparently increased immunoreaction and a diffuse cytoplasmic distribution pattern. Scale bar: 100 μm. (C) SCCx43KO -/- tubule containing round spermatids showing a finer staining pattern and localisation towards the BTB (arrows). Scale bar: 50 μm. (D) SCCx43KO -/- tubule with qualitative normal spermatogenesis showing the same staining pattern as adult WT mice (arrows). Scale bar: 100 μm.

    Techniques Used: Immunohistochemistry, Mouse Assay, Staining

    Claudin-11 immunohistochemistry in pre- and peripubertal WT and SCCx43KO -/- mice. (A, C, E, G, I, K) Testes of SCCx43KO -/- mice; (B, D, F, H, J, L) testes of WT mice. Postnatal development in days: Aged 2 (A and B), aged 8 (C and D), aged 12 (E and F), aged 14 (G and H), aged 16 (I and J) and aged 23 (K and L). (A and B) At the age of 2 days no claudin-11 protein is detectable in either of the genotypes. (C and D) A clear immunopositive but cytoplasmic reaction is visible at day 8 p.p. in both genotypes. (F, H, J, L) From day 12 p.p. a basal shift towards the BTB is visible in WT mice (arrows). (E (inset) G, I, K) In the seminiferous epithelium of SCCx43KO -/- mice a cytoplasmic immunolocalisation for claudin-11 is observable over the whole-time period. (E, asterisks) Only in tubules with residual spermatogenesis could an age-dependent shift of claudin-11 towards the BTB be observed. From day 12 p.p. lumen formation occurs in both genotypes. Scale bars: 100 μm. Insets are showing one representative tubule with basal localisation of claudin-11 in WT and diffuse cytoplasmic localisation in SCCx43KO -/- mice. Scale bars: 25 μm.
    Figure Legend Snippet: Claudin-11 immunohistochemistry in pre- and peripubertal WT and SCCx43KO -/- mice. (A, C, E, G, I, K) Testes of SCCx43KO -/- mice; (B, D, F, H, J, L) testes of WT mice. Postnatal development in days: Aged 2 (A and B), aged 8 (C and D), aged 12 (E and F), aged 14 (G and H), aged 16 (I and J) and aged 23 (K and L). (A and B) At the age of 2 days no claudin-11 protein is detectable in either of the genotypes. (C and D) A clear immunopositive but cytoplasmic reaction is visible at day 8 p.p. in both genotypes. (F, H, J, L) From day 12 p.p. a basal shift towards the BTB is visible in WT mice (arrows). (E (inset) G, I, K) In the seminiferous epithelium of SCCx43KO -/- mice a cytoplasmic immunolocalisation for claudin-11 is observable over the whole-time period. (E, asterisks) Only in tubules with residual spermatogenesis could an age-dependent shift of claudin-11 towards the BTB be observed. From day 12 p.p. lumen formation occurs in both genotypes. Scale bars: 100 μm. Insets are showing one representative tubule with basal localisation of claudin-11 in WT and diffuse cytoplasmic localisation in SCCx43KO -/- mice. Scale bars: 25 μm.

    Techniques Used: Immunohistochemistry, Mouse Assay

    22) Product Images from "Regulation of Neuregulin Expression in the Injured Rat Brain and Cultured Astrocytes"

    Article Title: Regulation of Neuregulin Expression in the Injured Rat Brain and Cultured Astrocytes

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.21-04-01257.2001

    Immunohistochemical localization of neuregulin and ErbB2 in the cerebrum of an 8-week-old rat. An antibody against neuregulin-β ( A–C ) or an antibody against ErbB2 ( D–F ) was used to stain paraformaldehyde-fixed thin sections. Immunolocalization of neuregulin ( A ) and ErbB2 ( D ) in the CA1 area of the hippocampus is shown. The distribution of neuregulin ( B ) and ErbB2 ( E ) in the cerebral cortex is also shown. Most neuregulin and ErbB2 immunoreactivities appear on neuronal cell surfaces. A higher magnification of immunostained sections shows the presence of neuregulin ( C ) and ErbB2 ( F ) on cortical neuronal cells. Scale bars: A,C,D,F, 50 μm; B,E, 500 μm.
    Figure Legend Snippet: Immunohistochemical localization of neuregulin and ErbB2 in the cerebrum of an 8-week-old rat. An antibody against neuregulin-β ( A–C ) or an antibody against ErbB2 ( D–F ) was used to stain paraformaldehyde-fixed thin sections. Immunolocalization of neuregulin ( A ) and ErbB2 ( D ) in the CA1 area of the hippocampus is shown. The distribution of neuregulin ( B ) and ErbB2 ( E ) in the cerebral cortex is also shown. Most neuregulin and ErbB2 immunoreactivities appear on neuronal cell surfaces. A higher magnification of immunostained sections shows the presence of neuregulin ( C ) and ErbB2 ( F ) on cortical neuronal cells. Scale bars: A,C,D,F, 50 μm; B,E, 500 μm.

    Techniques Used: Immunohistochemistry, Staining

    Immunohistochemical localization of ErbB2 and ErbB3 in the injured brain. A shows anti-ErbB2 immunoreactive cells appearing near the wound. B, D , Higher magnification images of an area adjacent to the wound stained with anti-ErbB2 and anti-ErbB3 antibodies, respectively. The immunopositive cells indicated by the arrowheads are shown at a higher magnification in the box . These immunopositive cells were not observed in the sections stained with antibodies preabsorbed with the corresponding recombinant peptides ( C, E ). In the deep layer of the injured cortex, ErbB2 ( F ) and ErbB3 ( G ) immunoreactivities were also detected. The black arrowheads shown in F and G indicate reactive astrocyte-like cells. WM , White matter. Scale bars: A , 0.5 mm; B–E (shown in E ), 50 μm; F, G, 20 μm.
    Figure Legend Snippet: Immunohistochemical localization of ErbB2 and ErbB3 in the injured brain. A shows anti-ErbB2 immunoreactive cells appearing near the wound. B, D , Higher magnification images of an area adjacent to the wound stained with anti-ErbB2 and anti-ErbB3 antibodies, respectively. The immunopositive cells indicated by the arrowheads are shown at a higher magnification in the box . These immunopositive cells were not observed in the sections stained with antibodies preabsorbed with the corresponding recombinant peptides ( C, E ). In the deep layer of the injured cortex, ErbB2 ( F ) and ErbB3 ( G ) immunoreactivities were also detected. The black arrowheads shown in F and G indicate reactive astrocyte-like cells. WM , White matter. Scale bars: A , 0.5 mm; B–E (shown in E ), 50 μm; F, G, 20 μm.

    Techniques Used: Immunohistochemistry, Staining, Recombinant

    Double-label fluorescent localization of neuregulin with GFAP, ErbB2 with GFAP, and ErbB3 with ErbB2 in an injured cortex. A , Neuregulin immunoreactivity near the injured site. B , GFAP immunoreactivity in the same section of A . C , Superimposed image of A and B . D , ErbB2 immunoreactivity near the injured site. E , GFAP immunoreactivity in the same section of D . F , Superimposed image of D and E . G , ErbB3 immunoreactivity near the injured site. H , ErbB2 immunoreactivity in the same section of G . I , Superimposed image of G and H . Scale bars, 10 μm.
    Figure Legend Snippet: Double-label fluorescent localization of neuregulin with GFAP, ErbB2 with GFAP, and ErbB3 with ErbB2 in an injured cortex. A , Neuregulin immunoreactivity near the injured site. B , GFAP immunoreactivity in the same section of A . C , Superimposed image of A and B . D , ErbB2 immunoreactivity near the injured site. E , GFAP immunoreactivity in the same section of D . F , Superimposed image of D and E . G , ErbB3 immunoreactivity near the injured site. H , ErbB2 immunoreactivity in the same section of G . I , Superimposed image of G and H . Scale bars, 10 μm.

    Techniques Used:

    23) Product Images from "Polymer Coatings of Cochlear Implant Electrode Surface – An Option for Improving Electrode-Nerve-Interface by Blocking Fibroblast Overgrowth"

    Article Title: Polymer Coatings of Cochlear Implant Electrode Surface – An Option for Improving Electrode-Nerve-Interface by Blocking Fibroblast Overgrowth

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0157710

    Representative images of DAB stained SGN adhering on polymer-coated glass plates following 48 h cultivation. Representative transmission light microscopic view of the SGN and their neuritogenesis following cultivation on ( A ) positive control (glass plates with ornithine/laminin coating alone), ( B ) PMTA, ( C ) PDMAA, ( D ) PEtOx and ( E ) negative control (glass plate without any coating). The SGN were incubated with the mouse anti-neurofilament antibody and stained with diaminobenzidine (DAB) via binding with the biotinylated anti-mouse IgG-antibody and ABC complex. Scale bars indicate 150 μm.
    Figure Legend Snippet: Representative images of DAB stained SGN adhering on polymer-coated glass plates following 48 h cultivation. Representative transmission light microscopic view of the SGN and their neuritogenesis following cultivation on ( A ) positive control (glass plates with ornithine/laminin coating alone), ( B ) PMTA, ( C ) PDMAA, ( D ) PEtOx and ( E ) negative control (glass plate without any coating). The SGN were incubated with the mouse anti-neurofilament antibody and stained with diaminobenzidine (DAB) via binding with the biotinylated anti-mouse IgG-antibody and ABC complex. Scale bars indicate 150 μm.

    Techniques Used: Staining, Transmission Assay, Positive Control, Negative Control, Incubation, Binding Assay

    24) Product Images from "Overexpression of heparan sulfate 6-O-sulfotransferase-2 in colorectal cancer"

    Article Title: Overexpression of heparan sulfate 6-O-sulfotransferase-2 in colorectal cancer

    Journal: Molecular and Clinical Oncology

    doi: 10.3892/mco.2013.151

    Kaplan-Meier curves for overall survival. Patients were divided into two groups according to their heparan sulfate 6- O -sulfotransferase-2 (HS6ST2) expression status (dotted line, HS6ST2-positive group; straight line, HS6ST2-negative group). The P-value was calculated using the log-rank test.
    Figure Legend Snippet: Kaplan-Meier curves for overall survival. Patients were divided into two groups according to their heparan sulfate 6- O -sulfotransferase-2 (HS6ST2) expression status (dotted line, HS6ST2-positive group; straight line, HS6ST2-negative group). The P-value was calculated using the log-rank test.

    Techniques Used: Expressing

    mRNA expression levels of heparan sulfate 6- O -sulfotransferase 2 ( HS6ST2 ) in 10 paired colorectal cancer (CRC) and non-cancerous colonic mucosal samples and in various cancer cell lines. (A) Signal intensities of HS6ST2 were obtained from a microarray analysis. HS6ST2 was overexpressed in CRC (gray bars) compared to the paired mucosal samples (black bars) in almost all the patients. (B) The mRNA expression levels of HS6ST2 were assessed using quantitative reverse transcription-polymerase chain reaction in a panel of 83 cancer cell lines. Pt, patient number; Rel. mRNA, normalized mRNA expression levels ( HS6ST2/GAPD × 10 6 ); GC, gastric cancer; EC, esophageal cancer; PaC, pancreatic cancer; BC, breast cancer; HCC, hepatocellular carcinoma; ProC, prostate cancer; LC, lung cancer.
    Figure Legend Snippet: mRNA expression levels of heparan sulfate 6- O -sulfotransferase 2 ( HS6ST2 ) in 10 paired colorectal cancer (CRC) and non-cancerous colonic mucosal samples and in various cancer cell lines. (A) Signal intensities of HS6ST2 were obtained from a microarray analysis. HS6ST2 was overexpressed in CRC (gray bars) compared to the paired mucosal samples (black bars) in almost all the patients. (B) The mRNA expression levels of HS6ST2 were assessed using quantitative reverse transcription-polymerase chain reaction in a panel of 83 cancer cell lines. Pt, patient number; Rel. mRNA, normalized mRNA expression levels ( HS6ST2/GAPD × 10 6 ); GC, gastric cancer; EC, esophageal cancer; PaC, pancreatic cancer; BC, breast cancer; HCC, hepatocellular carcinoma; ProC, prostate cancer; LC, lung cancer.

    Techniques Used: Expressing, Microarray, Reverse Transcription Polymerase Chain Reaction

    25) Product Images from "SAHA Suppresses Peritoneal Fibrosis in Mice"

    Article Title: SAHA Suppresses Peritoneal Fibrosis in Mice

    Journal: Peritoneal Dialysis International : Journal of the International Society for Peritoneal Dialysis

    doi: 10.3747/pdi.2013.00089

    The result of the immunohistochemical analysis for F4/80 and CD31. (A) In the CG group, a number of F4/80-positive cells were observed in thickened peritoneal compact zone. (B) These numbers were significantly decreased in the CG+SAHA group. (C) The peritoneal tissue of CG+SAHA group was incubated with normal IgG instead of F4/80 antibody as a negative control. (A–C), magnification 200×; bars indicate the thickness of the submesothelial compact zone. (D) Bar graph showing the number of F4/80–positive cells. Data are expressed as mean±SEM. (E) The number of CD31–positive vessels increased markedly in the CG group. (F) The number of CD31–positive vessels was reduced in the CG+SAHA group. (G) The peritoneal tissue of the CG+SAHA group was incubated with normal IgG instead of CD31 antibody as a negative control. (E-G), magnification 200×; bars indicate the thickness of the submesothelial compact zone. (H) Bar graph showing the number of CD31-positive vessels. Data are expressed as mean±SEM. * represents p
    Figure Legend Snippet: The result of the immunohistochemical analysis for F4/80 and CD31. (A) In the CG group, a number of F4/80-positive cells were observed in thickened peritoneal compact zone. (B) These numbers were significantly decreased in the CG+SAHA group. (C) The peritoneal tissue of CG+SAHA group was incubated with normal IgG instead of F4/80 antibody as a negative control. (A–C), magnification 200×; bars indicate the thickness of the submesothelial compact zone. (D) Bar graph showing the number of F4/80–positive cells. Data are expressed as mean±SEM. (E) The number of CD31–positive vessels increased markedly in the CG group. (F) The number of CD31–positive vessels was reduced in the CG+SAHA group. (G) The peritoneal tissue of the CG+SAHA group was incubated with normal IgG instead of CD31 antibody as a negative control. (E-G), magnification 200×; bars indicate the thickness of the submesothelial compact zone. (H) Bar graph showing the number of CD31-positive vessels. Data are expressed as mean±SEM. * represents p

    Techniques Used: Immunohistochemistry, Incubation, Negative Control

    26) Product Images from "Apolipoprotein E Inhibits Neointimal Hyperplasia after Arterial Injury in Mice"

    Article Title: Apolipoprotein E Inhibits Neointimal Hyperplasia after Arterial Injury in Mice

    Journal: The American Journal of Pathology

    doi:

    Immunohistochemical staining of smooth muscle α-actin in control ( a ) and injured carotid arteries ( b ) of an apoE(−/−) mouse. Paraffin sections were obtained 14 days after mechanically induced injury of the mouse carotid artery. The sections were incubated with a monoclonal antibody against α-smooth muscle cell α-actin at a dilution of 1:3,000. Immunoreactivity was detected by incubation with 0.5% biotinylated anti-mouse IgG, followed by incubation with avidin-peroxidase complex and visualized with 3,3′-diaminobenzidine. Scale bar, 50 μm.
    Figure Legend Snippet: Immunohistochemical staining of smooth muscle α-actin in control ( a ) and injured carotid arteries ( b ) of an apoE(−/−) mouse. Paraffin sections were obtained 14 days after mechanically induced injury of the mouse carotid artery. The sections were incubated with a monoclonal antibody against α-smooth muscle cell α-actin at a dilution of 1:3,000. Immunoreactivity was detected by incubation with 0.5% biotinylated anti-mouse IgG, followed by incubation with avidin-peroxidase complex and visualized with 3,3′-diaminobenzidine. Scale bar, 50 μm.

    Techniques Used: Immunohistochemistry, Staining, Incubation, Avidin-Biotin Assay

    27) Product Images from "Biochemical Characterization and Functional Studies of Acanthamoeba Mannose-Binding Protein "

    Article Title: Biochemical Characterization and Functional Studies of Acanthamoeba Mannose-Binding Protein

    Journal: Infection and Immunity

    doi: 10.1128/IAI.73.9.5775-5781.2005

    Acanthamoeba MBP is membrane associated. (A) Cell surface proteins of Acanthamoeba were biotinylated (Biot), and detergent extracts of biotinylated parasites were chromatographed on an α-Man affinity column. The amoeba MBP was eluted with 0.1 M α-Man and electrophoresed under denaturing or native conditions. Proteins from the gels were transferred onto a nitrocellulose paper, and the blots were developed using a freshly prepared solution of avidin-biotin-peroxidase complex. Note that under native nondenaturing conditions, a component migrating close to 440-kDa ferritin was detected, whereas under denaturing conditions, a 130-kDa component was detected. (B) Biotinylated MBP has affinity for α-Man. A sheet of nitrocellulose paper was incubated with a neoglycoprotein, Man-BSA, and blocked with BSA, and the paper was placed in a dot blot apparatus. The paper was then exposed to affinity-purified biotinylated MBP in the absence or presence of 0.1 M α-Man, α-Gal, or GalNAc, and the blot was developed using a freshly prepared solution of avidin-biotin-peroxidase complex. Note that the biotinylated component bound to Man-BSA, and this binding was inhibited by α-Man but not by other sugars.
    Figure Legend Snippet: Acanthamoeba MBP is membrane associated. (A) Cell surface proteins of Acanthamoeba were biotinylated (Biot), and detergent extracts of biotinylated parasites were chromatographed on an α-Man affinity column. The amoeba MBP was eluted with 0.1 M α-Man and electrophoresed under denaturing or native conditions. Proteins from the gels were transferred onto a nitrocellulose paper, and the blots were developed using a freshly prepared solution of avidin-biotin-peroxidase complex. Note that under native nondenaturing conditions, a component migrating close to 440-kDa ferritin was detected, whereas under denaturing conditions, a 130-kDa component was detected. (B) Biotinylated MBP has affinity for α-Man. A sheet of nitrocellulose paper was incubated with a neoglycoprotein, Man-BSA, and blocked with BSA, and the paper was placed in a dot blot apparatus. The paper was then exposed to affinity-purified biotinylated MBP in the absence or presence of 0.1 M α-Man, α-Gal, or GalNAc, and the blot was developed using a freshly prepared solution of avidin-biotin-peroxidase complex. Note that the biotinylated component bound to Man-BSA, and this binding was inhibited by α-Man but not by other sugars.

    Techniques Used: Affinity Column, Avidin-Biotin Assay, Incubation, Dot Blot, Affinity Purification, Binding Assay

    Polyclonal anti-MBP IgY inhibits (i) adhesion of Acanthamoeba to Man-BSA and to epithelial cells and (ii) amoeba-induced cytopathic effect. Wells of microtiter plates coated with Man-BSA (A) or monolayer cultures of epithelial cells (B) were incubated with 35 S-labeled amoebae that had been pretreated with medium alone (Media), anti-MBP IgY (Anti-MBP), preimmune IgY (PI), or 100 mM α-Man. After being washed with PBS, the numbers of bound parasites were estimated as the radioactivity recovered from the wells. The means plus standard deviations of three experiments are shown ( n = 12 for each group). (C) Anti- Acanthamoeba MBP inhibits amoeba-induced CPE. Epithelial cells were cultured to confluence on 96-well plates and then incubated for 18 h with acanthamoebae that had been preincubated with either anti-MBP IgY, preimmune IgY, or 100 mM α-Man. After being washed, the cells were fixed, stained with Giemsa, and photographed (left). The approximate cell density in each well was estimated by using the Plot Density tool of Quantity One software (Bio-Rad, Hercules, CA). Clear, unstained regions indicate loss of cells (i and iii). Dark, stained areas indicate the presence of cells (ii and iv). Note that the amoeba-induced CPE of host cells was completely inhibited when the assays were performed using anti-MBP IgY-treated parasites (ii). Similar results were obtained regardless of whether the experiments were performed with rabbit corneal epithelial cells or Caco-2 cells.
    Figure Legend Snippet: Polyclonal anti-MBP IgY inhibits (i) adhesion of Acanthamoeba to Man-BSA and to epithelial cells and (ii) amoeba-induced cytopathic effect. Wells of microtiter plates coated with Man-BSA (A) or monolayer cultures of epithelial cells (B) were incubated with 35 S-labeled amoebae that had been pretreated with medium alone (Media), anti-MBP IgY (Anti-MBP), preimmune IgY (PI), or 100 mM α-Man. After being washed with PBS, the numbers of bound parasites were estimated as the radioactivity recovered from the wells. The means plus standard deviations of three experiments are shown ( n = 12 for each group). (C) Anti- Acanthamoeba MBP inhibits amoeba-induced CPE. Epithelial cells were cultured to confluence on 96-well plates and then incubated for 18 h with acanthamoebae that had been preincubated with either anti-MBP IgY, preimmune IgY, or 100 mM α-Man. After being washed, the cells were fixed, stained with Giemsa, and photographed (left). The approximate cell density in each well was estimated by using the Plot Density tool of Quantity One software (Bio-Rad, Hercules, CA). Clear, unstained regions indicate loss of cells (i and iii). Dark, stained areas indicate the presence of cells (ii and iv). Note that the amoeba-induced CPE of host cells was completely inhibited when the assays were performed using anti-MBP IgY-treated parasites (ii). Similar results were obtained regardless of whether the experiments were performed with rabbit corneal epithelial cells or Caco-2 cells.

    Techniques Used: Incubation, Labeling, Radioactivity, Cell Culture, Staining, Software

    Acanthamoeba MBP is a mannose-containing glycoprotein. (A) Duplicate aliquots of purified Acanthamoeba MBP were electrophoresed on denaturing 10% SDS-polyacrylamide gels, and proteins from the gels were transferred onto a nitrocellulose paper. The blots were stained with Ponceau S (left) and were subsequently reacted with biotinylated s-ConA in the absence (middle) or presence (right) of 0.1 M α-Man. The blots were developed using a freshly prepared solution of avidin-biotin-peroxidase complex. Note that the amoeba MBP reacted strongly with s-ConA. The binding of s-ConA to MBP was abolished by α-Man. Lactoferrin (Lf) and human IgA (IgA) served as positive controls for mannose-containing glycoproteins, whereas ConA, which lacks mannose, served as a negative control. (B) Affinity-purified MBP was incubated in the absence (−) and presence (+) of PNGase F (1 h; 37°C). Aliquots from the reaction mixtures were electrophoresed on SDS-polyacrylamide gels. Note that PNGase F treatment resulted in an electrophoretic mobility shift of the MBP from ∼130 kDa to ∼110 kDa, showing that the protein contains N-linked oligosaccharides.
    Figure Legend Snippet: Acanthamoeba MBP is a mannose-containing glycoprotein. (A) Duplicate aliquots of purified Acanthamoeba MBP were electrophoresed on denaturing 10% SDS-polyacrylamide gels, and proteins from the gels were transferred onto a nitrocellulose paper. The blots were stained with Ponceau S (left) and were subsequently reacted with biotinylated s-ConA in the absence (middle) or presence (right) of 0.1 M α-Man. The blots were developed using a freshly prepared solution of avidin-biotin-peroxidase complex. Note that the amoeba MBP reacted strongly with s-ConA. The binding of s-ConA to MBP was abolished by α-Man. Lactoferrin (Lf) and human IgA (IgA) served as positive controls for mannose-containing glycoproteins, whereas ConA, which lacks mannose, served as a negative control. (B) Affinity-purified MBP was incubated in the absence (−) and presence (+) of PNGase F (1 h; 37°C). Aliquots from the reaction mixtures were electrophoresed on SDS-polyacrylamide gels. Note that PNGase F treatment resulted in an electrophoretic mobility shift of the MBP from ∼130 kDa to ∼110 kDa, showing that the protein contains N-linked oligosaccharides.

    Techniques Used: Purification, Staining, Avidin-Biotin Assay, Binding Assay, Negative Control, Affinity Purification, Incubation, Electrophoretic Mobility Shift Assay

    28) Product Images from "Cystic fibrosis remodels the regulation of purinergic signaling by NTPDase1 (CD39) and NTPDase3"

    Article Title: Cystic fibrosis remodels the regulation of purinergic signaling by NTPDase1 (CD39) and NTPDase3

    Journal: American Journal of Physiology - Lung Cellular and Molecular Physiology

    doi: 10.1152/ajplung.00019.2010

    Expression of NTPDase1 and NTPDase3 in human airway epithelia. A : both azide-sensitive NTPDases were detected at the mRNA level by RT-PCR in nasal epithelial cultures (NC), bronchial epithelial cultures (BC), nasal excised epithelia (NE), and bronchial
    Figure Legend Snippet: Expression of NTPDase1 and NTPDase3 in human airway epithelia. A : both azide-sensitive NTPDases were detected at the mRNA level by RT-PCR in nasal epithelial cultures (NC), bronchial epithelial cultures (BC), nasal excised epithelia (NE), and bronchial

    Techniques Used: Expressing, Reverse Transcription Polymerase Chain Reaction

    Widespread expression of NTPDase1 in human airways. Immunolabeling of NTPDase1 in frozen airway tissue sections photographed at ×10 ( left ) and ×40 ( right ). A and B : in the bronchial region, NTPDase1 labels the epithelium (Epi) as an intracellular
    Figure Legend Snippet: Widespread expression of NTPDase1 in human airways. Immunolabeling of NTPDase1 in frozen airway tissue sections photographed at ×10 ( left ) and ×40 ( right ). A and B : in the bronchial region, NTPDase1 labels the epithelium (Epi) as an intracellular

    Techniques Used: Expressing, Immunolabeling

    Airway distribution of NTPDase1 showing cell type-specific responses to the CF disease. Immunolabeling of NTPDase1 in frozen tissue sections photographed at ×10 ( left ) and ×40 ( right ). The disease does not affect the cell types immunolabeled,
    Figure Legend Snippet: Airway distribution of NTPDase1 showing cell type-specific responses to the CF disease. Immunolabeling of NTPDase1 in frozen tissue sections photographed at ×10 ( left ) and ×40 ( right ). The disease does not affect the cell types immunolabeled,

    Techniques Used: Immunolabeling

    29) Product Images from "The Highly Prolific Phenotype of Lacaune Sheep Is Associated with an Ectopic Expression of the B4GALNT2 Gene within the Ovary"

    Article Title: The Highly Prolific Phenotype of Lacaune Sheep Is Associated with an Ectopic Expression of the B4GALNT2 Gene within the Ovary

    Journal: PLoS Genetics

    doi: 10.1371/journal.pgen.1003809

    B4GALNT2 transferase activity revealed by DBA lectin and KM694 antibody staining in Lacaune sheep ovary. Photomicrographs of ovarian sections from +/+ and L/L ewes and stained either with biotinylated-DBA lectin (500 ng/ml) or KM694 mouse monoclonal antibody (1/1000 dilution). A GalNac treatment (200 µM) was used to compete for DBA staining as specificity control. Sections were counterstained with hematoxylin. A black segment indicates the microscopy magnification scale. GC, granulosa cell layer; TC, theca cell layer; Ant, antral cavity.
    Figure Legend Snippet: B4GALNT2 transferase activity revealed by DBA lectin and KM694 antibody staining in Lacaune sheep ovary. Photomicrographs of ovarian sections from +/+ and L/L ewes and stained either with biotinylated-DBA lectin (500 ng/ml) or KM694 mouse monoclonal antibody (1/1000 dilution). A GalNac treatment (200 µM) was used to compete for DBA staining as specificity control. Sections were counterstained with hematoxylin. A black segment indicates the microscopy magnification scale. GC, granulosa cell layer; TC, theca cell layer; Ant, antral cavity.

    Techniques Used: Activity Assay, Staining, Microscopy

    Western immunoblotting analysis of B4GALNT2 transferase activity in Lacaune sheep granulosa cells and follicular fluids. Granulosa cell protein extracts (50 µg) and follicular fluids (200 µg) from +/+ and L/L large antral follicles were precipitated (P) by agarose-DBA lectin or sepharose-protein A-KM694 monoclonal antibody. The resulting purified glycoproteins were separated on SDS-PAGE, transferred on nitrocellulose membrane and revealed after blotting (B) using biotinylated-DBA lectin or KM694 monoclonal antibody.
    Figure Legend Snippet: Western immunoblotting analysis of B4GALNT2 transferase activity in Lacaune sheep granulosa cells and follicular fluids. Granulosa cell protein extracts (50 µg) and follicular fluids (200 µg) from +/+ and L/L large antral follicles were precipitated (P) by agarose-DBA lectin or sepharose-protein A-KM694 monoclonal antibody. The resulting purified glycoproteins were separated on SDS-PAGE, transferred on nitrocellulose membrane and revealed after blotting (B) using biotinylated-DBA lectin or KM694 monoclonal antibody.

    Techniques Used: Western Blot, Activity Assay, Purification, SDS Page

    B4GALNT2 transferase activity revealed by DBA lectin after in vitro overexpression of B4GALNT2 in ovine granulosa cells. Primary ovine granulosa cells from +/+ small antral follicles were transiently transfected with either the pCDNA-hB4GALNT2 expressing the human form of B4GALNT2 or the empty pCDNA3.1 vector. Twenty-four hours after transfection, cells were stained with biotinylated-DBA lectin (500 ng/ml). Arrows indicated DBA positive staining only in B4GALNT2 transfected cells. Cells were counterstained with hematoxylin. A black bar indicates the microscopy magnification scale.
    Figure Legend Snippet: B4GALNT2 transferase activity revealed by DBA lectin after in vitro overexpression of B4GALNT2 in ovine granulosa cells. Primary ovine granulosa cells from +/+ small antral follicles were transiently transfected with either the pCDNA-hB4GALNT2 expressing the human form of B4GALNT2 or the empty pCDNA3.1 vector. Twenty-four hours after transfection, cells were stained with biotinylated-DBA lectin (500 ng/ml). Arrows indicated DBA positive staining only in B4GALNT2 transfected cells. Cells were counterstained with hematoxylin. A black bar indicates the microscopy magnification scale.

    Techniques Used: Activity Assay, In Vitro, Over Expression, Transfection, Expressing, Plasmid Preparation, Staining, Microscopy

    30) Product Images from "Organotypic vibrosections: Novel whole sagittal brain cultures"

    Article Title: Organotypic vibrosections: Novel whole sagittal brain cultures

    Journal: Journal of Neuroscience Methods

    doi: 10.1016/j.jneumeth.2011.07.021

    Co-localization of dopaminergic and cholinergic neurons and capillaries in organotypic sagittal vibrosections using chromogenic substrate (A and B) or fluorescence labelling (C–I). (A) shows a triple immunohistochemical staining for cholinergic neurons (DAB-nickel, black), dopaminergic neurons (SG, grey) and calbindin (VIP, violet). (B) shows TH+ nerve fibers (arrows, blue) crossing ChAT+ neurons (brown) in the basal nucleus of Meynert. (C)–(F) show co-localization of cholinergic ChAT+ neurons (arrow, C) with laminin+ capillaries (D). (G)–(I) show cytoplasmic staining of TH+ dopaminergic neurons (arrow, G). Nuclei were stained with DAPI (E, H). (F) and (I) show the merged pictures. Scale bar in (A) = 1200 μm, 30 μm (B) and 60 μm (C–I).
    Figure Legend Snippet: Co-localization of dopaminergic and cholinergic neurons and capillaries in organotypic sagittal vibrosections using chromogenic substrate (A and B) or fluorescence labelling (C–I). (A) shows a triple immunohistochemical staining for cholinergic neurons (DAB-nickel, black), dopaminergic neurons (SG, grey) and calbindin (VIP, violet). (B) shows TH+ nerve fibers (arrows, blue) crossing ChAT+ neurons (brown) in the basal nucleus of Meynert. (C)–(F) show co-localization of cholinergic ChAT+ neurons (arrow, C) with laminin+ capillaries (D). (G)–(I) show cytoplasmic staining of TH+ dopaminergic neurons (arrow, G). Nuclei were stained with DAPI (E, H). (F) and (I) show the merged pictures. Scale bar in (A) = 1200 μm, 30 μm (B) and 60 μm (C–I).

    Techniques Used: Fluorescence, Immunohistochemistry, Staining

    H 2 O 2 -induced (450 mM for 3 days) alterations in the hippocampus of organotypic sagittal vibrosections stained for DAPI (A and D), propidiumiodide (B and E; PI) and calbindin (C and F). Note enhanced PI staining and reduced calbindin staining after hydrogen peroxide. DG, dentate gyrus; CA1, pyramidal cell layer CA1. Scale bar in (F) = 500 μm.
    Figure Legend Snippet: H 2 O 2 -induced (450 mM for 3 days) alterations in the hippocampus of organotypic sagittal vibrosections stained for DAPI (A and D), propidiumiodide (B and E; PI) and calbindin (C and F). Note enhanced PI staining and reduced calbindin staining after hydrogen peroxide. DG, dentate gyrus; CA1, pyramidal cell layer CA1. Scale bar in (F) = 500 μm.

    Techniques Used: Staining

    31) Product Images from "Copper chelation with tetrathiomolybdate suppresses adjuvant-induced arthritis and inflammation-associated cachexia in rats"

    Article Title: Copper chelation with tetrathiomolybdate suppresses adjuvant-induced arthritis and inflammation-associated cachexia in rats

    Journal: Arthritis Research & Therapy

    doi: 10.1186/ar1801

    Immnunostaining for VEGF in synovial tissue in AIA rats. (a) , (c) , (e) AIA rats treated with deionized water and (b) , (d) tetrathiomolybdate (TM). Immunohistochemical staining was performed with the Vecto Stain avidin–biotin peroxidase complex kit (Vector Laboratories, Burlingame, CA, USA). Synovial tissues sections were stained with (a)–(d) mouse anti-VEGF monoclonal IgG antibodies (1:200 dilution, in PBS; Santa Cruz Biotechnology, Santa Cruz California, USA) and (e) a normal mouse IgG (1:200 dilution, in PBS). Positive immunostaining was indicated by brownish deposits. The counterstain was an aqueous solution of hematoxylin. (a), (b) Original magnification × 40; (c)–(e) original magnification × 400. AIA, adjuvant-induced arthritis; ET, endothelial cell; SL, synovial lining cell.
    Figure Legend Snippet: Immnunostaining for VEGF in synovial tissue in AIA rats. (a) , (c) , (e) AIA rats treated with deionized water and (b) , (d) tetrathiomolybdate (TM). Immunohistochemical staining was performed with the Vecto Stain avidin–biotin peroxidase complex kit (Vector Laboratories, Burlingame, CA, USA). Synovial tissues sections were stained with (a)–(d) mouse anti-VEGF monoclonal IgG antibodies (1:200 dilution, in PBS; Santa Cruz Biotechnology, Santa Cruz California, USA) and (e) a normal mouse IgG (1:200 dilution, in PBS). Positive immunostaining was indicated by brownish deposits. The counterstain was an aqueous solution of hematoxylin. (a), (b) Original magnification × 40; (c)–(e) original magnification × 400. AIA, adjuvant-induced arthritis; ET, endothelial cell; SL, synovial lining cell.

    Techniques Used: Immunohistochemistry, Staining, Avidin-Biotin Assay, Plasmid Preparation, Immunostaining

    32) Product Images from "The Importance of Titrating Antibodies for Immunocytochemical Methods"

    Article Title: The Importance of Titrating Antibodies for Immunocytochemical Methods

    Journal: Current protocols in neuroscience / editorial board, Jacqueline N. Crawley ... [et al.]

    doi: 10.1002/cpns.1

    The ABC peroxidase technique. This approach is similar to that shown in , but substitutes a biotinylated peroxidase. When incubated with a substrate such as DAB (lower left) or NiDAB (lower right), the colored insoluble product is deposited
    Figure Legend Snippet: The ABC peroxidase technique. This approach is similar to that shown in , but substitutes a biotinylated peroxidase. When incubated with a substrate such as DAB (lower left) or NiDAB (lower right), the colored insoluble product is deposited

    Techniques Used: Incubation

    TSA-amplified fluorescence using biotinylated tyramine and streptavidin fluorophore. Note the greatly increased number of fluorescent molecules compared with that seen for either fluorophore-tagged secondaries or ABC streptavidin methods. P = peroxidase.
    Figure Legend Snippet: TSA-amplified fluorescence using biotinylated tyramine and streptavidin fluorophore. Note the greatly increased number of fluorescent molecules compared with that seen for either fluorophore-tagged secondaries or ABC streptavidin methods. P = peroxidase.

    Techniques Used: Amplification, Fluorescence

    33) Product Images from "Expression and Potential Role of Fas-Associated Phosphatase-1 in Ovarian Cancer"

    Article Title: Expression and Potential Role of Fas-Associated Phosphatase-1 in Ovarian Cancer

    Journal: The American Journal of Pathology

    doi:

    Immunocytochemical analysis of FAP-1 in ovarian cancer cell lines. A: Cells were cultured in chamber slides, fixed in Bouin’s solution, and washed with PBS. Immunostaining was performed using a goat polyclonal antibody (Santa Cruz sc-1138) and a biotinylated horse anti-goat secondary antibody (Vector Laboratories). Antibody detection was by the diaminobenzidine method (brown) with hematoxylin counterstaining of nuclei (blue). Competition study using excess FAP-1 peptide (Santa Cruz sc-1138p) served as a negative control ( bottom ). B: Cell lines were fixed, suspended in agarose, and then embedded in paraffin for sectioning and immunostaining using polyclonal antiserum no. 1730. Immunodetection was performed involving the Rabbit Envision-Plus-horseradish peroxidase system with a Universal System automated immunostainer (DAKO). Omitting primary antibody or applying preimmune serum served as controls ( bottom ).
    Figure Legend Snippet: Immunocytochemical analysis of FAP-1 in ovarian cancer cell lines. A: Cells were cultured in chamber slides, fixed in Bouin’s solution, and washed with PBS. Immunostaining was performed using a goat polyclonal antibody (Santa Cruz sc-1138) and a biotinylated horse anti-goat secondary antibody (Vector Laboratories). Antibody detection was by the diaminobenzidine method (brown) with hematoxylin counterstaining of nuclei (blue). Competition study using excess FAP-1 peptide (Santa Cruz sc-1138p) served as a negative control ( bottom ). B: Cell lines were fixed, suspended in agarose, and then embedded in paraffin for sectioning and immunostaining using polyclonal antiserum no. 1730. Immunodetection was performed involving the Rabbit Envision-Plus-horseradish peroxidase system with a Universal System automated immunostainer (DAKO). Omitting primary antibody or applying preimmune serum served as controls ( bottom ).

    Techniques Used: Cell Culture, Immunostaining, Plasmid Preparation, Negative Control, Immunodetection

    34) Product Images from "Liver changes in severe Plasmodium falciparum malaria: histopathology, apoptosis and nuclear factor kappa B expression"

    Article Title: Liver changes in severe Plasmodium falciparum malaria: histopathology, apoptosis and nuclear factor kappa B expression

    Journal: Malaria Journal

    doi: 10.1186/1475-2875-13-106

    Representative immunohistochemical staining patterns of cleaved caspase-3 (A-C) and NF-κB p65 (D-F) in a normal liver showing negative staining for hepatocytes and Kupffer cells (A,D); in the livers of a severe P. falciparum malaria case without hyperbilirubinaemia (B,D) and with hyperbilirubinaemia (C,F). Hepatocytes are generally unaffected. Arrows show Kupffer cells lying next to the hepatic cord, within the sinusoidal area. In the normal liver, Kupffer cells are small, non-reactive and rarely express the cleaved caspase-3 marker (A) and show few NF-κB p65 (D) compared with severe P. falciparum malaria without hyperbilirubinaemia (B,E) and with hyperbilirubinaemia (C,F) where Kupffer cells are enlarged and hyperplastic. Most Kupffer cells containing haemozoin pigment (arrowheads) expressed apoptotic and NF-κB p65 markers. Numerous Kupffer cells show apoptosis (C) and NF-κB p65 expression (F) in severe P. falciparum malaria with hyperbilirubinaemia. All images are at 400x magnification; bars are 20 μm.
    Figure Legend Snippet: Representative immunohistochemical staining patterns of cleaved caspase-3 (A-C) and NF-κB p65 (D-F) in a normal liver showing negative staining for hepatocytes and Kupffer cells (A,D); in the livers of a severe P. falciparum malaria case without hyperbilirubinaemia (B,D) and with hyperbilirubinaemia (C,F). Hepatocytes are generally unaffected. Arrows show Kupffer cells lying next to the hepatic cord, within the sinusoidal area. In the normal liver, Kupffer cells are small, non-reactive and rarely express the cleaved caspase-3 marker (A) and show few NF-κB p65 (D) compared with severe P. falciparum malaria without hyperbilirubinaemia (B,E) and with hyperbilirubinaemia (C,F) where Kupffer cells are enlarged and hyperplastic. Most Kupffer cells containing haemozoin pigment (arrowheads) expressed apoptotic and NF-κB p65 markers. Numerous Kupffer cells show apoptosis (C) and NF-κB p65 expression (F) in severe P. falciparum malaria with hyperbilirubinaemia. All images are at 400x magnification; bars are 20 μm.

    Techniques Used: Immunohistochemistry, Staining, Negative Staining, Marker, Expressing

    Cleaved caspase-3 expression in Kupffer cells and lymphocytes in the portal tracts. Significant differences were observed between the severe malaria groups (with and without hyperbilirubinaemia) and the normal controls (a), and between the hyperbilirubinaemia and non-hyperbilirubinaemia groups (b) ( p
    Figure Legend Snippet: Cleaved caspase-3 expression in Kupffer cells and lymphocytes in the portal tracts. Significant differences were observed between the severe malaria groups (with and without hyperbilirubinaemia) and the normal controls (a), and between the hyperbilirubinaemia and non-hyperbilirubinaemia groups (b) ( p

    Techniques Used: Expressing

    Correlation between NF-κB p65 and cleaved caspase-3 activation. A- in Kupffer cells (Spearman’s ρ test: r s = 0.713, p
    Figure Legend Snippet: Correlation between NF-κB p65 and cleaved caspase-3 activation. A- in Kupffer cells (Spearman’s ρ test: r s = 0.713, p

    Techniques Used: Activation Assay

    35) Product Images from "Linagliptin alleviates fatty liver disease in diabetic db/db mice"

    Article Title: Linagliptin alleviates fatty liver disease in diabetic db/db mice

    Journal: World Journal of Diabetes

    doi: 10.4239/wjd.v7.i19.534

    Immunohistochemical staining for lymphatic vessel endothelial hyaluronan receptor-1 in the liver of intact (A and B), placebo-treated (C) and linagliptin-treated (D, E and F) db / db mice. Staining by anti-LYVE-1 antibodies, indirect streptavidin-biotin method; A, C, E and F: × 400; B and D: × 100. LYVE-1: Lymphatic vessel endothelial hyaluronan receptor-1.
    Figure Legend Snippet: Immunohistochemical staining for lymphatic vessel endothelial hyaluronan receptor-1 in the liver of intact (A and B), placebo-treated (C) and linagliptin-treated (D, E and F) db / db mice. Staining by anti-LYVE-1 antibodies, indirect streptavidin-biotin method; A, C, E and F: × 400; B and D: × 100. LYVE-1: Lymphatic vessel endothelial hyaluronan receptor-1.

    Techniques Used: Immunohistochemistry, Staining, Mouse Assay

    The area of immunohistochemical staining for lymphatic vessel endothelial hyaluronan receptor-1 in the liver of intact, placebo-treated and linagliptin-treated db/db mice. a P
    Figure Legend Snippet: The area of immunohistochemical staining for lymphatic vessel endothelial hyaluronan receptor-1 in the liver of intact, placebo-treated and linagliptin-treated db/db mice. a P

    Techniques Used: Immunohistochemistry, Staining, Mouse Assay

    36) Product Images from "Linagliptin alleviates fatty liver disease in diabetic db/db mice"

    Article Title: Linagliptin alleviates fatty liver disease in diabetic db/db mice

    Journal: World Journal of Diabetes

    doi: 10.4239/wjd.v7.i19.534

    Immunohistochemical staining for lymphatic vessel endothelial hyaluronan receptor-1 in the liver of intact (A and B), placebo-treated (C) and linagliptin-treated (D, E and F) db / db mice. Staining by anti-LYVE-1 antibodies, indirect streptavidin-biotin method; A, C, E and F: × 400; B and D: × 100. LYVE-1: Lymphatic vessel endothelial hyaluronan receptor-1.
    Figure Legend Snippet: Immunohistochemical staining for lymphatic vessel endothelial hyaluronan receptor-1 in the liver of intact (A and B), placebo-treated (C) and linagliptin-treated (D, E and F) db / db mice. Staining by anti-LYVE-1 antibodies, indirect streptavidin-biotin method; A, C, E and F: × 400; B and D: × 100. LYVE-1: Lymphatic vessel endothelial hyaluronan receptor-1.

    Techniques Used: Immunohistochemistry, Staining, Mouse Assay

    Liver histology in linagliptin-treated db/db diabetic mice. Heterogeneity of the changes of hepatocytes: A: Microvesicular lipid accumulation (L); B: No lipid accumulation. Light microscopy with yellow filter of semi-thin sections stained with toluidine blue; magnification × 1000.
    Figure Legend Snippet: Liver histology in linagliptin-treated db/db diabetic mice. Heterogeneity of the changes of hepatocytes: A: Microvesicular lipid accumulation (L); B: No lipid accumulation. Light microscopy with yellow filter of semi-thin sections stained with toluidine blue; magnification × 1000.

    Techniques Used: Mouse Assay, Light Microscopy, Staining

    The distribution of hepatocytes with lipid inclusions depending on the size of lipid droplets in linagliptin-treated and placebo-treated db/db mice. The reduction in the numeral density of hepatocytes with microsized, mediosized and macrosized droplets in linagliptin-treated mice (hep, hepatocyte, a P
    Figure Legend Snippet: The distribution of hepatocytes with lipid inclusions depending on the size of lipid droplets in linagliptin-treated and placebo-treated db/db mice. The reduction in the numeral density of hepatocytes with microsized, mediosized and macrosized droplets in linagliptin-treated mice (hep, hepatocyte, a P

    Techniques Used: Mouse Assay

    Ultrastructural changes in the hepatocytes of linagliptin-treated db/db mice. A: Heterogeneity of the hepatocytes: Cells with numerous lipid inclusions (1), cells with areas of hyperplasia of smooth ER and lipid vacuoles (2), cells with a relatively uniform distribution of organelles and rare lipid inclusions (3); B: Cells without hyperplasia of the smooth ER with a relatively homogenous distribution of organelles; distinct microvilli on vascular poles of the hepatocytes and on the lateral sides of parenchymal cells; the extension of spaces between hepatocytes (arrows); C and D: Plots of clusters of smooth ER membranes. L: Lipid inclusion; m: Mitochondria; s: Lumen of the sinusoid; SER: Smooth endoplasmic reticulum; bc: Bile capillary.
    Figure Legend Snippet: Ultrastructural changes in the hepatocytes of linagliptin-treated db/db mice. A: Heterogeneity of the hepatocytes: Cells with numerous lipid inclusions (1), cells with areas of hyperplasia of smooth ER and lipid vacuoles (2), cells with a relatively uniform distribution of organelles and rare lipid inclusions (3); B: Cells without hyperplasia of the smooth ER with a relatively homogenous distribution of organelles; distinct microvilli on vascular poles of the hepatocytes and on the lateral sides of parenchymal cells; the extension of spaces between hepatocytes (arrows); C and D: Plots of clusters of smooth ER membranes. L: Lipid inclusion; m: Mitochondria; s: Lumen of the sinusoid; SER: Smooth endoplasmic reticulum; bc: Bile capillary.

    Techniques Used: Mouse Assay

    The mean proportions of hepatocytes with different densities of lipid droplets in linagliptin-treated and placebo-treated db / db mice. The percent of hepatocytes with high density of lipid droplets (more than 15 droplets per cell) is reduced in linagliptin-treated mice compared to placebo-treated mice (hep, hepatocyte, L
    Figure Legend Snippet: The mean proportions of hepatocytes with different densities of lipid droplets in linagliptin-treated and placebo-treated db / db mice. The percent of hepatocytes with high density of lipid droplets (more than 15 droplets per cell) is reduced in linagliptin-treated mice compared to placebo-treated mice (hep, hepatocyte, L

    Techniques Used: Mouse Assay

    Ultrastructural changes in the hepatocytes of linagliptin-treated db/db mice. A: The complexes from the mitochondria, rough ER and lipid droplets; B: Mitochondria with separate granular ER profiles, myelin structures (white arrow), autophagosomes with electrondark content and ribosomes (black arrow) nearby the bile capillaries with pronounced microvilli; C: The transport of lipids into the gaps between hepatocytes (arrow); D: Large vacuoles in the cytoplasm of endothelial cells in the sinusoids. rER: Rough endoplasmic reticulum; sER: Smooth endoplasmic reticulum; bc: Bile capillary; D: The Disse space; c: A tuft of collagen; L: Lipid inclusion; m: Mitochondria; e: Erythrocyte.
    Figure Legend Snippet: Ultrastructural changes in the hepatocytes of linagliptin-treated db/db mice. A: The complexes from the mitochondria, rough ER and lipid droplets; B: Mitochondria with separate granular ER profiles, myelin structures (white arrow), autophagosomes with electrondark content and ribosomes (black arrow) nearby the bile capillaries with pronounced microvilli; C: The transport of lipids into the gaps between hepatocytes (arrow); D: Large vacuoles in the cytoplasm of endothelial cells in the sinusoids. rER: Rough endoplasmic reticulum; sER: Smooth endoplasmic reticulum; bc: Bile capillary; D: The Disse space; c: A tuft of collagen; L: Lipid inclusion; m: Mitochondria; e: Erythrocyte.

    Techniques Used: Mouse Assay

    The liver of linagliptin-treated db/db diabetic mouse. The dilatation of blood and lymphatic vessels of portal tracts, central veins was less profound. Numerous diplocariocytes were present (arrows). V: The vein of portal tract; b: Bile duct of portal tract; cv: Central vein. H and E; magnification × 400.
    Figure Legend Snippet: The liver of linagliptin-treated db/db diabetic mouse. The dilatation of blood and lymphatic vessels of portal tracts, central veins was less profound. Numerous diplocariocytes were present (arrows). V: The vein of portal tract; b: Bile duct of portal tract; cv: Central vein. H and E; magnification × 400.

    Techniques Used:

    The area of immunohistochemical staining for lymphatic vessel endothelial hyaluronan receptor-1 in the liver of intact, placebo-treated and linagliptin-treated db/db mice. a P
    Figure Legend Snippet: The area of immunohistochemical staining for lymphatic vessel endothelial hyaluronan receptor-1 in the liver of intact, placebo-treated and linagliptin-treated db/db mice. a P

    Techniques Used: Immunohistochemistry, Staining, Mouse Assay

    37) Product Images from "Social Isolation Modulates CLOCK Protein and Beta-Catenin Expression Pattern in Gonadotropin-Inhibitory Hormone Neurons in Male Rats"

    Article Title: Social Isolation Modulates CLOCK Protein and Beta-Catenin Expression Pattern in Gonadotropin-Inhibitory Hormone Neurons in Male Rats

    Journal: Frontiers in Endocrinology

    doi: 10.3389/fendo.2017.00225

    The effect of postweaning social isolation on β-catenin colocalization with gonadotropin-inhibitory hormone (GnIH) neurons in the dorsomedial hypothalamus region. (A) Comparison of β-catenin nuclear colocalization within GnIH neurons of the control and isolated rats at ZT12 and ZT18 (control: n = 6 and isolation: n = 6 for ZT12 and control: n = 9 and isolation: n = 9 for ZT18). (B) Comparison of β-catenin cytoplasmic colocalization in GnIH neurons of control and isolated rats in ZT12 and ZT18 (control: n = 6 and isolation: n = 6 for ZT12 and control: n = 9 and isolation: n = 9 for ZT18). Data are presented as means ± SEM for each set. Significance was set at p
    Figure Legend Snippet: The effect of postweaning social isolation on β-catenin colocalization with gonadotropin-inhibitory hormone (GnIH) neurons in the dorsomedial hypothalamus region. (A) Comparison of β-catenin nuclear colocalization within GnIH neurons of the control and isolated rats at ZT12 and ZT18 (control: n = 6 and isolation: n = 6 for ZT12 and control: n = 9 and isolation: n = 9 for ZT18). (B) Comparison of β-catenin cytoplasmic colocalization in GnIH neurons of control and isolated rats in ZT12 and ZT18 (control: n = 6 and isolation: n = 6 for ZT12 and control: n = 9 and isolation: n = 9 for ZT18). Data are presented as means ± SEM for each set. Significance was set at p

    Techniques Used: Isolation

    Alteration of gonadotropin-inhibitory hormone (GnIH) neuronal activity may involve change in β-catenin activity due to disturbances in CLOCK expression stemming from social isolation.
    Figure Legend Snippet: Alteration of gonadotropin-inhibitory hormone (GnIH) neuronal activity may involve change in β-catenin activity due to disturbances in CLOCK expression stemming from social isolation.

    Techniques Used: Activity Assay, Expressing, Isolation

    The colocalization of β-catenin immunostaining with DAPI within gonadotropin-inhibitory hormone (GnIH) neurons in the dorsomedial hypothalamus (DMH) region. (A) β-catenin immunostaining (red) and DAPI cytoplasmic staining (blue) and (B) colocalization with GnIH neuron (green). (C) β-catenin immunostaining (red) in the cytoplasm with DAPI nuclear staining (blue) and (D) colocalization with GnIH neuron (green). Scale bar = 20 µm. White arrows indicate the presence of β-catenin colocalization with GnIH neurons.
    Figure Legend Snippet: The colocalization of β-catenin immunostaining with DAPI within gonadotropin-inhibitory hormone (GnIH) neurons in the dorsomedial hypothalamus (DMH) region. (A) β-catenin immunostaining (red) and DAPI cytoplasmic staining (blue) and (B) colocalization with GnIH neuron (green). (C) β-catenin immunostaining (red) in the cytoplasm with DAPI nuclear staining (blue) and (D) colocalization with GnIH neuron (green). Scale bar = 20 µm. White arrows indicate the presence of β-catenin colocalization with GnIH neurons.

    Techniques Used: Immunostaining, Staining

    Colocalization of β-catenin within gonadotropin-inhibitory hormone (GnIH) neurons in the dorsomedial hypothalamus (DMH) region across different time points. β-catenin immunostaining (red) was observed within GnIH neurons (green) in (A) control at ZT12, (B) control at ZT18, (C) isolation at ZT12, and (D) isolation at ZT18. Scale bar = 25 µm. White arrows indicate cytoplasmic colocalization, while white arrowheads indicate colocalization within or around the nucleus of GnIH neurons.
    Figure Legend Snippet: Colocalization of β-catenin within gonadotropin-inhibitory hormone (GnIH) neurons in the dorsomedial hypothalamus (DMH) region across different time points. β-catenin immunostaining (red) was observed within GnIH neurons (green) in (A) control at ZT12, (B) control at ZT18, (C) isolation at ZT12, and (D) isolation at ZT18. Scale bar = 25 µm. White arrows indicate cytoplasmic colocalization, while white arrowheads indicate colocalization within or around the nucleus of GnIH neurons.

    Techniques Used: Immunostaining, Isolation

    38) Product Images from "Regulation of Neuregulin Expression in the Injured Rat Brain and Cultured Astrocytes"

    Article Title: Regulation of Neuregulin Expression in the Injured Rat Brain and Cultured Astrocytes

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.21-04-01257.2001

    Immunohistochemical localization of neuregulin and ErbB2 in the cerebrum of an 8-week-old rat. An antibody against neuregulin-β ( A–C ) or an antibody against ErbB2 ( D–F ) was used to stain paraformaldehyde-fixed thin sections. Immunolocalization of neuregulin ( A ) and ErbB2 ( D ) in the CA1 area of the hippocampus is shown. The distribution of neuregulin ( B ) and ErbB2 ( E ) in the cerebral cortex is also shown. Most neuregulin and ErbB2 immunoreactivities appear on neuronal cell surfaces. A higher magnification of immunostained sections shows the presence of neuregulin ( C ) and ErbB2 ( F ) on cortical neuronal cells. Scale bars: A,C,D,F, 50 μm; B,E, 500 μm.
    Figure Legend Snippet: Immunohistochemical localization of neuregulin and ErbB2 in the cerebrum of an 8-week-old rat. An antibody against neuregulin-β ( A–C ) or an antibody against ErbB2 ( D–F ) was used to stain paraformaldehyde-fixed thin sections. Immunolocalization of neuregulin ( A ) and ErbB2 ( D ) in the CA1 area of the hippocampus is shown. The distribution of neuregulin ( B ) and ErbB2 ( E ) in the cerebral cortex is also shown. Most neuregulin and ErbB2 immunoreactivities appear on neuronal cell surfaces. A higher magnification of immunostained sections shows the presence of neuregulin ( C ) and ErbB2 ( F ) on cortical neuronal cells. Scale bars: A,C,D,F, 50 μm; B,E, 500 μm.

    Techniques Used: Immunohistochemistry, Staining

    39) Product Images from "Regulation of Neuregulin Expression in the Injured Rat Brain and Cultured Astrocytes"

    Article Title: Regulation of Neuregulin Expression in the Injured Rat Brain and Cultured Astrocytes

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.21-04-01257.2001

    Immunohistochemical localization of ErbB2 and ErbB3 in the injured brain. A shows anti-ErbB2 immunoreactive cells appearing near the wound. B, D , Higher magnification images of an area adjacent to the wound stained with anti-ErbB2 and anti-ErbB3 antibodies, respectively. The immunopositive cells indicated by the arrowheads are shown at a higher magnification in the box . These immunopositive cells were not observed in the sections stained with antibodies preabsorbed with the corresponding recombinant peptides ( C, E ). In the deep layer of the injured cortex, ErbB2 ( F ) and ErbB3 ( G ) immunoreactivities were also detected. The black arrowheads shown in F and G indicate reactive astrocyte-like cells. WM , White matter. Scale bars: A , 0.5 mm; B–E (shown in E ), 50 μm; F, G, 20 μm.
    Figure Legend Snippet: Immunohistochemical localization of ErbB2 and ErbB3 in the injured brain. A shows anti-ErbB2 immunoreactive cells appearing near the wound. B, D , Higher magnification images of an area adjacent to the wound stained with anti-ErbB2 and anti-ErbB3 antibodies, respectively. The immunopositive cells indicated by the arrowheads are shown at a higher magnification in the box . These immunopositive cells were not observed in the sections stained with antibodies preabsorbed with the corresponding recombinant peptides ( C, E ). In the deep layer of the injured cortex, ErbB2 ( F ) and ErbB3 ( G ) immunoreactivities were also detected. The black arrowheads shown in F and G indicate reactive astrocyte-like cells. WM , White matter. Scale bars: A , 0.5 mm; B–E (shown in E ), 50 μm; F, G, 20 μm.

    Techniques Used: Immunohistochemistry, Staining, Recombinant

    Double-label fluorescent localization of neuregulin with GFAP, ErbB2 with GFAP, and ErbB3 with ErbB2 in an injured cortex. A , Neuregulin immunoreactivity near the injured site. B , GFAP immunoreactivity in the same section of A . C , Superimposed image of A and B . D , ErbB2 immunoreactivity near the injured site. E , GFAP immunoreactivity in the same section of D . F , Superimposed image of D and E . G , ErbB3 immunoreactivity near the injured site. H , ErbB2 immunoreactivity in the same section of G . I , Superimposed image of G and H . Scale bars, 10 μm.
    Figure Legend Snippet: Double-label fluorescent localization of neuregulin with GFAP, ErbB2 with GFAP, and ErbB3 with ErbB2 in an injured cortex. A , Neuregulin immunoreactivity near the injured site. B , GFAP immunoreactivity in the same section of A . C , Superimposed image of A and B . D , ErbB2 immunoreactivity near the injured site. E , GFAP immunoreactivity in the same section of D . F , Superimposed image of D and E . G , ErbB3 immunoreactivity near the injured site. H , ErbB2 immunoreactivity in the same section of G . I , Superimposed image of G and H . Scale bars, 10 μm.

    Techniques Used:

    40) Product Images from "A monoclonal antibody recognizing human cancers with amplification/overexpression of the human epidermal growth factor receptor"

    Article Title: A monoclonal antibody recognizing human cancers with amplification/overexpression of the human epidermal growth factor receptor

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    doi: 10.1073/pnas.232686499

    Hematoxylin/eosin ( A – C ) and immunohistochemical ( D – L ) (avidin–biotin-complex technique, diaminobenzidine tetrahydrochloride chromogen) staining of three glioblastoma specimens pretyped for presence of wtEGFR ( A , D , G , and J ), amplified EGFR ( B , E , H , and K ), or amplified EGFR and ΔEGFR ( C , F , I , and L ) with 528 ( D – F ), 806 ( G – I ), or DH8.3 ( J – L ). 528 staining of the three glioblastomas ( D – F ), 806 staining of glioblastoma having EGFR amplification without ΔEGFR ( H ) or with ΔEGFR ( I ), and DH8.3 staining of glioblastoma with amplified EGFR and ΔEGFR ( L ) are shown.
    Figure Legend Snippet: Hematoxylin/eosin ( A – C ) and immunohistochemical ( D – L ) (avidin–biotin-complex technique, diaminobenzidine tetrahydrochloride chromogen) staining of three glioblastoma specimens pretyped for presence of wtEGFR ( A , D , G , and J ), amplified EGFR ( B , E , H , and K ), or amplified EGFR and ΔEGFR ( C , F , I , and L ) with 528 ( D – F ), 806 ( G – I ), or DH8.3 ( J – L ). 528 staining of the three glioblastomas ( D – F ), 806 staining of glioblastoma having EGFR amplification without ΔEGFR ( H ) or with ΔEGFR ( I ), and DH8.3 staining of glioblastoma with amplified EGFR and ΔEGFR ( L ) are shown.

    Techniques Used: Immunohistochemistry, Avidin-Biotin Assay, Staining, Amplification

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    Avidin-Biotin Assay:

    Article Title: Corticosteroid-Binding Globulin is expressed in the adrenal gland and its absence impairs corticosterone synthesis and secretion in a sex-dependent manner
    Article Snippet: .. Then, slides were incubated with biotinylated rabbit anti-goat (1:400) and signal detection was performed with an avidin-biotin peroxidase complex (Vectastain ABC Kit, Vector Labs) and developed with diaminobenzidine hydrochloride chromogen (Sigma). .. The slides were visualized by light microscopy (Olympus BX-51) and image were captured with Olympus DP-70 Digital Camera System.

    Article Title: High concentrations of HGF inhibit skeletal muscle satellite cell proliferation in vitro by inducing expression of myostatin: a possible mechanism for reestablishing satellite cell quiescence in vivo
    Article Snippet: .. For the immunodetection of target proteins in satellite cells, the following materials were additionally used: antigen-affinity-purified goat polyclonal anti-mouse myostatin neutralizing antibody (AF788), rat monoclonal anti-mouse myostatin antibody (MAB788) and goat polyclonal anti-mouse c-met antibody (AF527) from R & D Systems; D3 mouse monoclonal antidesmin and G3G4 mouse monoclonal anti-BrdU antibodies from the Developmental Studies Hybridoma Bank (Iowa City, IA); SX118 mouse monoclonal anti-p21 (556430) and 5.8A mouse anti-MyoD antibodies (554130) from BD Biosciences (San Jose, CA); DM1A mouse monoclonal anti-chick α-tubulin antibody (T9026) from Sigma; affinity-purified biotinylated rabbit anti-goat IgG (BA-5000), horse anti-mouse IgG (BA-2000), rabbit anti-rat IgG (BA-4000) and horseradish peroxidase (HRPO)-labeled avidin kit (PK-6100) from Vector Laboratories (Burlingame, CA); affinity-purified HRPO-conjugated goat anti-mouse IgG (A-4416) and 3,3′-diaminobenzidine (DAB) from Sigma; enhanced chemiluminescence (ECL) detection kit (PRN2106) and nitrocellulose membranes (Hybond ECL, RPN2020D) from GE Healthcare (Little Chalfont, UK); biotinylated molecular weight standards (161-0319) from Bio-Rad (Hercules, CA); BIOMAX-XAR X-ray film (166-0760) from Eastman Kodak (Rochester, NY). ..

    Article Title: Expression of orexin A and its receptor 1 in the human prostate
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    Blocking Assay:

    Article Title: Expression of orexin A and its receptor 1 in the human prostate
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    Immunodetection:

    Article Title: High concentrations of HGF inhibit skeletal muscle satellite cell proliferation in vitro by inducing expression of myostatin: a possible mechanism for reestablishing satellite cell quiescence in vivo
    Article Snippet: .. For the immunodetection of target proteins in satellite cells, the following materials were additionally used: antigen-affinity-purified goat polyclonal anti-mouse myostatin neutralizing antibody (AF788), rat monoclonal anti-mouse myostatin antibody (MAB788) and goat polyclonal anti-mouse c-met antibody (AF527) from R & D Systems; D3 mouse monoclonal antidesmin and G3G4 mouse monoclonal anti-BrdU antibodies from the Developmental Studies Hybridoma Bank (Iowa City, IA); SX118 mouse monoclonal anti-p21 (556430) and 5.8A mouse anti-MyoD antibodies (554130) from BD Biosciences (San Jose, CA); DM1A mouse monoclonal anti-chick α-tubulin antibody (T9026) from Sigma; affinity-purified biotinylated rabbit anti-goat IgG (BA-5000), horse anti-mouse IgG (BA-2000), rabbit anti-rat IgG (BA-4000) and horseradish peroxidase (HRPO)-labeled avidin kit (PK-6100) from Vector Laboratories (Burlingame, CA); affinity-purified HRPO-conjugated goat anti-mouse IgG (A-4416) and 3,3′-diaminobenzidine (DAB) from Sigma; enhanced chemiluminescence (ECL) detection kit (PRN2106) and nitrocellulose membranes (Hybond ECL, RPN2020D) from GE Healthcare (Little Chalfont, UK); biotinylated molecular weight standards (161-0319) from Bio-Rad (Hercules, CA); BIOMAX-XAR X-ray film (166-0760) from Eastman Kodak (Rochester, NY). ..

    Incubation:

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    Article Title: Elevated CXCL1 expression in breast cancer stroma predicts poor prognosis and is inversely associated with expression of TGF-β signaling proteins
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    Article Title: A novel multiplex assay for simultaneous quantification of total and S129 phosphorylated human alpha-synuclein
    Article Snippet: .. The next day sections were rinsed with KPBS and incubated in 0.25 % Triton + 5 % normal serum in KPBS for 1 h containing secondary antibody biotinylated goat anti rabbit (1:200, Vector Laboratories Inc., USA). .. Sections were again washed with KPBS and incubated with 0.25 % triton + 5 % normal serum in KPBS containing AlexaFluor647 conjugated streptavidin (1:200, Invitrogen, USA) and secondary antibody donkey anti mouse coupled to AlexaFluor488 fluorophore (Jackson, USA) for 2 h. After washes with KPBS, sections were mounted and coverslipped using PVA-DABCO mounting medium (Sigma-Aldrich, Sweden).

    Article Title: Corticosteroid-Binding Globulin is expressed in the adrenal gland and its absence impairs corticosterone synthesis and secretion in a sex-dependent manner
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    IA:

    Article Title: High concentrations of HGF inhibit skeletal muscle satellite cell proliferation in vitro by inducing expression of myostatin: a possible mechanism for reestablishing satellite cell quiescence in vivo
    Article Snippet: .. For the immunodetection of target proteins in satellite cells, the following materials were additionally used: antigen-affinity-purified goat polyclonal anti-mouse myostatin neutralizing antibody (AF788), rat monoclonal anti-mouse myostatin antibody (MAB788) and goat polyclonal anti-mouse c-met antibody (AF527) from R & D Systems; D3 mouse monoclonal antidesmin and G3G4 mouse monoclonal anti-BrdU antibodies from the Developmental Studies Hybridoma Bank (Iowa City, IA); SX118 mouse monoclonal anti-p21 (556430) and 5.8A mouse anti-MyoD antibodies (554130) from BD Biosciences (San Jose, CA); DM1A mouse monoclonal anti-chick α-tubulin antibody (T9026) from Sigma; affinity-purified biotinylated rabbit anti-goat IgG (BA-5000), horse anti-mouse IgG (BA-2000), rabbit anti-rat IgG (BA-4000) and horseradish peroxidase (HRPO)-labeled avidin kit (PK-6100) from Vector Laboratories (Burlingame, CA); affinity-purified HRPO-conjugated goat anti-mouse IgG (A-4416) and 3,3′-diaminobenzidine (DAB) from Sigma; enhanced chemiluminescence (ECL) detection kit (PRN2106) and nitrocellulose membranes (Hybond ECL, RPN2020D) from GE Healthcare (Little Chalfont, UK); biotinylated molecular weight standards (161-0319) from Bio-Rad (Hercules, CA); BIOMAX-XAR X-ray film (166-0760) from Eastman Kodak (Rochester, NY). ..

    Affinity Purification:

    Article Title: High concentrations of HGF inhibit skeletal muscle satellite cell proliferation in vitro by inducing expression of myostatin: a possible mechanism for reestablishing satellite cell quiescence in vivo
    Article Snippet: .. For the immunodetection of target proteins in satellite cells, the following materials were additionally used: antigen-affinity-purified goat polyclonal anti-mouse myostatin neutralizing antibody (AF788), rat monoclonal anti-mouse myostatin antibody (MAB788) and goat polyclonal anti-mouse c-met antibody (AF527) from R & D Systems; D3 mouse monoclonal antidesmin and G3G4 mouse monoclonal anti-BrdU antibodies from the Developmental Studies Hybridoma Bank (Iowa City, IA); SX118 mouse monoclonal anti-p21 (556430) and 5.8A mouse anti-MyoD antibodies (554130) from BD Biosciences (San Jose, CA); DM1A mouse monoclonal anti-chick α-tubulin antibody (T9026) from Sigma; affinity-purified biotinylated rabbit anti-goat IgG (BA-5000), horse anti-mouse IgG (BA-2000), rabbit anti-rat IgG (BA-4000) and horseradish peroxidase (HRPO)-labeled avidin kit (PK-6100) from Vector Laboratories (Burlingame, CA); affinity-purified HRPO-conjugated goat anti-mouse IgG (A-4416) and 3,3′-diaminobenzidine (DAB) from Sigma; enhanced chemiluminescence (ECL) detection kit (PRN2106) and nitrocellulose membranes (Hybond ECL, RPN2020D) from GE Healthcare (Little Chalfont, UK); biotinylated molecular weight standards (161-0319) from Bio-Rad (Hercules, CA); BIOMAX-XAR X-ray film (166-0760) from Eastman Kodak (Rochester, NY). ..

    Molecular Weight:

    Article Title: High concentrations of HGF inhibit skeletal muscle satellite cell proliferation in vitro by inducing expression of myostatin: a possible mechanism for reestablishing satellite cell quiescence in vivo
    Article Snippet: .. For the immunodetection of target proteins in satellite cells, the following materials were additionally used: antigen-affinity-purified goat polyclonal anti-mouse myostatin neutralizing antibody (AF788), rat monoclonal anti-mouse myostatin antibody (MAB788) and goat polyclonal anti-mouse c-met antibody (AF527) from R & D Systems; D3 mouse monoclonal antidesmin and G3G4 mouse monoclonal anti-BrdU antibodies from the Developmental Studies Hybridoma Bank (Iowa City, IA); SX118 mouse monoclonal anti-p21 (556430) and 5.8A mouse anti-MyoD antibodies (554130) from BD Biosciences (San Jose, CA); DM1A mouse monoclonal anti-chick α-tubulin antibody (T9026) from Sigma; affinity-purified biotinylated rabbit anti-goat IgG (BA-5000), horse anti-mouse IgG (BA-2000), rabbit anti-rat IgG (BA-4000) and horseradish peroxidase (HRPO)-labeled avidin kit (PK-6100) from Vector Laboratories (Burlingame, CA); affinity-purified HRPO-conjugated goat anti-mouse IgG (A-4416) and 3,3′-diaminobenzidine (DAB) from Sigma; enhanced chemiluminescence (ECL) detection kit (PRN2106) and nitrocellulose membranes (Hybond ECL, RPN2020D) from GE Healthcare (Little Chalfont, UK); biotinylated molecular weight standards (161-0319) from Bio-Rad (Hercules, CA); BIOMAX-XAR X-ray film (166-0760) from Eastman Kodak (Rochester, NY). ..

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    Vector Laboratories avidin biotin complex solution
    Avidin Biotin Complex Solution, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 99/100, based on 182 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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