avidin biotin peroxidase complex system  (Vector Laboratories)


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    Avidin D Peroxidase labeled Av HRP Ready to Use R T U
    Description:
    Horseradish Peroxidase Avidin ready to use reagents are powerful tools to detect or purify biotinylated proteins nucleic acids and other macromolecules Vector Laboratories enzyme conjugated avidin and streptavidin are produced with the highest specific activity enzymes in optimal ratios Specific covalent linkages are chosen to provide stable highly active conjugates Horseradish Peroxidase Avidin D HRP Avidin D is produced by our own coupling procedure which preserves the high specific activity of the peroxidase Using biotinylated primary or secondary intermediates and peroxidase labeled Avidin D antigens can be localized in histological sections cytospin preparations or smears Horseradish Peroxidase Avidin D is offered as a concentrate 5 mg ml or in a ready to use R T U stabilized solution 100ml 1 g ml in a bottle fitted with a drop dispenser top
    Catalog Number:
    a-2704
    Price:
    None
    Size:
    100 ml
    Category:
    Proteins
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    Structured Review

    Vector Laboratories avidin biotin peroxidase complex system
    Avidin D Peroxidase labeled Av HRP Ready to Use R T U
    Horseradish Peroxidase Avidin ready to use reagents are powerful tools to detect or purify biotinylated proteins nucleic acids and other macromolecules Vector Laboratories enzyme conjugated avidin and streptavidin are produced with the highest specific activity enzymes in optimal ratios Specific covalent linkages are chosen to provide stable highly active conjugates Horseradish Peroxidase Avidin D HRP Avidin D is produced by our own coupling procedure which preserves the high specific activity of the peroxidase Using biotinylated primary or secondary intermediates and peroxidase labeled Avidin D antigens can be localized in histological sections cytospin preparations or smears Horseradish Peroxidase Avidin D is offered as a concentrate 5 mg ml or in a ready to use R T U stabilized solution 100ml 1 g ml in a bottle fitted with a drop dispenser top
    https://www.bioz.com/result/avidin biotin peroxidase complex system/product/Vector Laboratories
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    Images

    1) Product Images from "PINCH: More Than Just an Adaptor Protein in Cellular Response"

    Article Title: PINCH: More Than Just an Adaptor Protein in Cellular Response

    Journal: Journal of cellular physiology

    doi: 10.1002/jcp.22437

    Immunohistological analyses of human brain glioma tissues. Immunohistochemistry was performed using the avidin–biotin–peroxidase complex system. The sections of normal human brain tissue sections, low-grade astrocytoma and glioblastoma
    Figure Legend Snippet: Immunohistological analyses of human brain glioma tissues. Immunohistochemistry was performed using the avidin–biotin–peroxidase complex system. The sections of normal human brain tissue sections, low-grade astrocytoma and glioblastoma

    Techniques Used: Immunohistochemistry, Avidin-Biotin Assay

    2) Product Images from "Regulation of T-lymphocyte motility, adhesion and de-adhesion by a cell surface mechanism directed by low density lipoprotein receptor-related protein 1 and endogenous thrombospondin-1"

    Article Title: Regulation of T-lymphocyte motility, adhesion and de-adhesion by a cell surface mechanism directed by low density lipoprotein receptor-related protein 1 and endogenous thrombospondin-1

    Journal: Immunology

    doi: 10.1111/imm.12229

    Ustekinumab inhibits CXCL12-induced T-lymphocyte motility and effects on lipoprotein receptor-related protein 1 (LRP1) and thrombospondin 1 (TSP-1). (a) The influence of ustekinumab (100 μg/ml) on migration into a collagen matrix in the absence and presence of CXCL12 (50 ng/ml) as determined after 30 min. (b) Gel analysis [4–12% SDS–PAGE (LRP1) and 6% SDS–PAGE (TSP-1)] showing the influence of ustekinumab, CXCL12 and dynasore on the cell surface expression of TSP-1 and LRP1. The cells were surface biotinylated and immunoprecipitated after 10 min. (c) Western blotting (6% SDS–PAGE) of material from lysed cells after incubation for 30 min with and without CXCL12 (50 ng/ml). (d) Western blotting of material from lysed cells using different anti-TSP-1 antibodies (Ab9 reacts with the N-terminal domain of TSP-1) after incubation for 30 min with CXCL12 (50 ng/ml). The results in (a) show mean values of three independent experiments. The results in (b–d) show one representative experiment of three to seven independent experiments.
    Figure Legend Snippet: Ustekinumab inhibits CXCL12-induced T-lymphocyte motility and effects on lipoprotein receptor-related protein 1 (LRP1) and thrombospondin 1 (TSP-1). (a) The influence of ustekinumab (100 μg/ml) on migration into a collagen matrix in the absence and presence of CXCL12 (50 ng/ml) as determined after 30 min. (b) Gel analysis [4–12% SDS–PAGE (LRP1) and 6% SDS–PAGE (TSP-1)] showing the influence of ustekinumab, CXCL12 and dynasore on the cell surface expression of TSP-1 and LRP1. The cells were surface biotinylated and immunoprecipitated after 10 min. (c) Western blotting (6% SDS–PAGE) of material from lysed cells after incubation for 30 min with and without CXCL12 (50 ng/ml). (d) Western blotting of material from lysed cells using different anti-TSP-1 antibodies (Ab9 reacts with the N-terminal domain of TSP-1) after incubation for 30 min with CXCL12 (50 ng/ml). The results in (a) show mean values of three independent experiments. The results in (b–d) show one representative experiment of three to seven independent experiments.

    Techniques Used: Migration, SDS Page, Expressing, Immunoprecipitation, Western Blot, Incubation

    Ustekinumab inhibits T-lymphocyte motility through lipoprotein receptor-related protein 1 (LRP1) and thrombospondin 1 (TSP-1). (a,b) Motility was examined with cells in the presence of ustekinumab (100 μg/ml) or infliximab (100 μg/ml on intercellular adhesion molecule 1 (10 μg/ml) (a) and fibronectin (10 μg/ml) (b) as determined by a transwell assay measuring number of transmigrated cells. (c) Formation of conjugates of AF24 T cells with antigen-presenting HLA-identical B cells in the presence of ustekinumab (100 μg/ml) or infliximab (100 μg/ml). (d) Gel analysis (6% SDS–PAGE) showing the influence of incubation with ustekinumab on the cell surface expression of TSP-1, LRP1 and CD4 after 15 min, as demonstrated by immunoprecipitation of surface biotinylated cells. (e) Quantitative immunocytochemistry showing the influence of ustekinumab (100 μg/ml) and infliximab (100 μg/ml) on cell-surface-expressed and intracellular LRP1 and TSP-1 as determined after 30 min. The cell surface expression of CD4 is shown as a comparison. (a,b) Mean values of three independent experiments and (c) one representative experiment of two independent experiments. The results in (d) and (e) show one representative experiment of three to five independent experiments.
    Figure Legend Snippet: Ustekinumab inhibits T-lymphocyte motility through lipoprotein receptor-related protein 1 (LRP1) and thrombospondin 1 (TSP-1). (a,b) Motility was examined with cells in the presence of ustekinumab (100 μg/ml) or infliximab (100 μg/ml on intercellular adhesion molecule 1 (10 μg/ml) (a) and fibronectin (10 μg/ml) (b) as determined by a transwell assay measuring number of transmigrated cells. (c) Formation of conjugates of AF24 T cells with antigen-presenting HLA-identical B cells in the presence of ustekinumab (100 μg/ml) or infliximab (100 μg/ml). (d) Gel analysis (6% SDS–PAGE) showing the influence of incubation with ustekinumab on the cell surface expression of TSP-1, LRP1 and CD4 after 15 min, as demonstrated by immunoprecipitation of surface biotinylated cells. (e) Quantitative immunocytochemistry showing the influence of ustekinumab (100 μg/ml) and infliximab (100 μg/ml) on cell-surface-expressed and intracellular LRP1 and TSP-1 as determined after 30 min. The cell surface expression of CD4 is shown as a comparison. (a,b) Mean values of three independent experiments and (c) one representative experiment of two independent experiments. The results in (d) and (e) show one representative experiment of three to five independent experiments.

    Techniques Used: Transwell Assay, SDS Page, Incubation, Expressing, Immunoprecipitation, Immunocytochemistry

    3) Product Images from "Estrogen Receptor β-Mediated Nuclear Interaction Between IRS-1 and Rad51 Inhibits Homologous Recombination Directed DNA Repair in Medulloblastoma"

    Article Title: Estrogen Receptor β-Mediated Nuclear Interaction Between IRS-1 and Rad51 Inhibits Homologous Recombination Directed DNA Repair in Medulloblastoma

    Journal: Journal of cellular physiology

    doi: 10.1002/jcp.21683

    Immunohistological analysis of human medulloblastoma biopsies. Immunohistochemistry was performed using the avidin–biotin–peroxidase complex system. The sections of normal human cerebellum and two medulloblastoma biopsies were immunolabeled with anti-IRS-1 antibody (rabbit polyclonal, Upstate Biotechnology, Temecula, CA), and anti-ERβ antibodies (rabbit polyclonal, Abcam, Cambridge, MA), and microscopic evaluation was performed under the original magnification of 1,000×.
    Figure Legend Snippet: Immunohistological analysis of human medulloblastoma biopsies. Immunohistochemistry was performed using the avidin–biotin–peroxidase complex system. The sections of normal human cerebellum and two medulloblastoma biopsies were immunolabeled with anti-IRS-1 antibody (rabbit polyclonal, Upstate Biotechnology, Temecula, CA), and anti-ERβ antibodies (rabbit polyclonal, Abcam, Cambridge, MA), and microscopic evaluation was performed under the original magnification of 1,000×.

    Techniques Used: Immunohistochemistry, Avidin-Biotin Assay, Immunolabeling

    4) Product Images from "The ?-Chemokine Receptor D6 Is Expressed by Lymphatic Endothelium and a Subset of Vascular Tumors"

    Article Title: The ?-Chemokine Receptor D6 Is Expressed by Lymphatic Endothelium and a Subset of Vascular Tumors

    Journal: The American Journal of Pathology

    doi:

    D6-immunoreactive lymphatic vessels in the gut. Paraffin-embedded sections of the gut immunostained with anti-D6 antibodies visualized using an avidin-biotin-peroxidase detection system and a peroxidase substrate producing a red stain. Representative D6 immunoreactivity associated with lymphatics in a longitudinal section of a small intestinal villus ( A ), lamina propria mucosae of the colon ( B ), a cross-section of two villi in the large intestine ( C ), muscular layer of the colon ( D ), lymphoid follicle in the lamina propria ( E ), lamina muscularis in normal appendix ( F ), and a patient with acute appendicitis ( G ). Original magnifications: ×400 ( A ), ×280 ( B ), ×530 ( C ), ×600 ( D ), ×440 ( E , F , and G ). The asterisk in D marks an immunonegative blood vessel. All sections counterstained with hematoxylin.
    Figure Legend Snippet: D6-immunoreactive lymphatic vessels in the gut. Paraffin-embedded sections of the gut immunostained with anti-D6 antibodies visualized using an avidin-biotin-peroxidase detection system and a peroxidase substrate producing a red stain. Representative D6 immunoreactivity associated with lymphatics in a longitudinal section of a small intestinal villus ( A ), lamina propria mucosae of the colon ( B ), a cross-section of two villi in the large intestine ( C ), muscular layer of the colon ( D ), lymphoid follicle in the lamina propria ( E ), lamina muscularis in normal appendix ( F ), and a patient with acute appendicitis ( G ). Original magnifications: ×400 ( A ), ×280 ( B ), ×530 ( C ), ×600 ( D ), ×440 ( E , F , and G ). The asterisk in D marks an immunonegative blood vessel. All sections counterstained with hematoxylin.

    Techniques Used: Avidin-Biotin Assay, Staining

    D6 immunoreactivity in secondary lymphoid organs. Representative images of paraffin-embedded sections from secondary lymphoid organs, immunostained with either anti-D6 ( A–D and F ), or anti-podoplanin ( E and G ), antibodies. Immunoreactivity is visualized using an avidin-biotin-peroxidase detection system and a peroxidase substrate producing a red stain; all sections counterstained with hematoxylin. A and B: D6 immunostaining in tonsils. Asterisk marks an HEV (both original magnifications, ×1,000). C: D6-immunoreactive vessel in red pulp of a spleen (original magnification, ×1,250). D–G: Lymph node. Adjacent sections showing subcapsular ( D and E ) and medullary ( F and G ) sinuses of the lymph node stained with anti-D6 ( D and F ) or anti-podoplanin ( E and G ) antibodies. Original magnifications: ×720 ( D–G ).
    Figure Legend Snippet: D6 immunoreactivity in secondary lymphoid organs. Representative images of paraffin-embedded sections from secondary lymphoid organs, immunostained with either anti-D6 ( A–D and F ), or anti-podoplanin ( E and G ), antibodies. Immunoreactivity is visualized using an avidin-biotin-peroxidase detection system and a peroxidase substrate producing a red stain; all sections counterstained with hematoxylin. A and B: D6 immunostaining in tonsils. Asterisk marks an HEV (both original magnifications, ×1,000). C: D6-immunoreactive vessel in red pulp of a spleen (original magnification, ×1,250). D–G: Lymph node. Adjacent sections showing subcapsular ( D and E ) and medullary ( F and G ) sinuses of the lymph node stained with anti-D6 ( D and F ) or anti-podoplanin ( E and G ) antibodies. Original magnifications: ×720 ( D–G ).

    Techniques Used: Avidin-Biotin Assay, Staining, Immunostaining

    5) Product Images from "Induction of Tumor-specific T Cell Immunity by Anti-DR5 Antibody Therapy"

    Article Title: Induction of Tumor-specific T Cell Immunity by Anti-DR5 Antibody Therapy

    Journal: The Journal of Experimental Medicine

    doi: 10.1084/jem.20031457

    Characterization of MD5-1 in vitro. (A) Reactivity with mouse DR5, Fas, and Fn14 transfectants and mouse tumor cell lines. The thick histograms represent MD5-1 staining and the thin histograms represent control Ig staining. (B) Cytotoxic activity of biotinylated MD5-1 against 4T1 cells in the presence (□) or absence (○) of streptavidin. (C) Cytotoxic activity of MD5-1 against 4T1 cells in the presence of P815 cells with (○) or without (□) anti-FcR mAb (2.4G2). (D) Cytotoxic activity of mTRAIL/2PK-3 against 4T1 cells in the presence of MD5-1 or anti-TRAIL mAb (N2B2). (E) Effect of z-VAD-fmk on MD5-1–mediated cytotoxicity against 4T1 tumor cells. (F) Cytotoxic activity of MD5-1 and mTRAIL/2PK3 against R331-mock and R331-FLIP cells. Similar results were obtained in two or three independent experiments.
    Figure Legend Snippet: Characterization of MD5-1 in vitro. (A) Reactivity with mouse DR5, Fas, and Fn14 transfectants and mouse tumor cell lines. The thick histograms represent MD5-1 staining and the thin histograms represent control Ig staining. (B) Cytotoxic activity of biotinylated MD5-1 against 4T1 cells in the presence (□) or absence (○) of streptavidin. (C) Cytotoxic activity of MD5-1 against 4T1 cells in the presence of P815 cells with (○) or without (□) anti-FcR mAb (2.4G2). (D) Cytotoxic activity of mTRAIL/2PK-3 against 4T1 cells in the presence of MD5-1 or anti-TRAIL mAb (N2B2). (E) Effect of z-VAD-fmk on MD5-1–mediated cytotoxicity against 4T1 tumor cells. (F) Cytotoxic activity of MD5-1 and mTRAIL/2PK3 against R331-mock and R331-FLIP cells. Similar results were obtained in two or three independent experiments.

    Techniques Used: In Vitro, Staining, Activity Assay

    6) Product Images from "Cheongsangbangpung-tang ameliorated the acute inflammatory response via the inhibition of NF-κB activation and MAPK phosphorylation"

    Article Title: Cheongsangbangpung-tang ameliorated the acute inflammatory response via the inhibition of NF-κB activation and MAPK phosphorylation

    Journal: BMC Complementary and Alternative Medicine

    doi: 10.1186/s12906-016-1501-6

    Representative immunohistochemical profiles of COX-2 and iNOS on the paw skins. Note that marked increases of COX-2 ( a )- and iNOS ( b )-positive cells were detected on the epithelium and dermis of the dorsum and ventrum pedis skin tissues in CA rats compared with normal rats, respectively. However, these increases of epidermal and dermal COX-2- and iNOS-immunolabelled cells were effectively inhibited by treatment with dexamethasone and were also dose-dependently affected by treatment with CBTE at two different dosages: 0.3 and 1.0 g/kg. Immunoreactive cells were stained using ABC methods where a = Normal; b = Carrageenan (CA); c = CA and dexamethasone; d = CA and CBTE 0.3 g/kg; e = CA and CBTE 1.0 g/kg. Scale bars = 60 μm. CBTE, Cheongsangbangpung-tang extract; DEXA, dexamethasone
    Figure Legend Snippet: Representative immunohistochemical profiles of COX-2 and iNOS on the paw skins. Note that marked increases of COX-2 ( a )- and iNOS ( b )-positive cells were detected on the epithelium and dermis of the dorsum and ventrum pedis skin tissues in CA rats compared with normal rats, respectively. However, these increases of epidermal and dermal COX-2- and iNOS-immunolabelled cells were effectively inhibited by treatment with dexamethasone and were also dose-dependently affected by treatment with CBTE at two different dosages: 0.3 and 1.0 g/kg. Immunoreactive cells were stained using ABC methods where a = Normal; b = Carrageenan (CA); c = CA and dexamethasone; d = CA and CBTE 0.3 g/kg; e = CA and CBTE 1.0 g/kg. Scale bars = 60 μm. CBTE, Cheongsangbangpung-tang extract; DEXA, dexamethasone

    Techniques Used: Immunohistochemistry, Staining

    7) Product Images from "In vivo localization of human acetylcholinesterase-derived species in a β-sheet conformation at the core of senile plaques in Alzheimer's disease"

    Article Title: In vivo localization of human acetylcholinesterase-derived species in a β-sheet conformation at the core of senile plaques in Alzheimer's disease

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.RA118.006230

    Localization and recognition of mature plaques in the brain of hAPPswe single transgenic ( A, left column ) and hAChE-S/hAPPswe double transgenic mice ( A, right column, and B ). A, frozen brain sections (12 μm) from single and double transgenic mice were single-labeled with the Elite ABC M.O.M. kit or Vectastain Elite ABC rabbit IgG kit using a biotinylated anti-mouse or anti-rabbit secondary antibody, followed by avidin-conjugated peroxidase and then the peroxidase substrate (DAB, Vector Laboratories). The scale bar represents 200 μm (in the top left brain section). Black arrowheads indicate examples of mature plaques labeled with both anti-Aβ and anti-intact or anti-domains of hAChE-S, and the blue arrowheads indicate examples of mature plaques labeled only with anti-intact or anti-domains of hAChE-S. The insets show z projections of the same mature plaque (identified by a black circle in the full brain section) labeled with each of the following antibodies: HR2, Bam10, and 105A, and the scale bar represents 50 μm. One representative whole brain section per condition was collected as a montage of automatically tiled images. B, frozen brain sections (12 μm) from double hAChE-S/hAPPswe transgenic mice were single-labeled with the Elite ABC M.O.M. kit or Vectastain Elite ABC rabbit IgG kit using a biotinylated anti-mouse or anti-rabbit secondary antibody and FITC-conjugated avidin (Vector Laboratories). Shown are fluorescent labeling of whole brain sections ( left, one representative whole brain section per condition was collected as a montage of automatically tiled images) and z projections of mature plaques (fluorescent labeling and merged phase, right ). C, mouse brain map at the rostral level, indicating the main brain regions with their sub-areas. D, shown are quantitations of the area occupied overall by the fluorescent labeling from a specific antibody/reagent in the whole brain section of hAPPswe/hAChE double transgenic ( i.e. the whole brain section shown in B ) ( top graph ), the overall intensity of the fluorescent labeling in the whole brain section of hAPPswe/hAChE double transgenic ( middle graph ), and the fold ratio when compared with ThS of each fluorescent labeling in term of area occupied and intensity ( bottom graph ).
    Figure Legend Snippet: Localization and recognition of mature plaques in the brain of hAPPswe single transgenic ( A, left column ) and hAChE-S/hAPPswe double transgenic mice ( A, right column, and B ). A, frozen brain sections (12 μm) from single and double transgenic mice were single-labeled with the Elite ABC M.O.M. kit or Vectastain Elite ABC rabbit IgG kit using a biotinylated anti-mouse or anti-rabbit secondary antibody, followed by avidin-conjugated peroxidase and then the peroxidase substrate (DAB, Vector Laboratories). The scale bar represents 200 μm (in the top left brain section). Black arrowheads indicate examples of mature plaques labeled with both anti-Aβ and anti-intact or anti-domains of hAChE-S, and the blue arrowheads indicate examples of mature plaques labeled only with anti-intact or anti-domains of hAChE-S. The insets show z projections of the same mature plaque (identified by a black circle in the full brain section) labeled with each of the following antibodies: HR2, Bam10, and 105A, and the scale bar represents 50 μm. One representative whole brain section per condition was collected as a montage of automatically tiled images. B, frozen brain sections (12 μm) from double hAChE-S/hAPPswe transgenic mice were single-labeled with the Elite ABC M.O.M. kit or Vectastain Elite ABC rabbit IgG kit using a biotinylated anti-mouse or anti-rabbit secondary antibody and FITC-conjugated avidin (Vector Laboratories). Shown are fluorescent labeling of whole brain sections ( left, one representative whole brain section per condition was collected as a montage of automatically tiled images) and z projections of mature plaques (fluorescent labeling and merged phase, right ). C, mouse brain map at the rostral level, indicating the main brain regions with their sub-areas. D, shown are quantitations of the area occupied overall by the fluorescent labeling from a specific antibody/reagent in the whole brain section of hAPPswe/hAChE double transgenic ( i.e. the whole brain section shown in B ) ( top graph ), the overall intensity of the fluorescent labeling in the whole brain section of hAPPswe/hAChE double transgenic ( middle graph ), and the fold ratio when compared with ThS of each fluorescent labeling in term of area occupied and intensity ( bottom graph ).

    Techniques Used: Transgenic Assay, Mouse Assay, Labeling, Avidin-Biotin Assay, Plasmid Preparation

    8) 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

    9) 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

    10) Product Images from "Common Hepatic Branch of Vagus Nerve-Dependent Expression of Immediate Early Genes in the Mouse Brain by Intraportal L-Arginine: Comparison with Cholecystokinin-8"

    Article Title: Common Hepatic Branch of Vagus Nerve-Dependent Expression of Immediate Early Genes in the Mouse Brain by Intraportal L-Arginine: Comparison with Cholecystokinin-8

    Journal: Frontiers in Neuroscience

    doi: 10.3389/fnins.2017.00366

    Immunostaining with anti-c-Fos antibodies of the insular cortex in brain coronal slices from Arc-dVenus mice (the slices used in Figure 2 ). The mice were intraportally injected with saline (A) , Arg ( B , 0.61 mmol/kg), and CCK ( C , 1.75 nmol/kg), and fixed at 180 min after the portal vein injection. The solid black lines indicate the area of the insular cortex, and the dotted lines indicate the border of the granular/dysgranular and agranular insular cortices. The brain slices were treated with anti-c-Fos antibodies and the signals were visualized using the avidin-biotin-peroxidase complex method. Note that c-Fos positive cells (black dots) were increased in the insular cortex of the Arg-injected mouse. Ins: insular cortex. (D) The number of c-Fos positive cells in mice intraportally injected with saline (5 slices from 5 mice), Arg ( B , 0.61 mmol/kg, 5 slices from 5 mice), and CCK ( C , 1.75 nmol/kg, 4 slices from 4 mice) at bregma levels of −0.34 and −1.06 mm. ( D inset) The data from saline-injected (3 slices from 3 mice) and CCK-injected (1.75 nmol/kg, 5 slices from 5 mice) mice. These mice were fixed at 90 min after portal vein injection. Data are shown as mean ± SEM. * P
    Figure Legend Snippet: Immunostaining with anti-c-Fos antibodies of the insular cortex in brain coronal slices from Arc-dVenus mice (the slices used in Figure 2 ). The mice were intraportally injected with saline (A) , Arg ( B , 0.61 mmol/kg), and CCK ( C , 1.75 nmol/kg), and fixed at 180 min after the portal vein injection. The solid black lines indicate the area of the insular cortex, and the dotted lines indicate the border of the granular/dysgranular and agranular insular cortices. The brain slices were treated with anti-c-Fos antibodies and the signals were visualized using the avidin-biotin-peroxidase complex method. Note that c-Fos positive cells (black dots) were increased in the insular cortex of the Arg-injected mouse. Ins: insular cortex. (D) The number of c-Fos positive cells in mice intraportally injected with saline (5 slices from 5 mice), Arg ( B , 0.61 mmol/kg, 5 slices from 5 mice), and CCK ( C , 1.75 nmol/kg, 4 slices from 4 mice) at bregma levels of −0.34 and −1.06 mm. ( D inset) The data from saline-injected (3 slices from 3 mice) and CCK-injected (1.75 nmol/kg, 5 slices from 5 mice) mice. These mice were fixed at 90 min after portal vein injection. Data are shown as mean ± SEM. * P

    Techniques Used: Immunostaining, Mouse Assay, Injection, Avidin-Biotin Assay

    11) Product Images from "CD1d Expression in Paneth Cells and Rat Exocrine Pancreas Revealed by Novel Monoclonal Antibodies Which Differentially Affect NKT Cell Activation"

    Article Title: CD1d Expression in Paneth Cells and Rat Exocrine Pancreas Revealed by Novel Monoclonal Antibodies Which Differentially Affect NKT Cell Activation

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0013089

    CD1d distribution in lymphatic and non-lymphatic organs. ABC technique with unconjugated mAb WTH-1 unless otherwise stated. (A) LEW thymus. Bar = 500 µm. (B) Longitudinal section of LEW spleen. Hemalum counterstain. Bar = 250 µm. (C) Cross-section of LEW splenic white pulp. WTH-1 biotin-conjugated primary antibody. Bar = 250 µm. (D) C57BL/6 mouse thymus. Arrows indicate cortico-medullary boundary. Biotin-conjugated antibody. Bar = 250 µm. (E) HIS57 staining in LEW splenic white pulp. Bar = 250 µm. (F) CD4 (mAb W3/25) expression in LEW spleen. Bar = 500 µm. (G) LEW liver. Bar = 250 µm. (H) LEW heart. Hemalum counterstain. Bar = 250 µm. (I) LEW ileum. The epithelium at the tips of the villi (left rim of picture) is not preserved. Biotinylated WTH-1 and hemalum counterstain. Bar = 100 µm. (J) C57BL/6 ileum. Arrows indicate CD1d positive enteroendocrine cells in the epithelium. Biotin-conjugated primary antibody, tyramide-amplified ABC technique and hemalum counterstain. Bar = 50 µm. (K) C57BL/6 CD1d −/− ileum. Biotin-conjugated primary antibody, tyramide-amplified ABC technique and hemalum counterstain. Bar = 50 µm. (L) LEW pancreas. Biotinylated WTH-1. Bar = 50 µm. (M) C57BL/6 pancreas. Biotin-conjugated primary antibody, tyramide-amplified ABC technique. and hemalum counterstain. Bar = 50 µm. (N) C57BL/6 CD1d −/− pancreas. Biotin-conjugated primary antibody, tyramide-amplified ABC technique and hemalum counterstain. Bar = 50 µm. Abbreviations in lymphatic organs: m, medulla; c, cortex; rp, red pulp; pals, periarteriolar lymphatic sheath; mz, marginal zone and f, follicle. Abbreviations in non-lymphatic organs: c, crypts; lp, lamina propria; m, smooth muscle cells of the gut wall; i, islet of Langerhans and d, interlobular duct.
    Figure Legend Snippet: CD1d distribution in lymphatic and non-lymphatic organs. ABC technique with unconjugated mAb WTH-1 unless otherwise stated. (A) LEW thymus. Bar = 500 µm. (B) Longitudinal section of LEW spleen. Hemalum counterstain. Bar = 250 µm. (C) Cross-section of LEW splenic white pulp. WTH-1 biotin-conjugated primary antibody. Bar = 250 µm. (D) C57BL/6 mouse thymus. Arrows indicate cortico-medullary boundary. Biotin-conjugated antibody. Bar = 250 µm. (E) HIS57 staining in LEW splenic white pulp. Bar = 250 µm. (F) CD4 (mAb W3/25) expression in LEW spleen. Bar = 500 µm. (G) LEW liver. Bar = 250 µm. (H) LEW heart. Hemalum counterstain. Bar = 250 µm. (I) LEW ileum. The epithelium at the tips of the villi (left rim of picture) is not preserved. Biotinylated WTH-1 and hemalum counterstain. Bar = 100 µm. (J) C57BL/6 ileum. Arrows indicate CD1d positive enteroendocrine cells in the epithelium. Biotin-conjugated primary antibody, tyramide-amplified ABC technique and hemalum counterstain. Bar = 50 µm. (K) C57BL/6 CD1d −/− ileum. Biotin-conjugated primary antibody, tyramide-amplified ABC technique and hemalum counterstain. Bar = 50 µm. (L) LEW pancreas. Biotinylated WTH-1. Bar = 50 µm. (M) C57BL/6 pancreas. Biotin-conjugated primary antibody, tyramide-amplified ABC technique. and hemalum counterstain. Bar = 50 µm. (N) C57BL/6 CD1d −/− pancreas. Biotin-conjugated primary antibody, tyramide-amplified ABC technique and hemalum counterstain. Bar = 50 µm. Abbreviations in lymphatic organs: m, medulla; c, cortex; rp, red pulp; pals, periarteriolar lymphatic sheath; mz, marginal zone and f, follicle. Abbreviations in non-lymphatic organs: c, crypts; lp, lamina propria; m, smooth muscle cells of the gut wall; i, islet of Langerhans and d, interlobular duct.

    Techniques Used: Staining, Expressing, Amplification

    12) Product Images from "Immunoglobulin M Capture Assay for Serologic Confirmation of Early Lyme Disease: Analysis of Immune Complexes with Biotinylated Borrelia burgdorferi Sonicate Enhanced with Flagellin Peptide Epitope"

    Article Title: Immunoglobulin M Capture Assay for Serologic Confirmation of Early Lyme Disease: Analysis of Immune Complexes with Biotinylated Borrelia burgdorferi Sonicate Enhanced with Flagellin Peptide Epitope

    Journal: Journal of Clinical Microbiology

    doi:

    Influence of synthetic epitope flagellin antigen on free and IC-derived L antibodies to B. burgdorferi . Serum samples from patients containing IC-derived antibody (precipitated with PEG and resuspended in PEG) assayed with biotinylated whole-cell sonicate (Bb-bio) alone (a), serum samples containing IC-derived antibody assayed with biotinylated whole-cell sonicate (Bb-bio) plus biotinylated flagellin synthetic epitope-BSA conjugate (Fla-bio) (b), serum samples containing free (untreated) antibody assayed with biotinylated whole-cell sonicate (Bb-bio) alone (c), and serum samples containing free (untreated) antibody assayed with biotinylated whole-cell sonicate (Bb-bio) plus biotinylated flagellin synthetic epitope-BSA conjugate (Fla-bio) (d) as the antigen source were used to detect LD-specific IgM antibodies in M-capture ELISA. Results are expressed as an index value, as defined in Materials and Methods.
    Figure Legend Snippet: Influence of synthetic epitope flagellin antigen on free and IC-derived L antibodies to B. burgdorferi . Serum samples from patients containing IC-derived antibody (precipitated with PEG and resuspended in PEG) assayed with biotinylated whole-cell sonicate (Bb-bio) alone (a), serum samples containing IC-derived antibody assayed with biotinylated whole-cell sonicate (Bb-bio) plus biotinylated flagellin synthetic epitope-BSA conjugate (Fla-bio) (b), serum samples containing free (untreated) antibody assayed with biotinylated whole-cell sonicate (Bb-bio) alone (c), and serum samples containing free (untreated) antibody assayed with biotinylated whole-cell sonicate (Bb-bio) plus biotinylated flagellin synthetic epitope-BSA conjugate (Fla-bio) (d) as the antigen source were used to detect LD-specific IgM antibodies in M-capture ELISA. Results are expressed as an index value, as defined in Materials and Methods.

    Techniques Used: Derivative Assay, Enzyme-linked Immunosorbent Assay

    Influence of synthetic flagellin epitope (unprocessed serum). Serum samples from patients were assayed for LD (Lyme specific IgM antibodies) by M-capture ELISA. Either the biotinylated whole-cell sonicate (Bb-bio) alone (a), the biotinylated whole-cell sonicate (Bb-bio) plus biotinylated flagellin synthetic epitope-BSA conjugate (Fla-bio) (b), or the biotinylated flagellin synthetic epitope-BSA conjugate (Fla-bio) alone (c) was used as the antigen source. Results are expressed as net mean OD 450 , as defined in Materials and Methods. The sets of bars represent data for samples from patients 7, 1 (22 May 1997), 1 (23 May 1997), 2 to 5 and 95-11891 from left to right, respectively.
    Figure Legend Snippet: Influence of synthetic flagellin epitope (unprocessed serum). Serum samples from patients were assayed for LD (Lyme specific IgM antibodies) by M-capture ELISA. Either the biotinylated whole-cell sonicate (Bb-bio) alone (a), the biotinylated whole-cell sonicate (Bb-bio) plus biotinylated flagellin synthetic epitope-BSA conjugate (Fla-bio) (b), or the biotinylated flagellin synthetic epitope-BSA conjugate (Fla-bio) alone (c) was used as the antigen source. Results are expressed as net mean OD 450 , as defined in Materials and Methods. The sets of bars represent data for samples from patients 7, 1 (22 May 1997), 1 (23 May 1997), 2 to 5 and 95-11891 from left to right, respectively.

    Techniques Used: Enzyme-linked Immunosorbent Assay

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    Purification:

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    Avidin-Biotin Assay:

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    Vector Laboratories avidin biotin peroxidase complex system
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    Immunohistological analyses of human brain glioma tissues. Immunohistochemistry was performed using the avidin–biotin–peroxidase complex system. The sections of normal human brain tissue sections, low-grade astrocytoma and glioblastoma

    Journal: Journal of cellular physiology

    Article Title: PINCH: More Than Just an Adaptor Protein in Cellular Response

    doi: 10.1002/jcp.22437

    Figure Lengend Snippet: Immunohistological analyses of human brain glioma tissues. Immunohistochemistry was performed using the avidin–biotin–peroxidase complex system. The sections of normal human brain tissue sections, low-grade astrocytoma and glioblastoma

    Article Snippet: Immunohistochemistry was performed using the avidin–biotin–peroxidase complex system, according to the manufacturer's instructions (Vectastain Elite ABC Peroxidase Kit; Vector Laboratories, Burlingame, CA).

    Techniques: Immunohistochemistry, Avidin-Biotin Assay

    Ustekinumab inhibits CXCL12-induced T-lymphocyte motility and effects on lipoprotein receptor-related protein 1 (LRP1) and thrombospondin 1 (TSP-1). (a) The influence of ustekinumab (100 μg/ml) on migration into a collagen matrix in the absence and presence of CXCL12 (50 ng/ml) as determined after 30 min. (b) Gel analysis [4–12% SDS–PAGE (LRP1) and 6% SDS–PAGE (TSP-1)] showing the influence of ustekinumab, CXCL12 and dynasore on the cell surface expression of TSP-1 and LRP1. The cells were surface biotinylated and immunoprecipitated after 10 min. (c) Western blotting (6% SDS–PAGE) of material from lysed cells after incubation for 30 min with and without CXCL12 (50 ng/ml). (d) Western blotting of material from lysed cells using different anti-TSP-1 antibodies (Ab9 reacts with the N-terminal domain of TSP-1) after incubation for 30 min with CXCL12 (50 ng/ml). The results in (a) show mean values of three independent experiments. The results in (b–d) show one representative experiment of three to seven independent experiments.

    Journal: Immunology

    Article Title: Regulation of T-lymphocyte motility, adhesion and de-adhesion by a cell surface mechanism directed by low density lipoprotein receptor-related protein 1 and endogenous thrombospondin-1

    doi: 10.1111/imm.12229

    Figure Lengend Snippet: Ustekinumab inhibits CXCL12-induced T-lymphocyte motility and effects on lipoprotein receptor-related protein 1 (LRP1) and thrombospondin 1 (TSP-1). (a) The influence of ustekinumab (100 μg/ml) on migration into a collagen matrix in the absence and presence of CXCL12 (50 ng/ml) as determined after 30 min. (b) Gel analysis [4–12% SDS–PAGE (LRP1) and 6% SDS–PAGE (TSP-1)] showing the influence of ustekinumab, CXCL12 and dynasore on the cell surface expression of TSP-1 and LRP1. The cells were surface biotinylated and immunoprecipitated after 10 min. (c) Western blotting (6% SDS–PAGE) of material from lysed cells after incubation for 30 min with and without CXCL12 (50 ng/ml). (d) Western blotting of material from lysed cells using different anti-TSP-1 antibodies (Ab9 reacts with the N-terminal domain of TSP-1) after incubation for 30 min with CXCL12 (50 ng/ml). The results in (a) show mean values of three independent experiments. The results in (b–d) show one representative experiment of three to seven independent experiments.

    Article Snippet: Biotinylated peroxidase and avidin were from Vector Laboratories (Burlingame, CA).

    Techniques: Migration, SDS Page, Expressing, Immunoprecipitation, Western Blot, Incubation

    Ustekinumab inhibits T-lymphocyte motility through lipoprotein receptor-related protein 1 (LRP1) and thrombospondin 1 (TSP-1). (a,b) Motility was examined with cells in the presence of ustekinumab (100 μg/ml) or infliximab (100 μg/ml on intercellular adhesion molecule 1 (10 μg/ml) (a) and fibronectin (10 μg/ml) (b) as determined by a transwell assay measuring number of transmigrated cells. (c) Formation of conjugates of AF24 T cells with antigen-presenting HLA-identical B cells in the presence of ustekinumab (100 μg/ml) or infliximab (100 μg/ml). (d) Gel analysis (6% SDS–PAGE) showing the influence of incubation with ustekinumab on the cell surface expression of TSP-1, LRP1 and CD4 after 15 min, as demonstrated by immunoprecipitation of surface biotinylated cells. (e) Quantitative immunocytochemistry showing the influence of ustekinumab (100 μg/ml) and infliximab (100 μg/ml) on cell-surface-expressed and intracellular LRP1 and TSP-1 as determined after 30 min. The cell surface expression of CD4 is shown as a comparison. (a,b) Mean values of three independent experiments and (c) one representative experiment of two independent experiments. The results in (d) and (e) show one representative experiment of three to five independent experiments.

    Journal: Immunology

    Article Title: Regulation of T-lymphocyte motility, adhesion and de-adhesion by a cell surface mechanism directed by low density lipoprotein receptor-related protein 1 and endogenous thrombospondin-1

    doi: 10.1111/imm.12229

    Figure Lengend Snippet: Ustekinumab inhibits T-lymphocyte motility through lipoprotein receptor-related protein 1 (LRP1) and thrombospondin 1 (TSP-1). (a,b) Motility was examined with cells in the presence of ustekinumab (100 μg/ml) or infliximab (100 μg/ml on intercellular adhesion molecule 1 (10 μg/ml) (a) and fibronectin (10 μg/ml) (b) as determined by a transwell assay measuring number of transmigrated cells. (c) Formation of conjugates of AF24 T cells with antigen-presenting HLA-identical B cells in the presence of ustekinumab (100 μg/ml) or infliximab (100 μg/ml). (d) Gel analysis (6% SDS–PAGE) showing the influence of incubation with ustekinumab on the cell surface expression of TSP-1, LRP1 and CD4 after 15 min, as demonstrated by immunoprecipitation of surface biotinylated cells. (e) Quantitative immunocytochemistry showing the influence of ustekinumab (100 μg/ml) and infliximab (100 μg/ml) on cell-surface-expressed and intracellular LRP1 and TSP-1 as determined after 30 min. The cell surface expression of CD4 is shown as a comparison. (a,b) Mean values of three independent experiments and (c) one representative experiment of two independent experiments. The results in (d) and (e) show one representative experiment of three to five independent experiments.

    Article Snippet: Biotinylated peroxidase and avidin were from Vector Laboratories (Burlingame, CA).

    Techniques: Transwell Assay, SDS Page, Incubation, Expressing, Immunoprecipitation, Immunocytochemistry

    Immunohistological analysis of human medulloblastoma biopsies. Immunohistochemistry was performed using the avidin–biotin–peroxidase complex system. The sections of normal human cerebellum and two medulloblastoma biopsies were immunolabeled with anti-IRS-1 antibody (rabbit polyclonal, Upstate Biotechnology, Temecula, CA), and anti-ERβ antibodies (rabbit polyclonal, Abcam, Cambridge, MA), and microscopic evaluation was performed under the original magnification of 1,000×.

    Journal: Journal of cellular physiology

    Article Title: Estrogen Receptor β-Mediated Nuclear Interaction Between IRS-1 and Rad51 Inhibits Homologous Recombination Directed DNA Repair in Medulloblastoma

    doi: 10.1002/jcp.21683

    Figure Lengend Snippet: Immunohistological analysis of human medulloblastoma biopsies. Immunohistochemistry was performed using the avidin–biotin–peroxidase complex system. The sections of normal human cerebellum and two medulloblastoma biopsies were immunolabeled with anti-IRS-1 antibody (rabbit polyclonal, Upstate Biotechnology, Temecula, CA), and anti-ERβ antibodies (rabbit polyclonal, Abcam, Cambridge, MA), and microscopic evaluation was performed under the original magnification of 1,000×.

    Article Snippet: Immunohistochemistry was performed using the avidin–biotin–peroxidase complex system, according to the manufacturer’s instructions (Vectastain Elite ABC Peroxidase Kit; Vector Laboratories, Burlingame, CA).

    Techniques: Immunohistochemistry, Avidin-Biotin Assay, Immunolabeling

    D6-immunoreactive lymphatic vessels in the gut. Paraffin-embedded sections of the gut immunostained with anti-D6 antibodies visualized using an avidin-biotin-peroxidase detection system and a peroxidase substrate producing a red stain. Representative D6 immunoreactivity associated with lymphatics in a longitudinal section of a small intestinal villus ( A ), lamina propria mucosae of the colon ( B ), a cross-section of two villi in the large intestine ( C ), muscular layer of the colon ( D ), lymphoid follicle in the lamina propria ( E ), lamina muscularis in normal appendix ( F ), and a patient with acute appendicitis ( G ). Original magnifications: ×400 ( A ), ×280 ( B ), ×530 ( C ), ×600 ( D ), ×440 ( E , F , and G ). The asterisk in D marks an immunonegative blood vessel. All sections counterstained with hematoxylin.

    Journal: The American Journal of Pathology

    Article Title: The ?-Chemokine Receptor D6 Is Expressed by Lymphatic Endothelium and a Subset of Vascular Tumors

    doi:

    Figure Lengend Snippet: D6-immunoreactive lymphatic vessels in the gut. Paraffin-embedded sections of the gut immunostained with anti-D6 antibodies visualized using an avidin-biotin-peroxidase detection system and a peroxidase substrate producing a red stain. Representative D6 immunoreactivity associated with lymphatics in a longitudinal section of a small intestinal villus ( A ), lamina propria mucosae of the colon ( B ), a cross-section of two villi in the large intestine ( C ), muscular layer of the colon ( D ), lymphoid follicle in the lamina propria ( E ), lamina muscularis in normal appendix ( F ), and a patient with acute appendicitis ( G ). Original magnifications: ×400 ( A ), ×280 ( B ), ×530 ( C ), ×600 ( D ), ×440 ( E , F , and G ). The asterisk in D marks an immunonegative blood vessel. All sections counterstained with hematoxylin.

    Article Snippet: The bound antibodies were detected using the Vector avidin-biotin-peroxidase detection system and Nova-Red substrate (Vector Laboratories, Peterborough, UK), according to the manufacturers instructions.

    Techniques: Avidin-Biotin Assay, Staining

    D6 immunoreactivity in secondary lymphoid organs. Representative images of paraffin-embedded sections from secondary lymphoid organs, immunostained with either anti-D6 ( A–D and F ), or anti-podoplanin ( E and G ), antibodies. Immunoreactivity is visualized using an avidin-biotin-peroxidase detection system and a peroxidase substrate producing a red stain; all sections counterstained with hematoxylin. A and B: D6 immunostaining in tonsils. Asterisk marks an HEV (both original magnifications, ×1,000). C: D6-immunoreactive vessel in red pulp of a spleen (original magnification, ×1,250). D–G: Lymph node. Adjacent sections showing subcapsular ( D and E ) and medullary ( F and G ) sinuses of the lymph node stained with anti-D6 ( D and F ) or anti-podoplanin ( E and G ) antibodies. Original magnifications: ×720 ( D–G ).

    Journal: The American Journal of Pathology

    Article Title: The ?-Chemokine Receptor D6 Is Expressed by Lymphatic Endothelium and a Subset of Vascular Tumors

    doi:

    Figure Lengend Snippet: D6 immunoreactivity in secondary lymphoid organs. Representative images of paraffin-embedded sections from secondary lymphoid organs, immunostained with either anti-D6 ( A–D and F ), or anti-podoplanin ( E and G ), antibodies. Immunoreactivity is visualized using an avidin-biotin-peroxidase detection system and a peroxidase substrate producing a red stain; all sections counterstained with hematoxylin. A and B: D6 immunostaining in tonsils. Asterisk marks an HEV (both original magnifications, ×1,000). C: D6-immunoreactive vessel in red pulp of a spleen (original magnification, ×1,250). D–G: Lymph node. Adjacent sections showing subcapsular ( D and E ) and medullary ( F and G ) sinuses of the lymph node stained with anti-D6 ( D and F ) or anti-podoplanin ( E and G ) antibodies. Original magnifications: ×720 ( D–G ).

    Article Snippet: The bound antibodies were detected using the Vector avidin-biotin-peroxidase detection system and Nova-Red substrate (Vector Laboratories, Peterborough, UK), according to the manufacturers instructions.

    Techniques: Avidin-Biotin Assay, Staining, Immunostaining