biocytin  (Vector Laboratories)


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    Name:
    VECTASTAIN ABC HRP Kit Peroxidase Standard
    Description:
    VECTASTAIN ABC Peroxidase Staining Kit has more than 50 000 citations to its credit and remains widely popular Based on the versatile avidin biotin complex interaction the system is modular and along with our selection of secondary antibodies can accommodate a wide array of primary antibody and tissue species Our ABC kits are economical and continue to be a staple product in any immunohistochemistry IHC and immunocytochemistry ICC laboratory Peroxidase substrates produce sharp dense precipitates with crisp localization These characteristics in conjunction with the high sensitivity and low background of the VECTASTAIN ABC systems make the peroxidase enzyme a preferred choice in many applications eg In neural tissue the peroxidase system is often preferred because it gives more consistent labeling of both cell bodies and processes Original VECTASTAIN ABC Kit Good sensitivity low backgroundOriginal avidin biotin ABC complex formulationLow costAvailable without Standard kit or with biotinylated species specific secondary antibody Kit Contents 2 ml Reagent A2 ml Reagent BReagents A and B form the ABC enzyme complex The Avidin Biotin Complex MethodThe VECTASTAIN ABC systems are extremely sensitive due to the form and number of active enzyme molecules associated with the preformed Avidin Biotinylated enzyme Complex This ABC complex takes advantage of two important properties of avidin 1 an extraordinarily high affinity for biotin over one million times higher than antibody for most antigens and 2 four biotin binding sites These properties allow macromolecular complexes ABCs to be formed by mixing Avidin DH Reagent A with its paired biotinylated enzyme Reagent B prior to use The ABC reagent once formed remains stable for many hours after formation and can be used for several days after preparation The VECTASTAIN ABC Reagent can be used to detect any molecule that is biotinylated This property gives the avidin biotin complex ABC method great versatility in the types of targets that can be detected as well as the types of applications in which it can be employed Biotinylated primary antibodies secondaries lectins neuronal tracers nucleic acids and ligands can be effectively visualized in applications such as Tissue stainingMultiple labeling Multiplex IHC Western blottingSouthern and northern blottingIn situ hybridization detection ISH Enzyme immunoassays ELISA Neuronal tracingAll applications benefit from the high sensitivity low background reproducibility and economy of the VECTASTAIN ABC system
    Catalog Number:
    pk-4000
    Price:
    None
    Size:
    1 Kit
    Category:
    Protein chromogenic detection reagents or kits or substrates
    Reactivity:
    No antibody included
    Buy from Supplier


    Structured Review

    Vector Laboratories biocytin
    VECTASTAIN ABC HRP Kit Peroxidase Standard
    VECTASTAIN ABC Peroxidase Staining Kit has more than 50 000 citations to its credit and remains widely popular Based on the versatile avidin biotin complex interaction the system is modular and along with our selection of secondary antibodies can accommodate a wide array of primary antibody and tissue species Our ABC kits are economical and continue to be a staple product in any immunohistochemistry IHC and immunocytochemistry ICC laboratory Peroxidase substrates produce sharp dense precipitates with crisp localization These characteristics in conjunction with the high sensitivity and low background of the VECTASTAIN ABC systems make the peroxidase enzyme a preferred choice in many applications eg In neural tissue the peroxidase system is often preferred because it gives more consistent labeling of both cell bodies and processes Original VECTASTAIN ABC Kit Good sensitivity low backgroundOriginal avidin biotin ABC complex formulationLow costAvailable without Standard kit or with biotinylated species specific secondary antibody Kit Contents 2 ml Reagent A2 ml Reagent BReagents A and B form the ABC enzyme complex The Avidin Biotin Complex MethodThe VECTASTAIN ABC systems are extremely sensitive due to the form and number of active enzyme molecules associated with the preformed Avidin Biotinylated enzyme Complex This ABC complex takes advantage of two important properties of avidin 1 an extraordinarily high affinity for biotin over one million times higher than antibody for most antigens and 2 four biotin binding sites These properties allow macromolecular complexes ABCs to be formed by mixing Avidin DH Reagent A with its paired biotinylated enzyme Reagent B prior to use The ABC reagent once formed remains stable for many hours after formation and can be used for several days after preparation The VECTASTAIN ABC Reagent can be used to detect any molecule that is biotinylated This property gives the avidin biotin complex ABC method great versatility in the types of targets that can be detected as well as the types of applications in which it can be employed Biotinylated primary antibodies secondaries lectins neuronal tracers nucleic acids and ligands can be effectively visualized in applications such as Tissue stainingMultiple labeling Multiplex IHC Western blottingSouthern and northern blottingIn situ hybridization detection ISH Enzyme immunoassays ELISA Neuronal tracingAll applications benefit from the high sensitivity low background reproducibility and economy of the VECTASTAIN ABC system
    https://www.bioz.com/result/biocytin/product/Vector Laboratories
    Average 92 stars, based on 5635 article reviews
    Price from $9.99 to $1999.99
    biocytin - by Bioz Stars, 2020-09
    92/100 stars

    Images

    1) Product Images from "Distinct deep short-axon cell subtypes of the main olfactory bulb provide novel intra- and extrabulbar GABAergic connections"

    Article Title: Distinct deep short-axon cell subtypes of the main olfactory bulb provide novel intra- and extrabulbar GABAergic connections

    Journal: The Journal of neuroscience : the official journal of the Society for Neuroscience

    doi: 10.1523/JNEUROSCI.2490-08.2008

    Deep short-axon cell subtypes selectively innervate other GABAergic interneurons. A , Electron micrograph showing an axon bouton (b; black DAB precipitate) of a biocytin-filled GL-dSAC (MA324) forming a symmetrical synapse (arrowhead) onto the soma of
    Figure Legend Snippet: Deep short-axon cell subtypes selectively innervate other GABAergic interneurons. A , Electron micrograph showing an axon bouton (b; black DAB precipitate) of a biocytin-filled GL-dSAC (MA324) forming a symmetrical synapse (arrowhead) onto the soma of

    Techniques Used:

    Deep short-axon cells are GABAergic. A 1 , A 2 , Serial ultrathin sections of a bouton (b) of a biocytin-filled (large silver-enhanced particles in A 1 ) GL-dSAC (MA633) in the GL. The GABA immunopositive bouton (small gold particles in A 2 ) forms a symmetrical
    Figure Legend Snippet: Deep short-axon cells are GABAergic. A 1 , A 2 , Serial ultrathin sections of a bouton (b) of a biocytin-filled (large silver-enhanced particles in A 1 ) GL-dSAC (MA633) in the GL. The GABA immunopositive bouton (small gold particles in A 2 ) forms a symmetrical

    Techniques Used:

    2) Product Images from "D1-Like Dopamine Receptor Activation Modulates GABAergic Inhibition But Not Electrical Coupling between Neocortical Fast-Spiking Interneurons"

    Article Title: D1-Like Dopamine Receptor Activation Modulates GABAergic Inhibition But Not Electrical Coupling between Neocortical Fast-Spiking Interneurons

    Journal: The Journal of neuroscience : the official journal of the Society for Neuroscience

    doi: 10.1523/JNEUROSCI.5079-07.2008

    Morphological and physiological characteristics of EGFP-expressing FS interneurons in mouse neocortex. A , Neurolucida reconstruction of a pair of biocytin-filled FS cells that were reciprocally connected by GABAergic synapses and electrically coupled via gap junctions. Cell 1 axon, Light blue; dendrites, dark blue; cell 2 axon, light red; dendrites, dark red. B , Firing patterns of each cell in response to low- and high-intensity suprathreshold current injection. C , Single short-duration FS cell action potential, followed by prominent afterhyperpolarization. D , Expanded trace from hatched box in B showing rhythmic subthresh-old membrane potential oscillations typical of quiescent periods between epochs of high-frequency discharge. E , ISI for cell 1 from the middle trace in B .
    Figure Legend Snippet: Morphological and physiological characteristics of EGFP-expressing FS interneurons in mouse neocortex. A , Neurolucida reconstruction of a pair of biocytin-filled FS cells that were reciprocally connected by GABAergic synapses and electrically coupled via gap junctions. Cell 1 axon, Light blue; dendrites, dark blue; cell 2 axon, light red; dendrites, dark red. B , Firing patterns of each cell in response to low- and high-intensity suprathreshold current injection. C , Single short-duration FS cell action potential, followed by prominent afterhyperpolarization. D , Expanded trace from hatched box in B showing rhythmic subthresh-old membrane potential oscillations typical of quiescent periods between epochs of high-frequency discharge. E , ISI for cell 1 from the middle trace in B .

    Techniques Used: Expressing, Injection

    3) Product Images from "The impact of low-magnitude high-frequency vibration on fracture healing is profoundly influenced by the oestrogen status in mice"

    Article Title: The impact of low-magnitude high-frequency vibration on fracture healing is profoundly influenced by the oestrogen status in mice

    Journal: Disease Models & Mechanisms

    doi: 10.1242/dmm.018622

    Effects of LMHFV on bone healing in OVX mice 10 and 21 days after osteotomy. LMHFV significantly improved fracture healing and increased ERα ( Esr1 ) and Bglap expression. The dashed lines indicate the values of aged-matched non-OVX mice. (A) Flexural rigidity (EI) of the fracture callus after 21 days. (B) Total callus volume (TV) as assessed by μCT. (C) Bone volume/total volume (BV/TV) as assessed by μCT. (D) Callus composition on day 10 as assessed by histomorphometry, given as a percentage of the total callus area. Bone, TOT; cartilage, Cg; and fibrous tissue, FT. (E) Callus composition on day 21 as assessed by histomorphometry. (F) Percentage of mice with bony bridging of the fracture gap. (G) Gene expression in vibrated OVX versus non-vibrated OVX mice as assessed by qPCR, n =6. The dashed line indicates the level at which there is no difference in expression. (H,I) Representative immunohistological images of the periosteal fracture callus of non-vibrated and vibrated OVX mice. Immunostaining for ERα (H) and osteocalcin (I). Scale bars: 100 μm. * P
    Figure Legend Snippet: Effects of LMHFV on bone healing in OVX mice 10 and 21 days after osteotomy. LMHFV significantly improved fracture healing and increased ERα ( Esr1 ) and Bglap expression. The dashed lines indicate the values of aged-matched non-OVX mice. (A) Flexural rigidity (EI) of the fracture callus after 21 days. (B) Total callus volume (TV) as assessed by μCT. (C) Bone volume/total volume (BV/TV) as assessed by μCT. (D) Callus composition on day 10 as assessed by histomorphometry, given as a percentage of the total callus area. Bone, TOT; cartilage, Cg; and fibrous tissue, FT. (E) Callus composition on day 21 as assessed by histomorphometry. (F) Percentage of mice with bony bridging of the fracture gap. (G) Gene expression in vibrated OVX versus non-vibrated OVX mice as assessed by qPCR, n =6. The dashed line indicates the level at which there is no difference in expression. (H,I) Representative immunohistological images of the periosteal fracture callus of non-vibrated and vibrated OVX mice. Immunostaining for ERα (H) and osteocalcin (I). Scale bars: 100 μm. * P

    Techniques Used: Mouse Assay, Expressing, Real-time Polymerase Chain Reaction, Immunostaining

    4) 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

    5) 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:

    6) Product Images from "Casticin inhibits breast cancer cell migration and invasion by down-regulation of PI3K/Akt signaling pathway"

    Article Title: Casticin inhibits breast cancer cell migration and invasion by down-regulation of PI3K/Akt signaling pathway

    Journal: Bioscience Reports

    doi: 10.1042/BSR20180738

    Effects of casticin on the activity and expression of MMP-2/9 ( A ) MDA-MB-231 and 4T1 cells were respectively treated with 0, 0.25, and 0.50 µM of casticin for 24 h, and the culture medium was then subjected to gelatin zymography to analyze the activity of MMP-2/9. ( B ) The activity of MMP-2/9 was separately quantitated as described in the ‘Materials and methods’ section, and normalized to that of the control. ( C ) The mRNA levels of MMP-2/9 were determined with real-time quantitative RT-PCR after the cells were incubated with 0, 0.25, and 0.50 µM of casticin for 24 h. ( D ) Western blot analysis of the protein levels of MMP-2/9 in the cells treated with 0, 0.25, and 0.50 µM of casticin for 24 h. β-actin served as an internal control for the protein level. ( E ) The relative protein levels of MMP-2/9 were quantitated against the densitometric signal of the β-actin bands. Data are expressed as the mean ± S.D. of three independent experiments. * P
    Figure Legend Snippet: Effects of casticin on the activity and expression of MMP-2/9 ( A ) MDA-MB-231 and 4T1 cells were respectively treated with 0, 0.25, and 0.50 µM of casticin for 24 h, and the culture medium was then subjected to gelatin zymography to analyze the activity of MMP-2/9. ( B ) The activity of MMP-2/9 was separately quantitated as described in the ‘Materials and methods’ section, and normalized to that of the control. ( C ) The mRNA levels of MMP-2/9 were determined with real-time quantitative RT-PCR after the cells were incubated with 0, 0.25, and 0.50 µM of casticin for 24 h. ( D ) Western blot analysis of the protein levels of MMP-2/9 in the cells treated with 0, 0.25, and 0.50 µM of casticin for 24 h. β-actin served as an internal control for the protein level. ( E ) The relative protein levels of MMP-2/9 were quantitated against the densitometric signal of the β-actin bands. Data are expressed as the mean ± S.D. of three independent experiments. * P

    Techniques Used: Activity Assay, Expressing, Multiple Displacement Amplification, Zymography, Quantitative RT-PCR, Incubation, Western Blot

    7) 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

    8) Product Images from "The impact of low-magnitude high-frequency vibration on fracture healing is profoundly influenced by the oestrogen status in mice"

    Article Title: The impact of low-magnitude high-frequency vibration on fracture healing is profoundly influenced by the oestrogen status in mice

    Journal: Disease Models & Mechanisms

    doi: 10.1242/dmm.018622

    Effects of OVX on bone healing 10 and 21 days after osteotomy. OVX significantly impaired fracture healing, increased ERβ expression and inhibited Wnt/β-catenin signalling. (A) Flexural rigidity (EI) of the fracture callus after 21 days. (B) Total callus volume (TV) as assessed by using μCT. (C) Bone volume/total volume (BV/TV) as assessed by using μCT. (D) Callus composition on day 10 as assessed by histomorphometry, given as a percentage of the total callus area. Bone, TOT; cartilage, Cg; and fibrous tissue, FT. (E) Callus composition on day 21 assessed by histomorphometry. (F) Percentage of mice with bony bridging of the fracture gap. (G) Gene expression in OVX versus non-OVX mice as assessed by qPCR. The dashed line indicates the level at which there is no difference in expression. * P
    Figure Legend Snippet: Effects of OVX on bone healing 10 and 21 days after osteotomy. OVX significantly impaired fracture healing, increased ERβ expression and inhibited Wnt/β-catenin signalling. (A) Flexural rigidity (EI) of the fracture callus after 21 days. (B) Total callus volume (TV) as assessed by using μCT. (C) Bone volume/total volume (BV/TV) as assessed by using μCT. (D) Callus composition on day 10 as assessed by histomorphometry, given as a percentage of the total callus area. Bone, TOT; cartilage, Cg; and fibrous tissue, FT. (E) Callus composition on day 21 assessed by histomorphometry. (F) Percentage of mice with bony bridging of the fracture gap. (G) Gene expression in OVX versus non-OVX mice as assessed by qPCR. The dashed line indicates the level at which there is no difference in expression. * P

    Techniques Used: Expressing, Mouse Assay, Real-time Polymerase Chain Reaction

    Representative immunohistological images of the periosteal fracture callus. Upper row, non-vibrated non-OVX mouse; middle row, vibrated non-OVX mouse; bottom row, non-vibrated OVX mouse. Immunostaining for ERβ (A), sclerostin (B) and β-catenin (C). Scale bars: 100 μm.
    Figure Legend Snippet: Representative immunohistological images of the periosteal fracture callus. Upper row, non-vibrated non-OVX mouse; middle row, vibrated non-OVX mouse; bottom row, non-vibrated OVX mouse. Immunostaining for ERβ (A), sclerostin (B) and β-catenin (C). Scale bars: 100 μm.

    Techniques Used: Immunostaining

    Effects of LMHFV on bone healing in non-OVX mice at 10 and 21 days after osteotomy. LMHFV significantly impaired fracture healing, increased ERβ expression and inhibited Wnt/β-catenin signalling. (A) Flexural rigidity (EI) of the fracture callus after 21 days. (B) Total callus volume (TV) as assessed by μCT. (C) Bone volume/total volume (BV/TV) as assessed by μCT. (D) Callus composition on day 10 as assessed by histomorphometry, given as a percentage of the total callus area. Bone, TOT; cartilage, Cg; and fibrous tissue, FT. (E) Callus composition on day 21 as assessed by histomorphometry. (F) Percentage of mice with bony bridging of the fracture gap. (G) Gene expression in vibrated non-OVX mice versus non-vibrated non-OVX mice as assessed by qPCR. The dashed line indicates the level at which there is no difference in expression. * P
    Figure Legend Snippet: Effects of LMHFV on bone healing in non-OVX mice at 10 and 21 days after osteotomy. LMHFV significantly impaired fracture healing, increased ERβ expression and inhibited Wnt/β-catenin signalling. (A) Flexural rigidity (EI) of the fracture callus after 21 days. (B) Total callus volume (TV) as assessed by μCT. (C) Bone volume/total volume (BV/TV) as assessed by μCT. (D) Callus composition on day 10 as assessed by histomorphometry, given as a percentage of the total callus area. Bone, TOT; cartilage, Cg; and fibrous tissue, FT. (E) Callus composition on day 21 as assessed by histomorphometry. (F) Percentage of mice with bony bridging of the fracture gap. (G) Gene expression in vibrated non-OVX mice versus non-vibrated non-OVX mice as assessed by qPCR. The dashed line indicates the level at which there is no difference in expression. * P

    Techniques Used: Mouse Assay, Expressing, Real-time Polymerase Chain Reaction

    9) Product Images from "Synaptic Organization of Perisomatic GABAergic Inputs onto the Principal Cells of the Mouse Basolateral Amygdala"

    Article Title: Synaptic Organization of Perisomatic GABAergic Inputs onto the Principal Cells of the Mouse Basolateral Amygdala

    Journal: Frontiers in Neuroanatomy

    doi: 10.3389/fnana.2016.00020

    Dendritic and axonal arborization of the three perisomatic region-targeting interneurons are distinct. (A) Neurolucida reconstructions of the dendritic arbor of three example cells labeled in slice preparations. Concentric circles drawn on the reconstructions illustrate the radii used for Sholl Analysis. (B) Box chart comparison of total dendritic length, the ratio of the extent of the dendritic tree and the amygdala within the slices, and total dendritic surface. The mean (small open square), the median (midline of the box), the interquartile range (box), and the 5/95% values (ends of whisker bars) are plotted. (C) Comparison of the dendritic length and the number of dendritic segments as a function of dendritic order. (D) Dendritic length as a function of distance from the soma. (E) Neurolucida reconstructions of the biocytin-filled processes (dendrites in black, axon in color) of the same interneurons as in (A) . The borders of the amygdala are shown in gray. (F) Box chart comparison of total axon length, the ratio of the extent of the axon arbor and the amygdala within the slices, and the number of axon nodes. Box and whiskers as panel (B) . (G) Comparison of the number of varicosities on axon collaterals. Box and whiskers as panel (B). (H) Cumulative probability distributions of the inter-bouton distances for the three cell types. The initial 10 μm of the distribution is enlarged in the inset. (I) Number of varicosities as a function of soma distance. For more details, see Table 2 . All scale bars are 100 μm. * indicates significant differences.
    Figure Legend Snippet: Dendritic and axonal arborization of the three perisomatic region-targeting interneurons are distinct. (A) Neurolucida reconstructions of the dendritic arbor of three example cells labeled in slice preparations. Concentric circles drawn on the reconstructions illustrate the radii used for Sholl Analysis. (B) Box chart comparison of total dendritic length, the ratio of the extent of the dendritic tree and the amygdala within the slices, and total dendritic surface. The mean (small open square), the median (midline of the box), the interquartile range (box), and the 5/95% values (ends of whisker bars) are plotted. (C) Comparison of the dendritic length and the number of dendritic segments as a function of dendritic order. (D) Dendritic length as a function of distance from the soma. (E) Neurolucida reconstructions of the biocytin-filled processes (dendrites in black, axon in color) of the same interneurons as in (A) . The borders of the amygdala are shown in gray. (F) Box chart comparison of total axon length, the ratio of the extent of the axon arbor and the amygdala within the slices, and the number of axon nodes. Box and whiskers as panel (B) . (G) Comparison of the number of varicosities on axon collaterals. Box and whiskers as panel (B). (H) Cumulative probability distributions of the inter-bouton distances for the three cell types. The initial 10 μm of the distribution is enlarged in the inset. (I) Number of varicosities as a function of soma distance. For more details, see Table 2 . All scale bars are 100 μm. * indicates significant differences.

    Techniques Used: Labeling, Whisker Assay

    Neurochemical content and postsynaptic targets of interneurons innervating the perisomatic region of principal cells in the BLA . Maximum z intensity projection images taken of an in vitro biocytin-filled AAC (A) , PVBC (F) , or CCK/CB 1 BC (I) . (B) Varicosities of the AAC in (A) contact with an AIS visualized by ankyrin G staining and lack Calb immunoreactivity (C) . (D) A biocytin-filled bouton of an AAC forms a symmetrical synapse on an AIS. (E) Distribution of target axon diameters obtained by random sampling (55 boutons from 7 AACs). Black lines represent the mean value. (G) The biocytin-containing boutons of the same cell as in (F) form close contacts with the Kv2.1-labeled perisomatic region of a PC and express Calb (H) . (J) The boutons of the interneuron in (I) form close appositions with the Kv2.1-immunostained membranes of a PC and express CB 1 (K) . (L, M) Electron micrographs show biocytin-labeled axon terminals of a PVBC forming symmetrical synapses on a soma (s) or a small caliber dendrite (d; black arrows). The same postsynaptic elements also received symmetrical synapses from unlabeled axon endings (white arrows). (N) Ratio of boutons of PVBCs ( n = 12) and CCK/CB 1 BCs ( n = 12) forming close contacts with Kv2.1-immunostained somata, proximal dendrites, or which did not appose any Kv2.1-immunostained profiles (unidentified). Note, that the high ratio of boutons contacting the perisomatic region of PCs defines the cells as BCs. (O) A larger number of boutons from PVBCs (orange) than from CCK/CB 1 BCs (blue) contact the perisomatic region of individual PCs. Asterisks mark significant differences (for values see the text). The mean (small open square), the median (midline of the box), the interquartile range (box), and the 5/95% values (ends of whisker bars) are plotted. AAC, axo-axonic cell; PVBC, parvalbumin-containing basket cell; CCK/CB 1 BC, cholecystokinin and CB 1 cannabinoid receptor-expressing basket cell. Scale bars, 50 μm in (A,F,I) , 10 μm in (B,G,J) ; 1 μm in (C,H,K) ; 0.5 μm in (D,L,M) .
    Figure Legend Snippet: Neurochemical content and postsynaptic targets of interneurons innervating the perisomatic region of principal cells in the BLA . Maximum z intensity projection images taken of an in vitro biocytin-filled AAC (A) , PVBC (F) , or CCK/CB 1 BC (I) . (B) Varicosities of the AAC in (A) contact with an AIS visualized by ankyrin G staining and lack Calb immunoreactivity (C) . (D) A biocytin-filled bouton of an AAC forms a symmetrical synapse on an AIS. (E) Distribution of target axon diameters obtained by random sampling (55 boutons from 7 AACs). Black lines represent the mean value. (G) The biocytin-containing boutons of the same cell as in (F) form close contacts with the Kv2.1-labeled perisomatic region of a PC and express Calb (H) . (J) The boutons of the interneuron in (I) form close appositions with the Kv2.1-immunostained membranes of a PC and express CB 1 (K) . (L, M) Electron micrographs show biocytin-labeled axon terminals of a PVBC forming symmetrical synapses on a soma (s) or a small caliber dendrite (d; black arrows). The same postsynaptic elements also received symmetrical synapses from unlabeled axon endings (white arrows). (N) Ratio of boutons of PVBCs ( n = 12) and CCK/CB 1 BCs ( n = 12) forming close contacts with Kv2.1-immunostained somata, proximal dendrites, or which did not appose any Kv2.1-immunostained profiles (unidentified). Note, that the high ratio of boutons contacting the perisomatic region of PCs defines the cells as BCs. (O) A larger number of boutons from PVBCs (orange) than from CCK/CB 1 BCs (blue) contact the perisomatic region of individual PCs. Asterisks mark significant differences (for values see the text). The mean (small open square), the median (midline of the box), the interquartile range (box), and the 5/95% values (ends of whisker bars) are plotted. AAC, axo-axonic cell; PVBC, parvalbumin-containing basket cell; CCK/CB 1 BC, cholecystokinin and CB 1 cannabinoid receptor-expressing basket cell. Scale bars, 50 μm in (A,F,I) , 10 μm in (B,G,J) ; 1 μm in (C,H,K) ; 0.5 μm in (D,L,M) .

    Techniques Used: In Vitro, Staining, Sampling, Labeling, Whisker Assay, Expressing

    Immunostaining against Kv2.1 channel protein visualizes the extent of the perisomatic region along the proximal dendrites of principal cells in the BLA, a functional domain receiving predominantly GABAergic inputs. (A) Maximum z-intensity projection image of a biocytin-filled principal cell (PC) in the BLA shown together with GABAergic boutons visualized with immunostaining against VGAT and PanGAD. (B) GABAergic boutons in close apposition with the same PC as in (A) are indicated in a Neurolucida reconstruction (AIS, axon initial segment). (C) Relationship between the spine number and the distance from the soma. A Boltzmann function (blue line) fitted onto the spine distribution gave an inflection point at 30.5 ± 0.85 μm (red dot). Pooled data obtained from 68 dendrites of 11 PCs. (D) The distribution of GABAergic boutons along the dendrites as a function of the distance from the soma (19 dendrites of 4 PCs). (E) Kv2.1 immunostaining in the BLA. (F) The variance in the length of Kv2.1-immunopositive dendrites is shown. Horizontal line indicates the mean of 26.43 μm ( n = 68). (G) The length of the Kv2.1-labeling correlated with the diameter of biocytin-filled dendrites at their somatic origin, but it was independent from the dendritic branching pattern (i.e., the order of the dendrites). Red area indicates 95% confidence interval of the linear fit. (H) Excitatory and inhibitory (E/I) ratios on PCs calculated from data in (C, D) are shown aligned by the dendrite base or the end of Kv2.1-immunostained profiles. Note the steeper change in E/I ratio when aligned to the end of Kv2.1-immunolabeled dendrites (see text for details). (I) The density of GABAergic boutons on the PC somata and their Kv2.1-immunostained dendrites is similar when determined either in vitro and in vivo . (red lines: mean of the distributions). Scale bars, 20 μm in (A, B, E) .
    Figure Legend Snippet: Immunostaining against Kv2.1 channel protein visualizes the extent of the perisomatic region along the proximal dendrites of principal cells in the BLA, a functional domain receiving predominantly GABAergic inputs. (A) Maximum z-intensity projection image of a biocytin-filled principal cell (PC) in the BLA shown together with GABAergic boutons visualized with immunostaining against VGAT and PanGAD. (B) GABAergic boutons in close apposition with the same PC as in (A) are indicated in a Neurolucida reconstruction (AIS, axon initial segment). (C) Relationship between the spine number and the distance from the soma. A Boltzmann function (blue line) fitted onto the spine distribution gave an inflection point at 30.5 ± 0.85 μm (red dot). Pooled data obtained from 68 dendrites of 11 PCs. (D) The distribution of GABAergic boutons along the dendrites as a function of the distance from the soma (19 dendrites of 4 PCs). (E) Kv2.1 immunostaining in the BLA. (F) The variance in the length of Kv2.1-immunopositive dendrites is shown. Horizontal line indicates the mean of 26.43 μm ( n = 68). (G) The length of the Kv2.1-labeling correlated with the diameter of biocytin-filled dendrites at their somatic origin, but it was independent from the dendritic branching pattern (i.e., the order of the dendrites). Red area indicates 95% confidence interval of the linear fit. (H) Excitatory and inhibitory (E/I) ratios on PCs calculated from data in (C, D) are shown aligned by the dendrite base or the end of Kv2.1-immunostained profiles. Note the steeper change in E/I ratio when aligned to the end of Kv2.1-immunolabeled dendrites (see text for details). (I) The density of GABAergic boutons on the PC somata and their Kv2.1-immunostained dendrites is similar when determined either in vitro and in vivo . (red lines: mean of the distributions). Scale bars, 20 μm in (A, B, E) .

    Techniques Used: Immunostaining, Functional Assay, Labeling, Immunolabeling, In Vitro, In Vivo

    10) Product Images from "Stimulus-Dependent Translocation of κ Opioid Receptors to the Plasma Membrane"

    Article Title: Stimulus-Dependent Translocation of κ Opioid Receptors to the Plasma Membrane

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.19-07-02658.1999

    Schematic illustration showing translocation of presynaptic KOR1 from its transport vesicle to the plasma membrane. In the nerve terminals of the neural lobe, KOR1 appears to be transported in vesicles containing vasopressin ( VP ). Conditions that cause depolarization and release of neurohormone appear to cause KOR1 to be inserted into the plasma membrane, giving the receptor access to its ligand to transduce a signal across the plasma membrane.
    Figure Legend Snippet: Schematic illustration showing translocation of presynaptic KOR1 from its transport vesicle to the plasma membrane. In the nerve terminals of the neural lobe, KOR1 appears to be transported in vesicles containing vasopressin ( VP ). Conditions that cause depolarization and release of neurohormone appear to cause KOR1 to be inserted into the plasma membrane, giving the receptor access to its ligand to transduce a signal across the plasma membrane.

    Techniques Used: Translocation Assay, Transduction

    KOR1-IR translocates to the plasma membrane from large secretory vesicles in a stimulus-dependent manner. Experimental animals ( n = 3) were treated with an intraperitoneal injection of hypertonic saline 15 or 60 min before perfusion fixation. In control animals ( n = 3), a needle was inserted and withdrawn without the delivery of saline. The graph shows the summary of the quantification of immunogold particles representing KOR1-IR, expressed as percentage of total KOR1-IR. The values shown represent the mean ± SEM. Gold particles were counted in 464 nerve terminals. Control: large secretory vesicles, 58.2 ± 3.6%; plasma membrane, 14.6 ± 3.0%; 15 min stimulation: large secretory vesicles, 42.1 ± 1.0%; plasma membrane, 25.2 ± 2.2%; 60 min stimulation: large secretory vesicles, 56.0 ± 0.7%; plasma membrane, 12.8 ± 0.2%. * p
    Figure Legend Snippet: KOR1-IR translocates to the plasma membrane from large secretory vesicles in a stimulus-dependent manner. Experimental animals ( n = 3) were treated with an intraperitoneal injection of hypertonic saline 15 or 60 min before perfusion fixation. In control animals ( n = 3), a needle was inserted and withdrawn without the delivery of saline. The graph shows the summary of the quantification of immunogold particles representing KOR1-IR, expressed as percentage of total KOR1-IR. The values shown represent the mean ± SEM. Gold particles were counted in 464 nerve terminals. Control: large secretory vesicles, 58.2 ± 3.6%; plasma membrane, 14.6 ± 3.0%; 15 min stimulation: large secretory vesicles, 42.1 ± 1.0%; plasma membrane, 25.2 ± 2.2%; 60 min stimulation: large secretory vesicles, 56.0 ± 0.7%; plasma membrane, 12.8 ± 0.2%. * p

    Techniques Used: Injection

    A large portion of KOR1- and VPNP-IR colocalize in the same structures in the axons of the median eminence and nerve terminals within the neural lobe of the pituitary. Confocal micrographs of KOR1-IR ( red ) and VPNP-IR ( green ) in double-labeled single sections of rat median eminence ( A , B ) and posterior pituitary ( C , D ). Instances of colocalization are indicated by yellow (and arrows ), created by the digital merging of red (KOR-IR) and green (VPNP-IR). A , Low-magnification image of median eminence showing colocalization of KOR1- and VPNP-IR within the internal layer of the median eminence and scattered fibers in the external layer. B , High-magnification image showing colocalization of KOR1- and VPNP-IR in discrete puncta in a subset of fibers within the internal layer of the median eminence. C , Low-magnification image of nerve terminals within the neural lobe that are positive for both KOR1- and VPNP-IR. D , High-magnification image showing that KOR1- and VPNP-IR are colocalized within a subpopulation of the nerve terminals. Scale bars: (in C ) A , C , 50 μm; (in D ) B , D , 30 μm. III , Third ventricle; IL , intermediate lobe of the pituitary.
    Figure Legend Snippet: A large portion of KOR1- and VPNP-IR colocalize in the same structures in the axons of the median eminence and nerve terminals within the neural lobe of the pituitary. Confocal micrographs of KOR1-IR ( red ) and VPNP-IR ( green ) in double-labeled single sections of rat median eminence ( A , B ) and posterior pituitary ( C , D ). Instances of colocalization are indicated by yellow (and arrows ), created by the digital merging of red (KOR-IR) and green (VPNP-IR). A , Low-magnification image of median eminence showing colocalization of KOR1- and VPNP-IR within the internal layer of the median eminence and scattered fibers in the external layer. B , High-magnification image showing colocalization of KOR1- and VPNP-IR in discrete puncta in a subset of fibers within the internal layer of the median eminence. C , Low-magnification image of nerve terminals within the neural lobe that are positive for both KOR1- and VPNP-IR. D , High-magnification image showing that KOR1- and VPNP-IR are colocalized within a subpopulation of the nerve terminals. Scale bars: (in C ) A , C , 50 μm; (in D ) B , D , 30 μm. III , Third ventricle; IL , intermediate lobe of the pituitary.

    Techniques Used: Labeling

    KOR1- and VPNP-IR colocalize in the cell bodies of hypothalamic MNN. Confocal micrographs of KOR1 ( A , C ) and VPNP ( B , D ) double-labeled single sections. A , B , Single section of rat paraventricular nucleus double-labeled for KOR1-IR ( A ) and VPNP-IR ( B ). Examples of KOR1 and VPNP colocalization within cell bodies are indicated by arrows . C , D , Single section of rat supraoptic nucleus double-labeled for KOR1-IR ( C ) and VPNP-IR ( D ). Examples of KOR1 and VPNP colocalization within cell bodies are indicated by arrows . Scale bar: A–D , 100 μm.
    Figure Legend Snippet: KOR1- and VPNP-IR colocalize in the cell bodies of hypothalamic MNN. Confocal micrographs of KOR1 ( A , C ) and VPNP ( B , D ) double-labeled single sections. A , B , Single section of rat paraventricular nucleus double-labeled for KOR1-IR ( A ) and VPNP-IR ( B ). Examples of KOR1 and VPNP colocalization within cell bodies are indicated by arrows . C , D , Single section of rat supraoptic nucleus double-labeled for KOR1-IR ( C ) and VPNP-IR ( D ). Examples of KOR1 and VPNP colocalization within cell bodies are indicated by arrows . Scale bar: A–D , 100 μm.

    Techniques Used: Labeling

    KOR1-IR is associated with the membrane of large secretory vesicles containing VPNP-IR. Transmission electron microscopy micrographs of postembedding–immunogold staining for KOR1 (15 nm gold) and VPNP (5 nm gold) within the neural lobe. Serial sections single-labeled with anti-KOR1 ( A ) and anti-VPNP ( B ). The same vesicle ( small arrows ) is labeled with KOR1- and VPNP-IR in both sections ( A , B ). C , Single section double-labeled with anti-KOR1 (15 nm) and anti-VPNP (5 nm) also showing KOR1- and VPNP-IR colocalized in the same large secretory vesicle ( large arrow ). Single-labeled sections showing KOR1-IR on the membrane of a large secretory vesicle ( D ) and the plasma membrane ( E ). Scale bars: (in B ) A , B , 250 nm; C , 100 nm; (in E ) D , E , 100 nm.
    Figure Legend Snippet: KOR1-IR is associated with the membrane of large secretory vesicles containing VPNP-IR. Transmission electron microscopy micrographs of postembedding–immunogold staining for KOR1 (15 nm gold) and VPNP (5 nm gold) within the neural lobe. Serial sections single-labeled with anti-KOR1 ( A ) and anti-VPNP ( B ). The same vesicle ( small arrows ) is labeled with KOR1- and VPNP-IR in both sections ( A , B ). C , Single section double-labeled with anti-KOR1 (15 nm) and anti-VPNP (5 nm) also showing KOR1- and VPNP-IR colocalized in the same large secretory vesicle ( large arrow ). Single-labeled sections showing KOR1-IR on the membrane of a large secretory vesicle ( D ) and the plasma membrane ( E ). Scale bars: (in B ) A , B , 250 nm; C , 100 nm; (in E ) D , E , 100 nm.

    Techniques Used: Transmission Assay, Electron Microscopy, Staining, Labeling

    Subcellular distribution of KOR1 in the nerve terminals of rat posterior pituitary. The graph shows the summary of the quantification of immunogold particles representing KOR1-IR, expressed as percentage of total KOR1-IR. Subcellular compartments were defined as large secretory vesicles ( LSV ), plasma membrane ( PM ), cytoplasm ( CYTO ), and synaptic-like microvesicles ( SLMV ). Large secretory vesicles, 62.5 ± 1.8%; plasma membrane, 10.8 ± 1.2%; cytoplasm, 17 ± 2.1%; synaptic-like microvesicles, 10.7 ± 1.8%. Error bars indicate ±SEM.
    Figure Legend Snippet: Subcellular distribution of KOR1 in the nerve terminals of rat posterior pituitary. The graph shows the summary of the quantification of immunogold particles representing KOR1-IR, expressed as percentage of total KOR1-IR. Subcellular compartments were defined as large secretory vesicles ( LSV ), plasma membrane ( PM ), cytoplasm ( CYTO ), and synaptic-like microvesicles ( SLMV ). Large secretory vesicles, 62.5 ± 1.8%; plasma membrane, 10.8 ± 1.2%; cytoplasm, 17 ± 2.1%; synaptic-like microvesicles, 10.7 ± 1.8%. Error bars indicate ±SEM.

    Techniques Used:

    11) 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

    12) 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

    13) Product Images from "Myeloid cell transmigration across the CNS vasculature triggers IL-1β–driven neuroinflammation during autoimmune encephalomyelitis in mice"

    Article Title: Myeloid cell transmigration across the CNS vasculature triggers IL-1β–driven neuroinflammation during autoimmune encephalomyelitis in mice

    Journal: The Journal of Experimental Medicine

    doi: 10.1084/jem.20151437

    IL-1β drives a cytokine/chemokine expression profile in mouse and human blood–brain barrier/BSCB ECs predicted to favor neutrophil and monocyte activities. (A) Cytokine levels in conditioned media collected from primary BMECs treated with IL-1β or TNF + IFN-γ as measured using a multiplex ELISA cytokine/chemokine array. Differences compared with the control condition, i.e., culture medium in the absence of cytokine treatment, are expressed in ng/ml for cells stimulated with either 10 ng/ml of recombinant mouse IL-1β (black bars; n = 3) or a combination of TNF and IFN-γ (gray bars; n = 3). (B–D) The combination of immunohistochemistry for the endothelial marker CD31 with ISH for the detection of G-CSF (B), GM-CSF (C), and Il-6 (D) mRNAs in the spinal cord of C57BL/6 mice at EAE onset is shown ( n = 4). (E–I) Cytokines released by primary human BMECs after treatment with either 10 ng/ml of recombinant human IL-1β (black bars) or 100 U TNF + IFN-γ (gray bars). Levels of G-CSF (E) GM-CSF (F), IL-6 (G), CXCL8 (H), and CCL2 (I) are means ± SEM of experiments from two to five different primary cultures. (J and K) Immunohistochemistry against endothelial CD31 was combined with ISH for G-CSF (J) and Il-6 (K) mRNAs in spinal cord tissue sections from C57BL/6 mice ( n = 4/group) that received a single subdural injection of recombinant IL-1β (J and K) or saline (not depicted). *, P
    Figure Legend Snippet: IL-1β drives a cytokine/chemokine expression profile in mouse and human blood–brain barrier/BSCB ECs predicted to favor neutrophil and monocyte activities. (A) Cytokine levels in conditioned media collected from primary BMECs treated with IL-1β or TNF + IFN-γ as measured using a multiplex ELISA cytokine/chemokine array. Differences compared with the control condition, i.e., culture medium in the absence of cytokine treatment, are expressed in ng/ml for cells stimulated with either 10 ng/ml of recombinant mouse IL-1β (black bars; n = 3) or a combination of TNF and IFN-γ (gray bars; n = 3). (B–D) The combination of immunohistochemistry for the endothelial marker CD31 with ISH for the detection of G-CSF (B), GM-CSF (C), and Il-6 (D) mRNAs in the spinal cord of C57BL/6 mice at EAE onset is shown ( n = 4). (E–I) Cytokines released by primary human BMECs after treatment with either 10 ng/ml of recombinant human IL-1β (black bars) or 100 U TNF + IFN-γ (gray bars). Levels of G-CSF (E) GM-CSF (F), IL-6 (G), CXCL8 (H), and CCL2 (I) are means ± SEM of experiments from two to five different primary cultures. (J and K) Immunohistochemistry against endothelial CD31 was combined with ISH for G-CSF (J) and Il-6 (K) mRNAs in spinal cord tissue sections from C57BL/6 mice ( n = 4/group) that received a single subdural injection of recombinant IL-1β (J and K) or saline (not depicted). *, P

    Techniques Used: Expressing, Multiplex Assay, Enzyme-linked Immunosorbent Assay, Recombinant, Immunohistochemistry, Marker, In Situ Hybridization, Mouse Assay, Injection

    IL-1R1 is expressed by ECs of the pial venous plexus, which corresponds to the primary site of myeloid cell infiltration during acute EAE. (A–G) Immunofluorescence confocal microscopy of spinal cord tissue sections from EAE C57BL/6 mice. (A) Immunofluorescence was used to assess whether DsRed + cells are found in proximity of CD31 + ECs and IL-1R1 + blood vessels at onset of EAE. (B and C) IL-1R1 expression on ECs in a naive (B) and inflamed (C) spinal cord. The inset in C is a closeup image of the purple box. (D) Graph displaying the abluminal localization of IL-1R1 on ECs (white dashed line in B). (E) Confocal microscopy was used to assess colocalization (or lack thereof) of IL-1R1 + blood vessels with αSMA, a protein associated with smooth muscle cells in the tunica media of the artery wall (see insets). (F and G) Triple immunofluorescence staining was performed to assess colocalization of IL-1R1 with CD31, PDGFR-β (pericytes), or GFAP (astrocytes). (H) Myeloid cells (LysM-GFP + ) were seen to infiltrate almost exclusively through IL-1R1 + blood vessels. Bars: (A) 10 µm; (B and H) 25 µm; (E insets) 50 µm; (E) 100 µm; (F and G) 5 µm.
    Figure Legend Snippet: IL-1R1 is expressed by ECs of the pial venous plexus, which corresponds to the primary site of myeloid cell infiltration during acute EAE. (A–G) Immunofluorescence confocal microscopy of spinal cord tissue sections from EAE C57BL/6 mice. (A) Immunofluorescence was used to assess whether DsRed + cells are found in proximity of CD31 + ECs and IL-1R1 + blood vessels at onset of EAE. (B and C) IL-1R1 expression on ECs in a naive (B) and inflamed (C) spinal cord. The inset in C is a closeup image of the purple box. (D) Graph displaying the abluminal localization of IL-1R1 on ECs (white dashed line in B). (E) Confocal microscopy was used to assess colocalization (or lack thereof) of IL-1R1 + blood vessels with αSMA, a protein associated with smooth muscle cells in the tunica media of the artery wall (see insets). (F and G) Triple immunofluorescence staining was performed to assess colocalization of IL-1R1 with CD31, PDGFR-β (pericytes), or GFAP (astrocytes). (H) Myeloid cells (LysM-GFP + ) were seen to infiltrate almost exclusively through IL-1R1 + blood vessels. Bars: (A) 10 µm; (B and H) 25 µm; (E insets) 50 µm; (E) 100 µm; (F and G) 5 µm.

    Techniques Used: Immunofluorescence, Confocal Microscopy, Mouse Assay, Expressing, Staining

    14) 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

    15) 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

    16) Product Images from "Faster forgetting contributes to impaired spatial memory in the PDAPP mouse: Deficit in memory retrieval associated with increased sensitivity to interference?"

    Article Title: Faster forgetting contributes to impaired spatial memory in the PDAPP mouse: Deficit in memory retrieval associated with increased sensitivity to interference?

    Journal:

    doi: 10.1101/lm.990208

    Immunocytochemistry on fixed brain sections using 3D6 antibody to reveal plaques. ( A ) The absence of plaques in young 6-mo-old PDAPP mice. Scale bar, 100 μm. ( B ) Diffuse amyloid plaque deposition in the hippocampus and cortex in 16-mo-old PDAPP
    Figure Legend Snippet: Immunocytochemistry on fixed brain sections using 3D6 antibody to reveal plaques. ( A ) The absence of plaques in young 6-mo-old PDAPP mice. Scale bar, 100 μm. ( B ) Diffuse amyloid plaque deposition in the hippocampus and cortex in 16-mo-old PDAPP

    Techniques Used: Immunocytochemistry, Mouse Assay

    17) 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

    18) 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

    19) Product Images from "Preserved Calretinin Interneurons in an App Model of Alzheimer’s Disease Disrupt Hippocampal Inhibition via Upregulated P2Y1 Purinoreceptors"

    Article Title: Preserved Calretinin Interneurons in an App Model of Alzheimer’s Disease Disrupt Hippocampal Inhibition via Upregulated P2Y1 Purinoreceptors

    Journal: Cerebral Cortex (New York, NY)

    doi: 10.1093/cercor/bhz165

    Age-dependent phenotypical changes in the App NL-F/NL-F model of AD. ( A , C , E ) Z -stack images from confocal microscopy illustrating the expression of GFAP (for reactive astrocytes), CD68 (for microglia), and Aβ (all in red, secondary antibody Texas Red) together with DAPI staining for nuclei (in blue) in 12-month age-matched wild-type and App NL-F/NL-F mice, respectively. Similarly, bright-field images of tissue immunostained with biotinylated antibodies show conglomerates of GFAP, CD68, and Aβ in the same animals. Both immunofluorescence and immunoperoxidase-stained images taken at ×20 magnification (larger images, scale bar = 50 μm) and ×63 magnification (inserts, scale bar = 20 μm). ( B , D , F ) Analysis of GFAP, CD68, and Aβ from immunoperoxidase-stained tissue. Significant differences in the three markers of AD were seen between wild-type and App NL-F/NL-F mice only at 9–18 months and when comparing quantification at 9–18 months with the other two age cohorts. ( G , I ) Age-dependent accumulation of Aβ in selective subtypes of interneurons in hippocampal CA1. Aβ colocalization was found at significantly higher levels in SST and CCK cells (indicated by arrows), but not in calretinin (CR) cells in the same animals at 12 months (scale = 20 μm). ( J ) Quantification of colocalization of Aβ with either CCK, SST, or calretinin cells. A two-way ANOVA was performed with pairwise comparisons corrected for multiple comparisons (α = 0.05), with either post hoc Sidak’s test or Tukey’s test for multiple comparisons. * P
    Figure Legend Snippet: Age-dependent phenotypical changes in the App NL-F/NL-F model of AD. ( A , C , E ) Z -stack images from confocal microscopy illustrating the expression of GFAP (for reactive astrocytes), CD68 (for microglia), and Aβ (all in red, secondary antibody Texas Red) together with DAPI staining for nuclei (in blue) in 12-month age-matched wild-type and App NL-F/NL-F mice, respectively. Similarly, bright-field images of tissue immunostained with biotinylated antibodies show conglomerates of GFAP, CD68, and Aβ in the same animals. Both immunofluorescence and immunoperoxidase-stained images taken at ×20 magnification (larger images, scale bar = 50 μm) and ×63 magnification (inserts, scale bar = 20 μm). ( B , D , F ) Analysis of GFAP, CD68, and Aβ from immunoperoxidase-stained tissue. Significant differences in the three markers of AD were seen between wild-type and App NL-F/NL-F mice only at 9–18 months and when comparing quantification at 9–18 months with the other two age cohorts. ( G , I ) Age-dependent accumulation of Aβ in selective subtypes of interneurons in hippocampal CA1. Aβ colocalization was found at significantly higher levels in SST and CCK cells (indicated by arrows), but not in calretinin (CR) cells in the same animals at 12 months (scale = 20 μm). ( J ) Quantification of colocalization of Aβ with either CCK, SST, or calretinin cells. A two-way ANOVA was performed with pairwise comparisons corrected for multiple comparisons (α = 0.05), with either post hoc Sidak’s test or Tukey’s test for multiple comparisons. * P

    Techniques Used: Confocal Microscopy, Expressing, Staining, Mouse Assay, Immunofluorescence

    20) Product Images from "The impact of low-magnitude high-frequency vibration on fracture healing is profoundly influenced by the oestrogen status in mice"

    Article Title: The impact of low-magnitude high-frequency vibration on fracture healing is profoundly influenced by the oestrogen status in mice

    Journal: Disease Models & Mechanisms

    doi: 10.1242/dmm.018622

    Representative immunohistological images of the periosteal fracture callus. Upper row, non-vibrated non-OVX mouse; middle row, vibrated non-OVX mouse; bottom row, non-vibrated OVX mouse. Immunostaining for ERβ (A), sclerostin (B) and β-catenin (C). Scale bars: 100 μm.
    Figure Legend Snippet: Representative immunohistological images of the periosteal fracture callus. Upper row, non-vibrated non-OVX mouse; middle row, vibrated non-OVX mouse; bottom row, non-vibrated OVX mouse. Immunostaining for ERβ (A), sclerostin (B) and β-catenin (C). Scale bars: 100 μm.

    Techniques Used: Immunostaining

    21) Product Images from "Casticin inhibits breast cancer cell migration and invasion by down-regulation of PI3K/Akt signaling pathway"

    Article Title: Casticin inhibits breast cancer cell migration and invasion by down-regulation of PI3K/Akt signaling pathway

    Journal: Bioscience Reports

    doi: 10.1042/BSR20180738

    Effects of mutant Akt expression vector on casticin-mediated cell invasion and its related proteins MDA-MB-231 and 4T1 cells were respectively transfected with Akt1 cDNA or empty vector, and then treated with or without 0.50 µM of casticin for 24 h. ( A , B ) The protein expression levels of Akt, p-Akt, and MMP-9 were analyzed by Western blotting and quantitated against the densitometric signal of β-actin bands. * P
    Figure Legend Snippet: Effects of mutant Akt expression vector on casticin-mediated cell invasion and its related proteins MDA-MB-231 and 4T1 cells were respectively transfected with Akt1 cDNA or empty vector, and then treated with or without 0.50 µM of casticin for 24 h. ( A , B ) The protein expression levels of Akt, p-Akt, and MMP-9 were analyzed by Western blotting and quantitated against the densitometric signal of β-actin bands. * P

    Techniques Used: Mutagenesis, Expressing, Plasmid Preparation, Multiple Displacement Amplification, Transfection, Western Blot

    22) Product Images from "Immunohistochemical and Morphofunctional Studies of Skeletal Muscle Tissues with Electric Nerve Stimulation by In Vivo Cryotechnique"

    Article Title: Immunohistochemical and Morphofunctional Studies of Skeletal Muscle Tissues with Electric Nerve Stimulation by In Vivo Cryotechnique

    Journal: Acta Histochemica et Cytochemica

    doi: 10.1267/ahc.14068

    A flow chart showing the experimental design of the present study. Mouse gastrocnemius muscles and sciatic nerves are exposed under anesthesia, and the in vivo cryotechnique (IVCT) is performed for normal mice ( a ) after the organ exposure in vivo . It is also performed immediately ( b ) after the nerve stimulation has started, or at 3 min ( c ) or 10 min ( d ) after the same stimulation. Following the IVCT, the frozen muscle tissues are freeze-substituted in acetone containing 2% paraformaldehyde (PFA) and embedded in paraffin wax. The deparaffinized thin sections are first stained with hematoxylin-eosin (HE) or periodic-acid-Schiff (PAS), and then immunostained for albumin, IgG1, IgM and fast-myosin.
    Figure Legend Snippet: A flow chart showing the experimental design of the present study. Mouse gastrocnemius muscles and sciatic nerves are exposed under anesthesia, and the in vivo cryotechnique (IVCT) is performed for normal mice ( a ) after the organ exposure in vivo . It is also performed immediately ( b ) after the nerve stimulation has started, or at 3 min ( c ) or 10 min ( d ) after the same stimulation. Following the IVCT, the frozen muscle tissues are freeze-substituted in acetone containing 2% paraformaldehyde (PFA) and embedded in paraffin wax. The deparaffinized thin sections are first stained with hematoxylin-eosin (HE) or periodic-acid-Schiff (PAS), and then immunostained for albumin, IgG1, IgM and fast-myosin.

    Techniques Used: Flow Cytometry, In Vivo, Mouse Assay, Staining

    Light micrographs of serial thin sections obtained from the mouse gastrocnemius muscle tissues, prepared by IVCT without the nerve stimulation (control; a–e ), or immediately (immediately; f–j ), 3 min (3 min stimulation; k–o ) or 10 min (10 min stimulation; p–t ) after the continuous nerve stimulation has started. The thin sections are stained with HE ( a, f, k, p ), and immunostained for albumin ( b, g, l, q ) (higher magnifications; c, h, m, r ), immunoglobulin G1 (IgG1; d, i, n, s ) or immunoglobulin M (IgM; e, j, o, t ). Both IgG1 ( d, i, n, s ; black arrows) and IgM ( e, j, o, t ; white arrows) are immunolocalized in the extracellular matrix and blood vessels. In contrast, dot-like albumin immunostaining is observed in the sarcoplasm of contracting muscle fibers with the nerve stimulation ( l, m ; black arrowheads). The albumin immunoreaction products are more clearly detected after the longer nerve stimulation ( q, r ; black arrowheads). Tissue areas marked with rectangles in ( b ), ( g ), ( l ), ( q ) are highly magnified in ( c ), ( h ), ( m ), ( r ) respectively. Bars=50 μm.
    Figure Legend Snippet: Light micrographs of serial thin sections obtained from the mouse gastrocnemius muscle tissues, prepared by IVCT without the nerve stimulation (control; a–e ), or immediately (immediately; f–j ), 3 min (3 min stimulation; k–o ) or 10 min (10 min stimulation; p–t ) after the continuous nerve stimulation has started. The thin sections are stained with HE ( a, f, k, p ), and immunostained for albumin ( b, g, l, q ) (higher magnifications; c, h, m, r ), immunoglobulin G1 (IgG1; d, i, n, s ) or immunoglobulin M (IgM; e, j, o, t ). Both IgG1 ( d, i, n, s ; black arrows) and IgM ( e, j, o, t ; white arrows) are immunolocalized in the extracellular matrix and blood vessels. In contrast, dot-like albumin immunostaining is observed in the sarcoplasm of contracting muscle fibers with the nerve stimulation ( l, m ; black arrowheads). The albumin immunoreaction products are more clearly detected after the longer nerve stimulation ( q, r ; black arrowheads). Tissue areas marked with rectangles in ( b ), ( g ), ( l ), ( q ) are highly magnified in ( c ), ( h ), ( m ), ( r ) respectively. Bars=50 μm.

    Techniques Used: Staining, Immunostaining

    ( a, b ) Light micrographs of fast-myosin immunostaining in mouse gastrocnemius muscle tissues prepared by IVCT without the nerve stimulation ( a ; control) or at 3 min after the start of stimulation ( b ). The lengths of sarcomeres with or without the nerve stimulation appear to be different between the two groups. Both insets show highly magnified pictures. ( c, d ) The lengths of A band are measured on light micrographs of immunostained fast-myosin, which is needed for calculating the full-width at half-maximum values of each sarcomere. The length of sarcomere is measured as the distance between two adjacent peaks of fast-myosin immunoreactivity. ( e ) Scattered plot diagram of the ratios of (sarcomere length)/(A band length). The numerical values at the bottom show the means and standard deviations, and the asterisks show significant difference (Tukey’s multiple comparisons test, p
    Figure Legend Snippet: ( a, b ) Light micrographs of fast-myosin immunostaining in mouse gastrocnemius muscle tissues prepared by IVCT without the nerve stimulation ( a ; control) or at 3 min after the start of stimulation ( b ). The lengths of sarcomeres with or without the nerve stimulation appear to be different between the two groups. Both insets show highly magnified pictures. ( c, d ) The lengths of A band are measured on light micrographs of immunostained fast-myosin, which is needed for calculating the full-width at half-maximum values of each sarcomere. The length of sarcomere is measured as the distance between two adjacent peaks of fast-myosin immunoreactivity. ( e ) Scattered plot diagram of the ratios of (sarcomere length)/(A band length). The numerical values at the bottom show the means and standard deviations, and the asterisks show significant difference (Tukey’s multiple comparisons test, p

    Techniques Used: Immunostaining

    23) Product Images from "Melatonin Modulation of Sirtuin-1 Attenuates Liver Injury in a Hypercholesterolemic Mouse Model"

    Article Title: Melatonin Modulation of Sirtuin-1 Attenuates Liver Injury in a Hypercholesterolemic Mouse Model

    Journal: BioMed Research International

    doi: 10.1155/2018/7968452

    Photomicrographs of liver immunohistochemical analysis of iNOS (a–d) and of liver double immunofluorescence analysis of SOD1 (green staining) and CAT (red staining) (e–h) of ApoE −/− of 6 w (a, e), ApoE −/− of 15 w (b, f), control (c, g), and ApoE −/− + MEL (d, h). Bar: 20 μ m. v: central vein. The graphs summarized the iNOS (i), SOD1 (j), and CAT (k) histomorphometrical analysis. ∗ p ≤ 0.05 versus ApoE −/− of 6 w and # p ≤ 0.05 versus ApoE −/− of 15 w.
    Figure Legend Snippet: Photomicrographs of liver immunohistochemical analysis of iNOS (a–d) and of liver double immunofluorescence analysis of SOD1 (green staining) and CAT (red staining) (e–h) of ApoE −/− of 6 w (a, e), ApoE −/− of 15 w (b, f), control (c, g), and ApoE −/− + MEL (d, h). Bar: 20 μ m. v: central vein. The graphs summarized the iNOS (i), SOD1 (j), and CAT (k) histomorphometrical analysis. ∗ p ≤ 0.05 versus ApoE −/− of 6 w and # p ≤ 0.05 versus ApoE −/− of 15 w.

    Techniques Used: Immunohistochemistry, Immunofluorescence, Staining

    Photomicrographs of liver SIRT1 immunohistochemical analysis of ApoE −/− of 6 w (a), ApoE −/− of 15 w (b), control (c), and ApoE −/− + MEL (d). Bar: 20 μ m. v: central vein. The graph (e) summarizes the SIRT1 histomorphometrical analysis. ∗ p ≤ 0.05 versus ApoE −/− of 6 w and # p ≤ 0.05 versus ApoE −/− of 15 w.
    Figure Legend Snippet: Photomicrographs of liver SIRT1 immunohistochemical analysis of ApoE −/− of 6 w (a), ApoE −/− of 15 w (b), control (c), and ApoE −/− + MEL (d). Bar: 20 μ m. v: central vein. The graph (e) summarizes the SIRT1 histomorphometrical analysis. ∗ p ≤ 0.05 versus ApoE −/− of 6 w and # p ≤ 0.05 versus ApoE −/− of 15 w.

    Techniques Used: Immunohistochemistry

    24) Product Images from "Inhibition of Platelet-Derived Growth Factor Promotes Pericyte Loss and Angiogenesis in Ischemic Retinopathy"

    Article Title: Inhibition of Platelet-Derived Growth Factor Promotes Pericyte Loss and Angiogenesis in Ischemic Retinopathy

    Journal: The American Journal of Pathology

    doi:

    Three-μm paraffin sections of inner retina from 18-day-old Sprague Dawley rats immunolabeled with caspase-3. A: Untreated sham rats. B: Sham rats treated with 100 mg/kg/day STI571. C: Untreated ROP. D: ROP rats treated with 100 mg/kg/day STI571. Original magnification, ×400. N = 6 to 8 rats per group. Caspase-3-positive cells ( arrows ) were confirmed to be pericytes by examination of α-smooth muscle cell immunolabeling in consecutive sections (not shown). Caspase-3-positive cells are associated with blood vessels ( asterisks ) and most numerous in ROP rats treated with 100 mg/kg/day STI571 ( D ). Sections are counterstained with eosin. GCL, ganglion cell layer. Quantitation of apoptotic pericytes is shown graphically. Values are means ± SEM. N = 6 to 8 rats per group. U, untreated. *, P
    Figure Legend Snippet: Three-μm paraffin sections of inner retina from 18-day-old Sprague Dawley rats immunolabeled with caspase-3. A: Untreated sham rats. B: Sham rats treated with 100 mg/kg/day STI571. C: Untreated ROP. D: ROP rats treated with 100 mg/kg/day STI571. Original magnification, ×400. N = 6 to 8 rats per group. Caspase-3-positive cells ( arrows ) were confirmed to be pericytes by examination of α-smooth muscle cell immunolabeling in consecutive sections (not shown). Caspase-3-positive cells are associated with blood vessels ( asterisks ) and most numerous in ROP rats treated with 100 mg/kg/day STI571 ( D ). Sections are counterstained with eosin. GCL, ganglion cell layer. Quantitation of apoptotic pericytes is shown graphically. Values are means ± SEM. N = 6 to 8 rats per group. U, untreated. *, P

    Techniques Used: Immunolabeling, Quantitation Assay

    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 results of immunohistochemical analysis for phosphorylated Smad2/3 and TGF-β dependent profibrotic genes expression. (A) In the CG group, a number of phosphorylated-Smad2/3-positive cells were observed in the 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 phosphorylated Smad2/3 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 phosphorylated-Smad2/3–positive cells. Data are expressed as mean±SEM. (E) COLI α 1 expression levels were measured by quantitative RT-PCR relative to β-actin controls. Values are relative to the control group±SEM. (F) Fibronectin expression levels were measured by quantitative RT-PCR relative to β-actin controls. Values are relative to the control group±SEM. (G) CTGF expression levels were measured by quantitative RT-PCR relative to β-actin controls. Values are relative to the control group±SEM. * represents p
    Figure Legend Snippet: The results of immunohistochemical analysis for phosphorylated Smad2/3 and TGF-β dependent profibrotic genes expression. (A) In the CG group, a number of phosphorylated-Smad2/3-positive cells were observed in the 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 phosphorylated Smad2/3 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 phosphorylated-Smad2/3–positive cells. Data are expressed as mean±SEM. (E) COLI α 1 expression levels were measured by quantitative RT-PCR relative to β-actin controls. Values are relative to the control group±SEM. (F) Fibronectin expression levels were measured by quantitative RT-PCR relative to β-actin controls. Values are relative to the control group±SEM. (G) CTGF expression levels were measured by quantitative RT-PCR relative to β-actin controls. Values are relative to the control group±SEM. * represents p

    Techniques Used: Immunohistochemistry, Expressing, Incubation, Negative Control, Quantitative RT-PCR

    26) Product Images from "Selective Action of Orexin (Hypocretin) on Nonspecific Thalamocortical Projection Neurons"

    Article Title: Selective Action of Orexin (Hypocretin) on Nonspecific Thalamocortical Projection Neurons

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.22-18-07835.2002

    Actions of orexin (hypocretin) on Rh and VPL neurons. A , Localizations of the Rh and VPL nuclei with all injected cells ( dots , asterisks , and triangles ). IAM , Interanteromedial thalamic nucleus; ic , internal capsule; MD , mediodorsal thalamic nucleus; Sub , submedius thalamic nucleus; VPM , ventral posteromedial thalamic nucleus; Rt , reticular thalamic nucleus. Red triangles correspond to the injected cells shown in B and C . B, C , Neurobiotin-filled neurons in the Rh and VPL nuclei ( insets showing characteristic responses to hyperpolarizing pulses). D , Depolarizing and excitatory effect of orexin in the Rh neurons. E , Absence of effect of orexin in the VPL. Scale bars: A , 500 μm; B, C , 20 μm.
    Figure Legend Snippet: Actions of orexin (hypocretin) on Rh and VPL neurons. A , Localizations of the Rh and VPL nuclei with all injected cells ( dots , asterisks , and triangles ). IAM , Interanteromedial thalamic nucleus; ic , internal capsule; MD , mediodorsal thalamic nucleus; Sub , submedius thalamic nucleus; VPM , ventral posteromedial thalamic nucleus; Rt , reticular thalamic nucleus. Red triangles correspond to the injected cells shown in B and C . B, C , Neurobiotin-filled neurons in the Rh and VPL nuclei ( insets showing characteristic responses to hyperpolarizing pulses). D , Depolarizing and excitatory effect of orexin in the Rh neurons. E , Absence of effect of orexin in the VPL. Scale bars: A , 500 μm; B, C , 20 μm.

    Techniques Used: Injection

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