biotinylated anti guinea pig  (Vector Laboratories)


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    Vector Laboratories biotinylated anti guinea pig
    Pin1 enhances NL2 synaptic content not its surface abundance. ( a ) Surface NL2 derived from cultured hippocampal neurons of Pin1+/+ and Pin1−/− mice was isolated by biotinylation assay and detected by anti-NL2 antibody. No <t>biotinylated</t> neuronal cells were processed in parallel to evaluate unspecific NL2 binding. Western blot detecting glycophosphatidylinositol-anchored Flotilin was used as loading control ( n =4). Full images of western blots are in Supplementary Fig. 5 . ( b ) Typical examples of hippocampal neurons from Pin1+/+ and Pin1−/− immunolabeled for endogenous gephyrin (magenta), NL2 (green) and VGAT (blue) at DIV10. Enlarged boxed areas are shown aside to the corresponding full view image. Post-synaptic clustering is demonstrated by apposition of gephyrin/NL2 clusters to VGAT positive terminals on the merge window. Scale bars, 20 μm in full view images and 5 μm in enlarged panels. ( c ) Distribution histograms of NL2 cluster density (normalized to 100 μm 2 ), the average cluster size and intensity in Pin1+/+ and Pin1−/− hippocampal neurons. ( d ) Distribution histograms of the percentage of NL2 co-localizing with gephryin and the percentage of double labelled NL2/gephyrin puncta overlapping with the presynaptic marker VGAT. ( e ) Distribution histograms of gephyrin cluster density (normalized to 100 μm 2 ), the average cluster size and intensity (calculated as described in c ) in both mouse genotypes. The number of hippocampal neurons investigated in each experiments (three independent experiments) were as follows: n =10 for Pin1+/+, n =12 for Pin1−/−. For each neurons, at least five dendritic regions of interests were measured, mean values±s.d., ** P
    Biotinylated Anti Guinea Pig, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/biotinylated anti guinea pig/product/Vector Laboratories
    Average 96 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    biotinylated anti guinea pig - by Bioz Stars, 2022-05
    96/100 stars

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    1) Product Images from "Pin1-dependent signalling negatively affects GABAergic transmission by modulating neuroligin2/gephyrin interaction"

    Article Title: Pin1-dependent signalling negatively affects GABAergic transmission by modulating neuroligin2/gephyrin interaction

    Journal: Nature Communications

    doi: 10.1038/ncomms6066

    Pin1 enhances NL2 synaptic content not its surface abundance. ( a ) Surface NL2 derived from cultured hippocampal neurons of Pin1+/+ and Pin1−/− mice was isolated by biotinylation assay and detected by anti-NL2 antibody. No biotinylated neuronal cells were processed in parallel to evaluate unspecific NL2 binding. Western blot detecting glycophosphatidylinositol-anchored Flotilin was used as loading control ( n =4). Full images of western blots are in Supplementary Fig. 5 . ( b ) Typical examples of hippocampal neurons from Pin1+/+ and Pin1−/− immunolabeled for endogenous gephyrin (magenta), NL2 (green) and VGAT (blue) at DIV10. Enlarged boxed areas are shown aside to the corresponding full view image. Post-synaptic clustering is demonstrated by apposition of gephyrin/NL2 clusters to VGAT positive terminals on the merge window. Scale bars, 20 μm in full view images and 5 μm in enlarged panels. ( c ) Distribution histograms of NL2 cluster density (normalized to 100 μm 2 ), the average cluster size and intensity in Pin1+/+ and Pin1−/− hippocampal neurons. ( d ) Distribution histograms of the percentage of NL2 co-localizing with gephryin and the percentage of double labelled NL2/gephyrin puncta overlapping with the presynaptic marker VGAT. ( e ) Distribution histograms of gephyrin cluster density (normalized to 100 μm 2 ), the average cluster size and intensity (calculated as described in c ) in both mouse genotypes. The number of hippocampal neurons investigated in each experiments (three independent experiments) were as follows: n =10 for Pin1+/+, n =12 for Pin1−/−. For each neurons, at least five dendritic regions of interests were measured, mean values±s.d., ** P
    Figure Legend Snippet: Pin1 enhances NL2 synaptic content not its surface abundance. ( a ) Surface NL2 derived from cultured hippocampal neurons of Pin1+/+ and Pin1−/− mice was isolated by biotinylation assay and detected by anti-NL2 antibody. No biotinylated neuronal cells were processed in parallel to evaluate unspecific NL2 binding. Western blot detecting glycophosphatidylinositol-anchored Flotilin was used as loading control ( n =4). Full images of western blots are in Supplementary Fig. 5 . ( b ) Typical examples of hippocampal neurons from Pin1+/+ and Pin1−/− immunolabeled for endogenous gephyrin (magenta), NL2 (green) and VGAT (blue) at DIV10. Enlarged boxed areas are shown aside to the corresponding full view image. Post-synaptic clustering is demonstrated by apposition of gephyrin/NL2 clusters to VGAT positive terminals on the merge window. Scale bars, 20 μm in full view images and 5 μm in enlarged panels. ( c ) Distribution histograms of NL2 cluster density (normalized to 100 μm 2 ), the average cluster size and intensity in Pin1+/+ and Pin1−/− hippocampal neurons. ( d ) Distribution histograms of the percentage of NL2 co-localizing with gephryin and the percentage of double labelled NL2/gephyrin puncta overlapping with the presynaptic marker VGAT. ( e ) Distribution histograms of gephyrin cluster density (normalized to 100 μm 2 ), the average cluster size and intensity (calculated as described in c ) in both mouse genotypes. The number of hippocampal neurons investigated in each experiments (three independent experiments) were as follows: n =10 for Pin1+/+, n =12 for Pin1−/−. For each neurons, at least five dendritic regions of interests were measured, mean values±s.d., ** P

    Techniques Used: Derivative Assay, Cell Culture, Mouse Assay, Isolation, Cell Surface Biotinylation Assay, Binding Assay, Western Blot, Immunolabeling, Marker

    2) Product Images from "Rapid production of antigen-specific monoclonal antibodies from a variety of animals"

    Article Title: Rapid production of antigen-specific monoclonal antibodies from a variety of animals

    Journal: BMC Biology

    doi: 10.1186/1741-7007-10-80

    Production of guinea pig monoclonal antibodies (mAbs) against human insulin . (A) Representative fluorescence-activated cell sorting (FACS) graph of human insulin-immunized guinea pig lymphocytes stained with anti-guinea pig IgG, ER-tracker and insulin-Cy3. Gates for lymphocytes (R1), plasma/plasmablast cells (PCs) (IgG low endoplasmic reticulum (ER) high , R2) and antigen-specific plasma/plasmablast cells (ASPCs) (IgG low ER high insulin + , R3) were established. (B) Representative agarose gel electrophoresis of cognate pairs of V genes amplified from single-cell-sorted R3-gated cells. (C) polymerase chain reaction (PCR) success ratio for the V genes. (D) Antigen specificity of mAbs produced from the R3-gated cells. (E) Binding affinity and binding epitopes of the highly binding clones in (D). (F) Immunohistochemical staining of insulin with c08 mAb in (E) (red) and glucagon (green) in a mouse pancreatic section.
    Figure Legend Snippet: Production of guinea pig monoclonal antibodies (mAbs) against human insulin . (A) Representative fluorescence-activated cell sorting (FACS) graph of human insulin-immunized guinea pig lymphocytes stained with anti-guinea pig IgG, ER-tracker and insulin-Cy3. Gates for lymphocytes (R1), plasma/plasmablast cells (PCs) (IgG low endoplasmic reticulum (ER) high , R2) and antigen-specific plasma/plasmablast cells (ASPCs) (IgG low ER high insulin + , R3) were established. (B) Representative agarose gel electrophoresis of cognate pairs of V genes amplified from single-cell-sorted R3-gated cells. (C) polymerase chain reaction (PCR) success ratio for the V genes. (D) Antigen specificity of mAbs produced from the R3-gated cells. (E) Binding affinity and binding epitopes of the highly binding clones in (D). (F) Immunohistochemical staining of insulin with c08 mAb in (E) (red) and glucagon (green) in a mouse pancreatic section.

    Techniques Used: Fluorescence, FACS, Staining, Agarose Gel Electrophoresis, Amplification, Polymerase Chain Reaction, Produced, Binding Assay, Clone Assay, Immunohistochemistry

    3) Product Images from "Macrophage lipoprotein lipase promotes foam cell formation and atherosclerosis in vivo"

    Article Title: Macrophage lipoprotein lipase promotes foam cell formation and atherosclerosis in vivo

    Journal: Journal of Clinical Investigation

    doi:

    Immunocytochemical detection of macrophages in the myocardium of LPL +/+ →C57BL/6 mice. Macrophages are stained with rat mAb MOMA-2 as the primary antibody, followed by biotinylated goat anti-rat IgG as the secondary antibody. The sections were incubated with avidin-biotin complex labeled with alkaline phosphatase, and the enzymatic activity was viewed with Fast Red TR/Naphthol AS-NX substrate. The sections were counterstained with hematoxylin. The primary antibody was omitted during the incubation of negative control sections, and no red staining was seen in these sections (data not shown). ×40.
    Figure Legend Snippet: Immunocytochemical detection of macrophages in the myocardium of LPL +/+ →C57BL/6 mice. Macrophages are stained with rat mAb MOMA-2 as the primary antibody, followed by biotinylated goat anti-rat IgG as the secondary antibody. The sections were incubated with avidin-biotin complex labeled with alkaline phosphatase, and the enzymatic activity was viewed with Fast Red TR/Naphthol AS-NX substrate. The sections were counterstained with hematoxylin. The primary antibody was omitted during the incubation of negative control sections, and no red staining was seen in these sections (data not shown). ×40.

    Techniques Used: Mouse Assay, Staining, Incubation, Avidin-Biotin Assay, Labeling, Activity Assay, Negative Control

    4) Product Images from "Novel Role for Matricellular Proteins in the Regulation of Islet β Cell Survival"

    Article Title: Novel Role for Matricellular Proteins in the Regulation of Islet β Cell Survival

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M114.573980

    SPARC is detected in stromal PS1 cells but not INS-1 β cells by immunocytochemistry. INS-1 and PS1 cells were grown on coverslips, fixed using 10% NBF and stained using anti-SPARC antibody ( panels a–d ) or with biotinylated secondary antibody
    Figure Legend Snippet: SPARC is detected in stromal PS1 cells but not INS-1 β cells by immunocytochemistry. INS-1 and PS1 cells were grown on coverslips, fixed using 10% NBF and stained using anti-SPARC antibody ( panels a–d ) or with biotinylated secondary antibody

    Techniques Used: Immunocytochemistry, Staining

    5) Product Images from "Characterization of G-Protein-Gated K+ Channels Composed of Kir3.2 Subunits in Dopaminergic Neurons of the Substantia Nigra"

    Article Title: Characterization of G-Protein-Gated K+ Channels Composed of Kir3.2 Subunits in Dopaminergic Neurons of the Substantia Nigra

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.19-03-01006.1999

    A , RT-PCR analysis of Kir3.0 mRNAs in rat SN and Cx. Using the Kir3.0-specific primers indicated above each panel, their expression was examined in cDNAs obtained from rat SN ( odd numbers ) and Cx ( even numbers ). PCR products (519, 369, 456, and 574 bp) of Kir3.2a, Kir3.2c, Kir3.3, and Kir3.2b were detected in both SN and Cx, whereas that of Kir3.1 (666 bp) was found in Cx but not in SN. Numbers indicate the standard markers in base pairs. B , Immunoprecipitation analysis of Kir3.2 isoforms in rat SN and Cx. Biotinylated membrane proteins of rat SN ( a ) or Cx ( b ) were incubated with aG2C-3 ( lanes 1 - 3 ) or aG2A-5 antibodies ( lanes 4 , 5 ) as indicated. The immunoprecipitants were detected with streptavidin–HRP ( SA - HRP ; lanes 1 , 4 ), aG2A-5 ( lane 2 ), aG1C-1 ( lane 3 ), or aG2C-3 antibodies ( lane 5 ). The positions of Kir3.2a ( small open arrowheads ) and Kir3.2c ( large arrowheads ) isoforms and Kir3.1 subunits ( arrows ) are indicated. IgG heavy chains or unknown bands are indicated with asterisks and number signs , respectively. Numbers on the left of the panels indicate the molecular weights of the standard markers in kilodaltons. C , Detection of Kir3.3 in the aG2A-5 immunoprecipitant from rat Cx. The lysates of HEK293T cells transfected with the plasmids indicated in each lane were examined for specificity of aG3NC and aG2B-2 with immunoblot analysis ( a ). Both antibodies could specifically detect proteins at 41 kDa of Kir3.3 and 38 kDa of Kir3.2b, respectively. When the PVDF membranes blotted with SA–HRP were overexposed to the films until the bands of Kir3.2a and Kir3.2c were indistinguishable ( b ), a faint signal at 40 kDa ( small arrows ) was detected in the immunocomplex of aG2A-5 obtained from Cx ( lane 2 ), not from SN ( lane 1 ). The 40 kDa protein in the immunoprecipitant has an immunoreactivity to aG3NC. However, signal with aG2B-2 could not be found either in SN or in Cx.
    Figure Legend Snippet: A , RT-PCR analysis of Kir3.0 mRNAs in rat SN and Cx. Using the Kir3.0-specific primers indicated above each panel, their expression was examined in cDNAs obtained from rat SN ( odd numbers ) and Cx ( even numbers ). PCR products (519, 369, 456, and 574 bp) of Kir3.2a, Kir3.2c, Kir3.3, and Kir3.2b were detected in both SN and Cx, whereas that of Kir3.1 (666 bp) was found in Cx but not in SN. Numbers indicate the standard markers in base pairs. B , Immunoprecipitation analysis of Kir3.2 isoforms in rat SN and Cx. Biotinylated membrane proteins of rat SN ( a ) or Cx ( b ) were incubated with aG2C-3 ( lanes 1 - 3 ) or aG2A-5 antibodies ( lanes 4 , 5 ) as indicated. The immunoprecipitants were detected with streptavidin–HRP ( SA - HRP ; lanes 1 , 4 ), aG2A-5 ( lane 2 ), aG1C-1 ( lane 3 ), or aG2C-3 antibodies ( lane 5 ). The positions of Kir3.2a ( small open arrowheads ) and Kir3.2c ( large arrowheads ) isoforms and Kir3.1 subunits ( arrows ) are indicated. IgG heavy chains or unknown bands are indicated with asterisks and number signs , respectively. Numbers on the left of the panels indicate the molecular weights of the standard markers in kilodaltons. C , Detection of Kir3.3 in the aG2A-5 immunoprecipitant from rat Cx. The lysates of HEK293T cells transfected with the plasmids indicated in each lane were examined for specificity of aG3NC and aG2B-2 with immunoblot analysis ( a ). Both antibodies could specifically detect proteins at 41 kDa of Kir3.3 and 38 kDa of Kir3.2b, respectively. When the PVDF membranes blotted with SA–HRP were overexposed to the films until the bands of Kir3.2a and Kir3.2c were indistinguishable ( b ), a faint signal at 40 kDa ( small arrows ) was detected in the immunocomplex of aG2A-5 obtained from Cx ( lane 2 ), not from SN ( lane 1 ). The 40 kDa protein in the immunoprecipitant has an immunoreactivity to aG3NC. However, signal with aG2B-2 could not be found either in SN or in Cx.

    Techniques Used: Reverse Transcription Polymerase Chain Reaction, Expressing, Polymerase Chain Reaction, Immunoprecipitation, Incubation, Transfection

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    Vector Laboratories biotinylated anti guinea pig
    Pin1 enhances NL2 synaptic content not its surface abundance. ( a ) Surface NL2 derived from cultured hippocampal neurons of Pin1+/+ and Pin1−/− mice was isolated by biotinylation assay and detected by anti-NL2 antibody. No <t>biotinylated</t> neuronal cells were processed in parallel to evaluate unspecific NL2 binding. Western blot detecting glycophosphatidylinositol-anchored Flotilin was used as loading control ( n =4). Full images of western blots are in Supplementary Fig. 5 . ( b ) Typical examples of hippocampal neurons from Pin1+/+ and Pin1−/− immunolabeled for endogenous gephyrin (magenta), NL2 (green) and VGAT (blue) at DIV10. Enlarged boxed areas are shown aside to the corresponding full view image. Post-synaptic clustering is demonstrated by apposition of gephyrin/NL2 clusters to VGAT positive terminals on the merge window. Scale bars, 20 μm in full view images and 5 μm in enlarged panels. ( c ) Distribution histograms of NL2 cluster density (normalized to 100 μm 2 ), the average cluster size and intensity in Pin1+/+ and Pin1−/− hippocampal neurons. ( d ) Distribution histograms of the percentage of NL2 co-localizing with gephryin and the percentage of double labelled NL2/gephyrin puncta overlapping with the presynaptic marker VGAT. ( e ) Distribution histograms of gephyrin cluster density (normalized to 100 μm 2 ), the average cluster size and intensity (calculated as described in c ) in both mouse genotypes. The number of hippocampal neurons investigated in each experiments (three independent experiments) were as follows: n =10 for Pin1+/+, n =12 for Pin1−/−. For each neurons, at least five dendritic regions of interests were measured, mean values±s.d., ** P
    Biotinylated Anti Guinea Pig, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/biotinylated anti guinea pig/product/Vector Laboratories
    Average 96 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    biotinylated anti guinea pig - by Bioz Stars, 2022-05
    96/100 stars
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    Pin1 enhances NL2 synaptic content not its surface abundance. ( a ) Surface NL2 derived from cultured hippocampal neurons of Pin1+/+ and Pin1−/− mice was isolated by biotinylation assay and detected by anti-NL2 antibody. No biotinylated neuronal cells were processed in parallel to evaluate unspecific NL2 binding. Western blot detecting glycophosphatidylinositol-anchored Flotilin was used as loading control ( n =4). Full images of western blots are in Supplementary Fig. 5 . ( b ) Typical examples of hippocampal neurons from Pin1+/+ and Pin1−/− immunolabeled for endogenous gephyrin (magenta), NL2 (green) and VGAT (blue) at DIV10. Enlarged boxed areas are shown aside to the corresponding full view image. Post-synaptic clustering is demonstrated by apposition of gephyrin/NL2 clusters to VGAT positive terminals on the merge window. Scale bars, 20 μm in full view images and 5 μm in enlarged panels. ( c ) Distribution histograms of NL2 cluster density (normalized to 100 μm 2 ), the average cluster size and intensity in Pin1+/+ and Pin1−/− hippocampal neurons. ( d ) Distribution histograms of the percentage of NL2 co-localizing with gephryin and the percentage of double labelled NL2/gephyrin puncta overlapping with the presynaptic marker VGAT. ( e ) Distribution histograms of gephyrin cluster density (normalized to 100 μm 2 ), the average cluster size and intensity (calculated as described in c ) in both mouse genotypes. The number of hippocampal neurons investigated in each experiments (three independent experiments) were as follows: n =10 for Pin1+/+, n =12 for Pin1−/−. For each neurons, at least five dendritic regions of interests were measured, mean values±s.d., ** P

    Journal: Nature Communications

    Article Title: Pin1-dependent signalling negatively affects GABAergic transmission by modulating neuroligin2/gephyrin interaction

    doi: 10.1038/ncomms6066

    Figure Lengend Snippet: Pin1 enhances NL2 synaptic content not its surface abundance. ( a ) Surface NL2 derived from cultured hippocampal neurons of Pin1+/+ and Pin1−/− mice was isolated by biotinylation assay and detected by anti-NL2 antibody. No biotinylated neuronal cells were processed in parallel to evaluate unspecific NL2 binding. Western blot detecting glycophosphatidylinositol-anchored Flotilin was used as loading control ( n =4). Full images of western blots are in Supplementary Fig. 5 . ( b ) Typical examples of hippocampal neurons from Pin1+/+ and Pin1−/− immunolabeled for endogenous gephyrin (magenta), NL2 (green) and VGAT (blue) at DIV10. Enlarged boxed areas are shown aside to the corresponding full view image. Post-synaptic clustering is demonstrated by apposition of gephyrin/NL2 clusters to VGAT positive terminals on the merge window. Scale bars, 20 μm in full view images and 5 μm in enlarged panels. ( c ) Distribution histograms of NL2 cluster density (normalized to 100 μm 2 ), the average cluster size and intensity in Pin1+/+ and Pin1−/− hippocampal neurons. ( d ) Distribution histograms of the percentage of NL2 co-localizing with gephryin and the percentage of double labelled NL2/gephyrin puncta overlapping with the presynaptic marker VGAT. ( e ) Distribution histograms of gephyrin cluster density (normalized to 100 μm 2 ), the average cluster size and intensity (calculated as described in c ) in both mouse genotypes. The number of hippocampal neurons investigated in each experiments (three independent experiments) were as follows: n =10 for Pin1+/+, n =12 for Pin1−/−. For each neurons, at least five dendritic regions of interests were measured, mean values±s.d., ** P

    Article Snippet: Antibodies The following antibodies were used in immunohistochemistry and immunocitochemistry: anti-gephyrin Mab7a (Synaptic System Cat. No 147021), anti-VGAT rabbit or guinea pig (1:1,000, Synaptic System Cat. No 131004), anti-NL2 rabbit affinity purified (1:500, Synaptic system Cat, No 129203), guinea pig anti-GABAA γ2 subunit (1:2,000 (ref. )), biotinylated anti-guinea pig (1:200, Vector Laboratories, Cat No BA-7000).

    Techniques: Derivative Assay, Cell Culture, Mouse Assay, Isolation, Cell Surface Biotinylation Assay, Binding Assay, Western Blot, Immunolabeling, Marker

    Production of guinea pig monoclonal antibodies (mAbs) against human insulin . (A) Representative fluorescence-activated cell sorting (FACS) graph of human insulin-immunized guinea pig lymphocytes stained with anti-guinea pig IgG, ER-tracker and insulin-Cy3. Gates for lymphocytes (R1), plasma/plasmablast cells (PCs) (IgG low endoplasmic reticulum (ER) high , R2) and antigen-specific plasma/plasmablast cells (ASPCs) (IgG low ER high insulin + , R3) were established. (B) Representative agarose gel electrophoresis of cognate pairs of V genes amplified from single-cell-sorted R3-gated cells. (C) polymerase chain reaction (PCR) success ratio for the V genes. (D) Antigen specificity of mAbs produced from the R3-gated cells. (E) Binding affinity and binding epitopes of the highly binding clones in (D). (F) Immunohistochemical staining of insulin with c08 mAb in (E) (red) and glucagon (green) in a mouse pancreatic section.

    Journal: BMC Biology

    Article Title: Rapid production of antigen-specific monoclonal antibodies from a variety of animals

    doi: 10.1186/1741-7007-10-80

    Figure Lengend Snippet: Production of guinea pig monoclonal antibodies (mAbs) against human insulin . (A) Representative fluorescence-activated cell sorting (FACS) graph of human insulin-immunized guinea pig lymphocytes stained with anti-guinea pig IgG, ER-tracker and insulin-Cy3. Gates for lymphocytes (R1), plasma/plasmablast cells (PCs) (IgG low endoplasmic reticulum (ER) high , R2) and antigen-specific plasma/plasmablast cells (ASPCs) (IgG low ER high insulin + , R3) were established. (B) Representative agarose gel electrophoresis of cognate pairs of V genes amplified from single-cell-sorted R3-gated cells. (C) polymerase chain reaction (PCR) success ratio for the V genes. (D) Antigen specificity of mAbs produced from the R3-gated cells. (E) Binding affinity and binding epitopes of the highly binding clones in (D). (F) Immunohistochemical staining of insulin with c08 mAb in (E) (red) and glucagon (green) in a mouse pancreatic section.

    Article Snippet: The insulin signal was visualized with goat anti-guinea pig antibody-AP and the VECTOR Red Alkaline Phosphatase Substrate Kit (Vector Labs, http://www.vectorlabs.com/ ).

    Techniques: Fluorescence, FACS, Staining, Agarose Gel Electrophoresis, Amplification, Polymerase Chain Reaction, Produced, Binding Assay, Clone Assay, Immunohistochemistry

    Immunocytochemical detection of macrophages in the myocardium of LPL +/+ →C57BL/6 mice. Macrophages are stained with rat mAb MOMA-2 as the primary antibody, followed by biotinylated goat anti-rat IgG as the secondary antibody. The sections were incubated with avidin-biotin complex labeled with alkaline phosphatase, and the enzymatic activity was viewed with Fast Red TR/Naphthol AS-NX substrate. The sections were counterstained with hematoxylin. The primary antibody was omitted during the incubation of negative control sections, and no red staining was seen in these sections (data not shown). ×40.

    Journal: Journal of Clinical Investigation

    Article Title: Macrophage lipoprotein lipase promotes foam cell formation and atherosclerosis in vivo

    doi:

    Figure Lengend Snippet: Immunocytochemical detection of macrophages in the myocardium of LPL +/+ →C57BL/6 mice. Macrophages are stained with rat mAb MOMA-2 as the primary antibody, followed by biotinylated goat anti-rat IgG as the secondary antibody. The sections were incubated with avidin-biotin complex labeled with alkaline phosphatase, and the enzymatic activity was viewed with Fast Red TR/Naphthol AS-NX substrate. The sections were counterstained with hematoxylin. The primary antibody was omitted during the incubation of negative control sections, and no red staining was seen in these sections (data not shown). ×40.

    Article Snippet: The sections were treated with goat biotinylated antibodies to chicken IgG (Vector Laboratories, Burlingame, California, USA) or to rat IgG (PharMingen, San Diego, California, USA) for 45 minutes at 37°C.

    Techniques: Mouse Assay, Staining, Incubation, Avidin-Biotin Assay, Labeling, Activity Assay, Negative Control

    SPARC is detected in stromal PS1 cells but not INS-1 β cells by immunocytochemistry. INS-1 and PS1 cells were grown on coverslips, fixed using 10% NBF and stained using anti-SPARC antibody ( panels a–d ) or with biotinylated secondary antibody

    Journal: The Journal of Biological Chemistry

    Article Title: Novel Role for Matricellular Proteins in the Regulation of Islet β Cell Survival

    doi: 10.1074/jbc.M114.573980

    Figure Lengend Snippet: SPARC is detected in stromal PS1 cells but not INS-1 β cells by immunocytochemistry. INS-1 and PS1 cells were grown on coverslips, fixed using 10% NBF and stained using anti-SPARC antibody ( panels a–d ) or with biotinylated secondary antibody

    Article Snippet: For co-staining experiments, sections were incubated with SPARC goat antibody (1/50, R & D Systems) overnight at 4 °C, followed by incubation with biotinylated anti-goat antibody (Vector labs) for 1 h at room temperature.

    Techniques: Immunocytochemistry, Staining