goat anti rabbit secondary ab  (Bio-Rad)

 
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    Name:
    Goat anti Rabbit IgG IgM HRP Human Adsorbed
    Description:

    Catalog Number:
    STAR4010P
    Price:
    None
    Applications:
    Immunohistology, ELISA, Immunohistology - Paraffin Sections
    Format:
    HRP
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    Structured Review

    Bio-Rad goat anti rabbit secondary ab

    https://www.bioz.com/result/goat anti rabbit secondary ab/product/Bio-Rad
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    goat anti rabbit secondary ab - by Bioz Stars, 2021-01
    99/100 stars

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    Incubation:

    Article Title: Suppressor of cytokine signalling protein SOCS3 expression is increased at sites of acute and chronic inflammation
    Article Snippet: .. The blot was incubated with rabbit polyclonal anti-SOCS3 sera (ab16030 and ab53984) (ABCAM, Cambridge, UK) and bands detected with goat anti-rabbit horseradish peroxidase (HRP) (Biorad) and chemiluminescence (SuperSignal West Pico, Pierce). .. The blot was stripped and re-probed with rabbit anti-tubulin polyclonal antiserum (Cell Signaling Technology) to demonstrate equal protein loading in all lanes.

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    Bio-Rad anti immunoglobulin g horseradish peroxidase conjugate
    IRF7 binds to the an IRF7-RE located in the FXR promoter. (A) Electrophoretic Mobility shift assay (EMSA). Nuclear extracts from Raw264.7 cells left untreated or stimulated with CpG were incubated in the presence of a wild type or a mutated IRF7 biotin-labeled probe. Competition experiments were performed with a 100 fold excess of unlabeled oligo or with 1 µg IRF7 antibody. (B) Chromatin immunoprecipitation (ChIP). ChIP assay carried out in Raw264.7 cells left untreated or primed with CpG as described in materials and methods section. Values are normalized relative to input DNA concentration and are expressed relative to those of not treated cells immunoprecipitated with an anti <t>IgG</t> antibody, condition set as 1. Analysis was carried out in triplicate and the experiment was repeated twice. *P
    Anti Immunoglobulin G Horseradish Peroxidase Conjugate, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 317 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti immunoglobulin g horseradish peroxidase conjugate/product/Bio-Rad
    Average 99 stars, based on 317 article reviews
    Price from $9.99 to $1999.99
    anti immunoglobulin g horseradish peroxidase conjugate - by Bioz Stars, 2021-01
    99/100 stars
      Buy from Supplier

    92
    Bio-Rad hrp conjugated goat anti rabbit secondary antibody
    Selective binding of the C1 fusion protein of <t>IC140</t> to axonemes lacking the I1 complex. Increasing amounts of purified fusion protein were mixed and incubated with isolated axonemes from either pf28pf30, lacking the I1 complex (lanes a–d), or pf28 (lanes e–h) (see MATERIALS AND METHODS). (A) Western blots using anti-IC140 serum, which reveals the 53-kDa fusion protein (double arrowhead) and IC140 (arrowhead) and using <t>HRP</t> secondary antibodies and developed with chemiluminescent reagents. (B) Duplicate gel stained with Commasie brilliant blue, confirming equal loads for each sample.
    Hrp Conjugated Goat Anti Rabbit Secondary Antibody, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 92/100, based on 19 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hrp conjugated goat anti rabbit secondary antibody/product/Bio-Rad
    Average 92 stars, based on 19 article reviews
    Price from $9.99 to $1999.99
    hrp conjugated goat anti rabbit secondary antibody - by Bioz Stars, 2021-01
    92/100 stars
      Buy from Supplier

    N/A
    Antibody goat anti rabbit antibody conjugated to horseradish peroxidase HRP lyophilized for shipping and long term storage education use only
      Buy from Supplier

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    IRF7 binds to the an IRF7-RE located in the FXR promoter. (A) Electrophoretic Mobility shift assay (EMSA). Nuclear extracts from Raw264.7 cells left untreated or stimulated with CpG were incubated in the presence of a wild type or a mutated IRF7 biotin-labeled probe. Competition experiments were performed with a 100 fold excess of unlabeled oligo or with 1 µg IRF7 antibody. (B) Chromatin immunoprecipitation (ChIP). ChIP assay carried out in Raw264.7 cells left untreated or primed with CpG as described in materials and methods section. Values are normalized relative to input DNA concentration and are expressed relative to those of not treated cells immunoprecipitated with an anti IgG antibody, condition set as 1. Analysis was carried out in triplicate and the experiment was repeated twice. *P

    Journal: PLoS ONE

    Article Title: The Bile Acid Sensor FXR Is Required for Immune-Regulatory Activities of TLR-9 in Intestinal Inflammation

    doi: 10.1371/journal.pone.0054472

    Figure Lengend Snippet: IRF7 binds to the an IRF7-RE located in the FXR promoter. (A) Electrophoretic Mobility shift assay (EMSA). Nuclear extracts from Raw264.7 cells left untreated or stimulated with CpG were incubated in the presence of a wild type or a mutated IRF7 biotin-labeled probe. Competition experiments were performed with a 100 fold excess of unlabeled oligo or with 1 µg IRF7 antibody. (B) Chromatin immunoprecipitation (ChIP). ChIP assay carried out in Raw264.7 cells left untreated or primed with CpG as described in materials and methods section. Values are normalized relative to input DNA concentration and are expressed relative to those of not treated cells immunoprecipitated with an anti IgG antibody, condition set as 1. Analysis was carried out in triplicate and the experiment was repeated twice. *P

    Article Snippet: The anti-immunoglobulin G horseradish peroxidase conjugate (Bio-Rad) was used as the secondary antibody and specific protein bands were visualized using the Super Signal West Dura reagent (Pierce), following the manufacturer's suggested protocol.

    Techniques: Electrophoretic Mobility Shift Assay, Incubation, Labeling, Chromatin Immunoprecipitation, Concentration Assay, Immunoprecipitation

    Oxidative adducts are enhanced in experimental and human myocardium during Chagas disease. ( A ) Sprague-Dawley rats (or C3H/HeN mice) were infected with T. cruzi, and cells were harvested at day 40 (acute stage) and 180 (chronic stage) post-infection. Heart homogenates were resolved on 10% acrylamide gels, and Western blotting was performed with specific antibodies to detect 4 hydroxynonenal (4-HNE, panel a ), malondialdehyde (MDA, panel b ), dinitrophenyl (DNP)-derivatized carbonyl ( panel c ), and 3-nitrotyrosine (3NT, panel d ) adducts. Coomassie blue staining of membranes ( panel e ) confirmed the equal loading of samples. ( B ) Cryostat sections of human cardiac biopsies (5-µm) from normal healthy donors ( panels a, c, e ) and chagasic patients ( panels b, d, f ) were submitted to immunohistochemistry as described in Materials and Methods . Shown are representative images of immunostaining with anti-4-HNE antibodies ( panels a, b ). Tissue sections were incubated with DNPH to derivatize carbonyl proteins, and immunostaining was performed with anti-DNP antibody ( panels c–f ). HRP-conjugated ( panels a–d ) and rhodamine-conjugated ( panels e, f ) secondary antibodies were utilized to capture the color (brown) or fluorescence signal, respectively.

    Journal: PLoS ONE

    Article Title: Cardiac-Oxidized Antigens Are Targets of Immune Recognition by Antibodies and Potential Molecular Determinants in Chagas Disease Pathogenesis

    doi: 10.1371/journal.pone.0028449

    Figure Lengend Snippet: Oxidative adducts are enhanced in experimental and human myocardium during Chagas disease. ( A ) Sprague-Dawley rats (or C3H/HeN mice) were infected with T. cruzi, and cells were harvested at day 40 (acute stage) and 180 (chronic stage) post-infection. Heart homogenates were resolved on 10% acrylamide gels, and Western blotting was performed with specific antibodies to detect 4 hydroxynonenal (4-HNE, panel a ), malondialdehyde (MDA, panel b ), dinitrophenyl (DNP)-derivatized carbonyl ( panel c ), and 3-nitrotyrosine (3NT, panel d ) adducts. Coomassie blue staining of membranes ( panel e ) confirmed the equal loading of samples. ( B ) Cryostat sections of human cardiac biopsies (5-µm) from normal healthy donors ( panels a, c, e ) and chagasic patients ( panels b, d, f ) were submitted to immunohistochemistry as described in Materials and Methods . Shown are representative images of immunostaining with anti-4-HNE antibodies ( panels a, b ). Tissue sections were incubated with DNPH to derivatize carbonyl proteins, and immunostaining was performed with anti-DNP antibody ( panels c–f ). HRP-conjugated ( panels a–d ) and rhodamine-conjugated ( panels e, f ) secondary antibodies were utilized to capture the color (brown) or fluorescence signal, respectively.

    Article Snippet: Membranes were probed with sera from normal or chagasic rats, mice or human patients (1∶100 dilution) followed by HRP-conjugated secondary antibody (1∶5000, BioRad), and signal was detected by an ECL plus chemiluminiscence detection system (GE-Healthcare).

    Techniques: Mouse Assay, Infection, Western Blot, Multiple Displacement Amplification, Staining, Immunohistochemistry, Immunostaining, Incubation, Fluorescence

    Serum anti‐α‐Gal antibody response in COVID‐19 asymptomatic and symptomatic cases and healthy controls. A, The IgA, IgE, IgM and IgG anti‐α‐Gal antibody titers were determined by ELISA. Individuals were grouped as healthy controls ( n = 37), asymptomatic ( n = 10), hospital discharge ( n = 27), hospitalized ( n = 29) and ICU ( n = 25). The results were compared between different groups by one‐way ANOVA test ( p

    Journal: Journal of Medical Virology

    Article Title: The antibody response to the glycan α‐Gal correlates with COVID‐19 disease symptoms, et al. The antibody response to the glycan α‐Gal correlates with COVID‐19 disease symptoms

    doi: 10.1002/jmv.26575

    Figure Lengend Snippet: Serum anti‐α‐Gal antibody response in COVID‐19 asymptomatic and symptomatic cases and healthy controls. A, The IgA, IgE, IgM and IgG anti‐α‐Gal antibody titers were determined by ELISA. Individuals were grouped as healthy controls ( n = 37), asymptomatic ( n = 10), hospital discharge ( n = 27), hospitalized ( n = 29) and ICU ( n = 25). The results were compared between different groups by one‐way ANOVA test ( p

    Article Snippet: Plates were washed four times with PBST and 100 µl/well of goat anti‐human immunoglobulins‐peroxidase IgG (FC specific; Sigma‐Aldrich), IgM (µ‐chain specific; Sigma‐Aldrich), IgE (ɛ‐chain specific; Sigma‐Aldrich), and IgA (heavy chain specific; Bio‐Rad) secondary antibodies diluted 1:1000, v/v in blocking solution were added and incubated for 1 h at RT.

    Techniques: Enzyme-linked Immunosorbent Assay

    Selective binding of the C1 fusion protein of IC140 to axonemes lacking the I1 complex. Increasing amounts of purified fusion protein were mixed and incubated with isolated axonemes from either pf28pf30, lacking the I1 complex (lanes a–d), or pf28 (lanes e–h) (see MATERIALS AND METHODS). (A) Western blots using anti-IC140 serum, which reveals the 53-kDa fusion protein (double arrowhead) and IC140 (arrowhead) and using HRP secondary antibodies and developed with chemiluminescent reagents. (B) Duplicate gel stained with Commasie brilliant blue, confirming equal loads for each sample.

    Journal: Molecular Biology of the Cell

    Article Title: The Mr 140,000 Intermediate Chain of Chlamydomonas Flagellar Inner Arm Dynein Is a WD-Repeat Protein Implicated in Dynein Arm Anchoring

    doi:

    Figure Lengend Snippet: Selective binding of the C1 fusion protein of IC140 to axonemes lacking the I1 complex. Increasing amounts of purified fusion protein were mixed and incubated with isolated axonemes from either pf28pf30, lacking the I1 complex (lanes a–d), or pf28 (lanes e–h) (see MATERIALS AND METHODS). (A) Western blots using anti-IC140 serum, which reveals the 53-kDa fusion protein (double arrowhead) and IC140 (arrowhead) and using HRP secondary antibodies and developed with chemiluminescent reagents. (B) Duplicate gel stained with Commasie brilliant blue, confirming equal loads for each sample.

    Article Snippet: The membrane was blocked with 5% nonfat dry milk followed by incubation first with anti-IC140 antibody (1:3000–1:6000 dilution) and then with HRP-conjugated goat anti-rabbit secondary antibody (1:5000, Bio-Rad ).

    Techniques: Binding Assay, Purification, Incubation, Isolation, Western Blot, Staining