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biotinylated irrelevant antigen  (R&D Systems)


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    Structured Review

    R&D Systems biotinylated irrelevant antigen
    High-throughput binding and bioactivity screen allows identification of unique J.HAL® IgG candidates that bind SARS-CoV-2 spike protein and effectively block spike:Human ACE2 receptor interaction. (A and B) Unpurified transfection supernatants from two independent screens were tested by AlphaLISA for binding to <t>biotinylated</t> SARS-CoV-2 spike protein and in parallel to biotinylated irrelevant target protein. Positive control antibody M-3418 (S309) demonstrates binding specificity, whereas isotype control antibody demonstrates lack of binding. Data were graphed using GraphPad prism software. (C and D) Unpurified transfection supernatants from two independent screens were tested for their ability to block binding of SARS-CoV-2 spike protein to human ACE-2 using ELISA. Positive control antibody M-2381 (red symbol) demonstrates effective blockade, whereas isotype control antibody demonstrates lack thereof. Data were graphed as % inhibition +/− SD using GraphPad prism software.
    Biotinylated Irrelevant Antigen, supplied by R&D Systems, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/biotinylated+irrelevant+antigen/Recombinant+Human+ULBP-2+His-tag+Avi-tag+Protein%2C+CF/pmc11456866-155-39-46
    Average 92 stars, based on 1 article reviews
    biotinylated irrelevant antigen - by Bioz Stars, 2026-09
    92/100 stars

    Images

    1) Product Images from "AI-based antibody discovery platform identifies novel, diverse, and pharmacologically active therapeutic antibodies against multiple SARS-CoV-2 strains"

    Article Title: AI-based antibody discovery platform identifies novel, diverse, and pharmacologically active therapeutic antibodies against multiple SARS-CoV-2 strains

    Journal: Antibody Therapeutics

    doi: 10.1093/abt/tbae025

    High-throughput binding and bioactivity screen allows identification of unique J.HAL® IgG candidates that bind SARS-CoV-2 spike protein and effectively block spike:Human ACE2 receptor interaction. (A and B) Unpurified transfection supernatants from two independent screens were tested by AlphaLISA for binding to biotinylated SARS-CoV-2 spike protein and in parallel to biotinylated irrelevant target protein. Positive control antibody M-3418 (S309) demonstrates binding specificity, whereas isotype control antibody demonstrates lack of binding. Data were graphed using GraphPad prism software. (C and D) Unpurified transfection supernatants from two independent screens were tested for their ability to block binding of SARS-CoV-2 spike protein to human ACE-2 using ELISA. Positive control antibody M-2381 (red symbol) demonstrates effective blockade, whereas isotype control antibody demonstrates lack thereof. Data were graphed as % inhibition +/− SD using GraphPad prism software.
    Figure Legend Snippet: High-throughput binding and bioactivity screen allows identification of unique J.HAL® IgG candidates that bind SARS-CoV-2 spike protein and effectively block spike:Human ACE2 receptor interaction. (A and B) Unpurified transfection supernatants from two independent screens were tested by AlphaLISA for binding to biotinylated SARS-CoV-2 spike protein and in parallel to biotinylated irrelevant target protein. Positive control antibody M-3418 (S309) demonstrates binding specificity, whereas isotype control antibody demonstrates lack of binding. Data were graphed using GraphPad prism software. (C and D) Unpurified transfection supernatants from two independent screens were tested for their ability to block binding of SARS-CoV-2 spike protein to human ACE-2 using ELISA. Positive control antibody M-2381 (red symbol) demonstrates effective blockade, whereas isotype control antibody demonstrates lack thereof. Data were graphed as % inhibition +/− SD using GraphPad prism software.

    Techniques Used: High Throughput Screening Assay, Binding Assay, Blocking Assay, Transfection, Positive Control, Control, Software, Enzyme-linked Immunosorbent Assay, Inhibition

    J.HAL® IgG antibodies exhibit dose-dependent binding to SARS-CoV-2 spike protein. Unpurified transfection supernatants were concentration normalized and tested for binding in a 9-point serial titration series to biotinylated SARS-CoV-2 spike protein by AlphaLISA. Representative binding profiles for 30 J.HAL® antibodies are shown in the subplots A-F above, along with the positive control antibody M-3418 (S309). Data were graphed as mean +/− SD using GraphPad prism software.
    Figure Legend Snippet: J.HAL® IgG antibodies exhibit dose-dependent binding to SARS-CoV-2 spike protein. Unpurified transfection supernatants were concentration normalized and tested for binding in a 9-point serial titration series to biotinylated SARS-CoV-2 spike protein by AlphaLISA. Representative binding profiles for 30 J.HAL® antibodies are shown in the subplots A-F above, along with the positive control antibody M-3418 (S309). Data were graphed as mean +/− SD using GraphPad prism software.

    Techniques Used: Binding Assay, Transfection, Concentration Assay, Titration, Positive Control, Software



    Similar Products

    biotinylated irrelevant antigen  (R&D Systems)
    92
    R&D Systems biotinylated irrelevant antigen
    High-throughput binding and bioactivity screen allows identification of unique J.HAL® IgG candidates that bind SARS-CoV-2 spike protein and effectively block spike:Human ACE2 receptor interaction. (A and B) Unpurified transfection supernatants from two independent screens were tested by AlphaLISA for binding to <t>biotinylated</t> SARS-CoV-2 spike protein and in parallel to biotinylated irrelevant target protein. Positive control antibody M-3418 (S309) demonstrates binding specificity, whereas isotype control antibody demonstrates lack of binding. Data were graphed using GraphPad prism software. (C and D) Unpurified transfection supernatants from two independent screens were tested for their ability to block binding of SARS-CoV-2 spike protein to human ACE-2 using ELISA. Positive control antibody M-2381 (red symbol) demonstrates effective blockade, whereas isotype control antibody demonstrates lack thereof. Data were graphed as % inhibition +/− SD using GraphPad prism software.
    Biotinylated Irrelevant Antigen, supplied by R&D Systems, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/biotinylated+irrelevant+antigen/Recombinant+Human+ULBP-2+His-tag+Avi-tag+Protein%2C+CF/pmc11456866-155-39-46
    Average 92 stars, based on 1 article reviews
    biotinylated irrelevant antigen - by Bioz Stars, 2026-09
    92/100 stars
    		  Buy from Supplier

    Image Search Results


    High-throughput binding and bioactivity screen allows identification of unique J.HAL® IgG candidates that bind SARS-CoV-2 spike protein and effectively block spike:Human ACE2 receptor interaction. (A and B) Unpurified transfection supernatants from two independent screens were tested by AlphaLISA for binding to biotinylated SARS-CoV-2 spike protein and in parallel to biotinylated irrelevant target protein. Positive control antibody M-3418 (S309) demonstrates binding specificity, whereas isotype control antibody demonstrates lack of binding. Data were graphed using GraphPad prism software. (C and D) Unpurified transfection supernatants from two independent screens were tested for their ability to block binding of SARS-CoV-2 spike protein to human ACE-2 using ELISA. Positive control antibody M-2381 (red symbol) demonstrates effective blockade, whereas isotype control antibody demonstrates lack thereof. Data were graphed as % inhibition +/− SD using GraphPad prism software.

    Journal: Antibody Therapeutics

    Article Title: AI-based antibody discovery platform identifies novel, diverse, and pharmacologically active therapeutic antibodies against multiple SARS-CoV-2 strains

    doi: 10.1093/abt/tbae025

    Figure Lengend Snippet: High-throughput binding and bioactivity screen allows identification of unique J.HAL® IgG candidates that bind SARS-CoV-2 spike protein and effectively block spike:Human ACE2 receptor interaction. (A and B) Unpurified transfection supernatants from two independent screens were tested by AlphaLISA for binding to biotinylated SARS-CoV-2 spike protein and in parallel to biotinylated irrelevant target protein. Positive control antibody M-3418 (S309) demonstrates binding specificity, whereas isotype control antibody demonstrates lack of binding. Data were graphed using GraphPad prism software. (C and D) Unpurified transfection supernatants from two independent screens were tested for their ability to block binding of SARS-CoV-2 spike protein to human ACE-2 using ELISA. Positive control antibody M-2381 (red symbol) demonstrates effective blockade, whereas isotype control antibody demonstrates lack thereof. Data were graphed as % inhibition +/− SD using GraphPad prism software.

    Article Snippet: Briefly, 10 μl of unpurified transfection supernatant diluted 1:200 in 1x Immunoassay buffer (Perkin Elmer cat# AL000F) was preincubated with either 10 μl biotinylated SARS-CoV-2 spike protein (3 nM final concentration; R&D Systems cat# BT10549) or with 10 μl biotinylated irrelevant antigen (3 nM final concentration; R&D Systems cat# AVI10538–050) for 20 min at RT in 96 half-area white microplates (Corning cat# CLS3693).

    Techniques: High Throughput Screening Assay, Binding Assay, Blocking Assay, Transfection, Positive Control, Control, Software, Enzyme-linked Immunosorbent Assay, Inhibition

    J.HAL® IgG antibodies exhibit dose-dependent binding to SARS-CoV-2 spike protein. Unpurified transfection supernatants were concentration normalized and tested for binding in a 9-point serial titration series to biotinylated SARS-CoV-2 spike protein by AlphaLISA. Representative binding profiles for 30 J.HAL® antibodies are shown in the subplots A-F above, along with the positive control antibody M-3418 (S309). Data were graphed as mean +/− SD using GraphPad prism software.

    Journal: Antibody Therapeutics

    Article Title: AI-based antibody discovery platform identifies novel, diverse, and pharmacologically active therapeutic antibodies against multiple SARS-CoV-2 strains

    doi: 10.1093/abt/tbae025

    Figure Lengend Snippet: J.HAL® IgG antibodies exhibit dose-dependent binding to SARS-CoV-2 spike protein. Unpurified transfection supernatants were concentration normalized and tested for binding in a 9-point serial titration series to biotinylated SARS-CoV-2 spike protein by AlphaLISA. Representative binding profiles for 30 J.HAL® antibodies are shown in the subplots A-F above, along with the positive control antibody M-3418 (S309). Data were graphed as mean +/− SD using GraphPad prism software.

    Article Snippet: Briefly, 10 μl of unpurified transfection supernatant diluted 1:200 in 1x Immunoassay buffer (Perkin Elmer cat# AL000F) was preincubated with either 10 μl biotinylated SARS-CoV-2 spike protein (3 nM final concentration; R&D Systems cat# BT10549) or with 10 μl biotinylated irrelevant antigen (3 nM final concentration; R&D Systems cat# AVI10538–050) for 20 min at RT in 96 half-area white microplates (Corning cat# CLS3693).

    Techniques: Binding Assay, Transfection, Concentration Assay, Titration, Positive Control, Software