streptavidin coated 96 well maxisorp plates  (Thermo Fisher)


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    Structured Review

    Thermo Fisher streptavidin coated 96 well maxisorp plates
    ), are shown. (B) Peptide A specificity of the MAbs in an ELISA. Biotin-conjugated peptide A was added to <t>streptavidin-coated</t> 96-well plates (200 ng/well). Each MAb (ascites fluid) was diluted 1:1,000 and used as the primary antibody. The y . An ELISA was performed with 1:20,000-diluted ascites fluid in the presence or absence of various concentrations of NaSCN as indicated. The specific binding affinity was calculated based on the values obtained with or without NaSCN. The data shown represent three independent experiments. Error bars represent the standard deviation.
    Streptavidin Coated 96 Well Maxisorp Plates, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/streptavidin coated 96 well maxisorp plates/product/Thermo Fisher
    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    streptavidin coated 96 well maxisorp plates - by Bioz Stars, 2020-05
    85/100 stars

    Related Products / Commonly Used Together

    biotin-conjugated peptide

    Images

    1) Product Images from "Amino Acid Residue-Specific Neutralization and Nonneutralization of Hepatitis C Virus by Monoclonal Antibodies to the E2 Protein"

    Article Title: Amino Acid Residue-Specific Neutralization and Nonneutralization of Hepatitis C Virus by Monoclonal Antibodies to the E2 Protein

    Journal: Journal of Virology

    doi: 10.1128/JVI.00994-12

    ), are shown. (B) Peptide A specificity of the MAbs in an ELISA. Biotin-conjugated peptide A was added to streptavidin-coated 96-well plates (200 ng/well). Each MAb (ascites fluid) was diluted 1:1,000 and used as the primary antibody. The y . An ELISA was performed with 1:20,000-diluted ascites fluid in the presence or absence of various concentrations of NaSCN as indicated. The specific binding affinity was calculated based on the values obtained with or without NaSCN. The data shown represent three independent experiments. Error bars represent the standard deviation.
    Figure Legend Snippet: ), are shown. (B) Peptide A specificity of the MAbs in an ELISA. Biotin-conjugated peptide A was added to streptavidin-coated 96-well plates (200 ng/well). Each MAb (ascites fluid) was diluted 1:1,000 and used as the primary antibody. The y . An ELISA was performed with 1:20,000-diluted ascites fluid in the presence or absence of various concentrations of NaSCN as indicated. The specific binding affinity was calculated based on the values obtained with or without NaSCN. The data shown represent three independent experiments. Error bars represent the standard deviation.

    Techniques Used: Enzyme-linked Immunosorbent Assay, Binding Assay, Standard Deviation

    Use of mutational analysis to identify the residues that are critical for antibody recognition. (A) Biotin-conjugated peptides were chemically synthesized to represent the truncated peptide B, i.e., B short, from the E2 protein of HCV genotype 1a (H77 strain) and its mutations. The B short mutant peptides contained a single alanine substitution at positions 437, 438, 440, 441, and 442, respectively. A hyphen indicates an amino acid residue identical to that of the H77 sequence. (B) Biotin-conjugated B short peptide and its mutants were added to streptavidin-coated 96-well plates at 200 ng/well in an ELISA. Each MAb (ascites fluid) was diluted 1:10 5 dilution, and applied as the primary antibody. The data shown represent at least three independent experiments. The x axis indicates the antibodies used in the assay. The y axis indicates the absorbance at 405 nm, representing specific binding of a given antibody to each individual peptide.
    Figure Legend Snippet: Use of mutational analysis to identify the residues that are critical for antibody recognition. (A) Biotin-conjugated peptides were chemically synthesized to represent the truncated peptide B, i.e., B short, from the E2 protein of HCV genotype 1a (H77 strain) and its mutations. The B short mutant peptides contained a single alanine substitution at positions 437, 438, 440, 441, and 442, respectively. A hyphen indicates an amino acid residue identical to that of the H77 sequence. (B) Biotin-conjugated B short peptide and its mutants were added to streptavidin-coated 96-well plates at 200 ng/well in an ELISA. Each MAb (ascites fluid) was diluted 1:10 5 dilution, and applied as the primary antibody. The data shown represent at least three independent experiments. The x axis indicates the antibodies used in the assay. The y axis indicates the absorbance at 405 nm, representing specific binding of a given antibody to each individual peptide.

    Techniques Used: Synthesized, Mutagenesis, Sequencing, Enzyme-linked Immunosorbent Assay, Binding Assay

    Related Articles

    Incubation:

    Article Title: Amino Acid Residue-Specific Neutralization and Nonneutralization of Hepatitis C Virus by Monoclonal Antibodies to the E2 Protein
    Article Snippet: .. Biotin-conjugated peptide (200 ng/well) was added to streptavidin-coated 96-well Maxisorp plates (Thermo Fisher Scientific, Rockford, IL), followed by incubation at room temperature for 1 h in Super Block blocking buffer (Thermo Scientific). .. After the plate was washed four times with phosphate-buffered saline (PBS; pH 7.4) containing 0.05% Tween 20 to remove unbound peptides, serial dilutions of the test antibodies were added to the plate, followed by incubation at 37°C for 1 h. The plate was then washed four times before the secondary antibody, either a goat anti-mouse peroxidase-conjugated IgG or a goat anti-human peroxidase-conjugated IgG (Sigma-Aldrich) at a 1:5,000 dilution, was added to the wells, followed by incubation at 37°C for 1 h. After four washes, the reaction was developed with ABTS [2,2′azinobis(3-ethylbenzthiazolinesulfonic acid)] peroxidase substrate (KPL, Gaithersburg, MD) and stopped by the addition of 100 μl of a 1% sodium dodecyl sulfate (SDS) solution.

    Blocking Assay:

    Article Title: Amino Acid Residue-Specific Neutralization and Nonneutralization of Hepatitis C Virus by Monoclonal Antibodies to the E2 Protein
    Article Snippet: .. Biotin-conjugated peptide (200 ng/well) was added to streptavidin-coated 96-well Maxisorp plates (Thermo Fisher Scientific, Rockford, IL), followed by incubation at room temperature for 1 h in Super Block blocking buffer (Thermo Scientific). .. After the plate was washed four times with phosphate-buffered saline (PBS; pH 7.4) containing 0.05% Tween 20 to remove unbound peptides, serial dilutions of the test antibodies were added to the plate, followed by incubation at 37°C for 1 h. The plate was then washed four times before the secondary antibody, either a goat anti-mouse peroxidase-conjugated IgG or a goat anti-human peroxidase-conjugated IgG (Sigma-Aldrich) at a 1:5,000 dilution, was added to the wells, followed by incubation at 37°C for 1 h. After four washes, the reaction was developed with ABTS [2,2′azinobis(3-ethylbenzthiazolinesulfonic acid)] peroxidase substrate (KPL, Gaithersburg, MD) and stopped by the addition of 100 μl of a 1% sodium dodecyl sulfate (SDS) solution.

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    Thermo Fisher streptavidin coated 96 well maxisorp plates
    ), are shown. (B) Peptide A specificity of the MAbs in an ELISA. Biotin-conjugated peptide A was added to <t>streptavidin-coated</t> 96-well plates (200 ng/well). Each MAb (ascites fluid) was diluted 1:1,000 and used as the primary antibody. The y . An ELISA was performed with 1:20,000-diluted ascites fluid in the presence or absence of various concentrations of NaSCN as indicated. The specific binding affinity was calculated based on the values obtained with or without NaSCN. The data shown represent three independent experiments. Error bars represent the standard deviation.
    Streptavidin Coated 96 Well Maxisorp Plates, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/streptavidin coated 96 well maxisorp plates/product/Thermo Fisher
    Average 85 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    streptavidin coated 96 well maxisorp plates - by Bioz Stars, 2020-05
    85/100 stars
      Buy from Supplier

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    ), are shown. (B) Peptide A specificity of the MAbs in an ELISA. Biotin-conjugated peptide A was added to streptavidin-coated 96-well plates (200 ng/well). Each MAb (ascites fluid) was diluted 1:1,000 and used as the primary antibody. The y . An ELISA was performed with 1:20,000-diluted ascites fluid in the presence or absence of various concentrations of NaSCN as indicated. The specific binding affinity was calculated based on the values obtained with or without NaSCN. The data shown represent three independent experiments. Error bars represent the standard deviation.

    Journal: Journal of Virology

    Article Title: Amino Acid Residue-Specific Neutralization and Nonneutralization of Hepatitis C Virus by Monoclonal Antibodies to the E2 Protein

    doi: 10.1128/JVI.00994-12

    Figure Lengend Snippet: ), are shown. (B) Peptide A specificity of the MAbs in an ELISA. Biotin-conjugated peptide A was added to streptavidin-coated 96-well plates (200 ng/well). Each MAb (ascites fluid) was diluted 1:1,000 and used as the primary antibody. The y . An ELISA was performed with 1:20,000-diluted ascites fluid in the presence or absence of various concentrations of NaSCN as indicated. The specific binding affinity was calculated based on the values obtained with or without NaSCN. The data shown represent three independent experiments. Error bars represent the standard deviation.

    Article Snippet: Biotin-conjugated peptide (200 ng/well) was added to streptavidin-coated 96-well Maxisorp plates (Thermo Fisher Scientific, Rockford, IL), followed by incubation at room temperature for 1 h in Super Block blocking buffer (Thermo Scientific).

    Techniques: Enzyme-linked Immunosorbent Assay, Binding Assay, Standard Deviation

    Use of mutational analysis to identify the residues that are critical for antibody recognition. (A) Biotin-conjugated peptides were chemically synthesized to represent the truncated peptide B, i.e., B short, from the E2 protein of HCV genotype 1a (H77 strain) and its mutations. The B short mutant peptides contained a single alanine substitution at positions 437, 438, 440, 441, and 442, respectively. A hyphen indicates an amino acid residue identical to that of the H77 sequence. (B) Biotin-conjugated B short peptide and its mutants were added to streptavidin-coated 96-well plates at 200 ng/well in an ELISA. Each MAb (ascites fluid) was diluted 1:10 5 dilution, and applied as the primary antibody. The data shown represent at least three independent experiments. The x axis indicates the antibodies used in the assay. The y axis indicates the absorbance at 405 nm, representing specific binding of a given antibody to each individual peptide.

    Journal: Journal of Virology

    Article Title: Amino Acid Residue-Specific Neutralization and Nonneutralization of Hepatitis C Virus by Monoclonal Antibodies to the E2 Protein

    doi: 10.1128/JVI.00994-12

    Figure Lengend Snippet: Use of mutational analysis to identify the residues that are critical for antibody recognition. (A) Biotin-conjugated peptides were chemically synthesized to represent the truncated peptide B, i.e., B short, from the E2 protein of HCV genotype 1a (H77 strain) and its mutations. The B short mutant peptides contained a single alanine substitution at positions 437, 438, 440, 441, and 442, respectively. A hyphen indicates an amino acid residue identical to that of the H77 sequence. (B) Biotin-conjugated B short peptide and its mutants were added to streptavidin-coated 96-well plates at 200 ng/well in an ELISA. Each MAb (ascites fluid) was diluted 1:10 5 dilution, and applied as the primary antibody. The data shown represent at least three independent experiments. The x axis indicates the antibodies used in the assay. The y axis indicates the absorbance at 405 nm, representing specific binding of a given antibody to each individual peptide.

    Article Snippet: Biotin-conjugated peptide (200 ng/well) was added to streptavidin-coated 96-well Maxisorp plates (Thermo Fisher Scientific, Rockford, IL), followed by incubation at room temperature for 1 h in Super Block blocking buffer (Thermo Scientific).

    Techniques: Synthesized, Mutagenesis, Sequencing, Enzyme-linked Immunosorbent Assay, Binding Assay