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non-linear regression analyses for drying curve fittings  (OriginLab corp)


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    OriginLab corp non-linear regression analyses for drying curve fittings
    Non Linear Regression Analyses For Drying Curve Fittings, supplied by OriginLab corp, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/non-linear regression analyses for drying curve fittings/product/OriginLab corp
    Average 90 stars, based on 1 article reviews
    non-linear regression analyses for drying curve fittings - by Bioz Stars, 2026-05
    90/100 stars

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    Binding and neutralizing activity of humanized anti-Abrin antibody S008. (A) S008 binds to abrin in a dose-dependent manner determined by ELISA. Absorbance values for different antibody concentrations (0.005 to 5 μg/mL) were detected at 450 nm. The EC50 value of S008 was 0.317 μg/mL, while that of 10D8 was 0.553 μg/mL, and EC50 values were calculated using GraphPad <t>Prism’s</t> Nonliner regression (curve fit) of XY analyses; (B) Kinetic analysis of antibody binding to abrin measured by the ForteBio method. Left: 10D8 (KD=0.2836 nmol/L); right: S008 (KD=0.2095 nmol/L). (C) Inhibition rate of protein synthesis induced by diluted recombinant abrin A chain treatment. The IC50 of protein synthesis in vitro was determined to be 0.01 μg/mL; (D) S008 and 10D8 neutralized the A chain and recovered protein synthesis in a dose-dependent manner. Left: luminescence values of 10D8 and S008. Positive control without abrin A chain, negative control without antibodies. (** P < 0.01, *** P < 0.001; ns, no significance). Right: Rates of protein synthesis by 10D8 and S008 were calculated using the equation (RLU of the experimental group)/(RLU of positive control group) ×100%. (E) Effect of different concentration of abrin on cell death. (F) S008 protected both Jurkat (left) and Vero (right) cells against abrin toxicity in a dose-dependent manner.
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    Binding and neutralizing activity of humanized anti-Abrin antibody S008. (A) S008 binds to abrin in a dose-dependent manner determined by ELISA. Absorbance values for different antibody concentrations (0.005 to 5 μg/mL) were detected at 450 nm. The EC50 value of S008 was 0.317 μg/mL, while that of 10D8 was 0.553 μg/mL, and EC50 values were calculated using GraphPad Prism’s Nonliner regression (curve fit) of XY analyses; (B) Kinetic analysis of antibody binding to abrin measured by the ForteBio method. Left: 10D8 (KD=0.2836 nmol/L); right: S008 (KD=0.2095 nmol/L). (C) Inhibition rate of protein synthesis induced by diluted recombinant abrin A chain treatment. The IC50 of protein synthesis in vitro was determined to be 0.01 μg/mL; (D) S008 and 10D8 neutralized the A chain and recovered protein synthesis in a dose-dependent manner. Left: luminescence values of 10D8 and S008. Positive control without abrin A chain, negative control without antibodies. (** P < 0.01, *** P < 0.001; ns, no significance). Right: Rates of protein synthesis by 10D8 and S008 were calculated using the equation (RLU of the experimental group)/(RLU of positive control group) ×100%. (E) Effect of different concentration of abrin on cell death. (F) S008 protected both Jurkat (left) and Vero (right) cells against abrin toxicity in a dose-dependent manner.

    Journal: Frontiers in Immunology

    Article Title: A Novel Humanized Anti-Abrin A Chain Antibody Inhibits Abrin Toxicity In Vitro and In Vivo

    doi: 10.3389/fimmu.2022.831536

    Figure Lengend Snippet: Binding and neutralizing activity of humanized anti-Abrin antibody S008. (A) S008 binds to abrin in a dose-dependent manner determined by ELISA. Absorbance values for different antibody concentrations (0.005 to 5 μg/mL) were detected at 450 nm. The EC50 value of S008 was 0.317 μg/mL, while that of 10D8 was 0.553 μg/mL, and EC50 values were calculated using GraphPad Prism’s Nonliner regression (curve fit) of XY analyses; (B) Kinetic analysis of antibody binding to abrin measured by the ForteBio method. Left: 10D8 (KD=0.2836 nmol/L); right: S008 (KD=0.2095 nmol/L). (C) Inhibition rate of protein synthesis induced by diluted recombinant abrin A chain treatment. The IC50 of protein synthesis in vitro was determined to be 0.01 μg/mL; (D) S008 and 10D8 neutralized the A chain and recovered protein synthesis in a dose-dependent manner. Left: luminescence values of 10D8 and S008. Positive control without abrin A chain, negative control without antibodies. (** P < 0.01, *** P < 0.001; ns, no significance). Right: Rates of protein synthesis by 10D8 and S008 were calculated using the equation (RLU of the experimental group)/(RLU of positive control group) ×100%. (E) Effect of different concentration of abrin on cell death. (F) S008 protected both Jurkat (left) and Vero (right) cells against abrin toxicity in a dose-dependent manner.

    Article Snippet: EC50 values were calculated using GraphPad Prism’s Nonliner regression (curve fit) of XY analyses with the formula Y=Bottom+(Top-Bottom)/(1 + 10^((LogEC50-X) ×HillSlope)).

    Techniques: Binding Assay, Activity Assay, Enzyme-linked Immunosorbent Assay, Inhibition, Recombinant, In Vitro, Positive Control, Negative Control, Concentration Assay

    Binding and neutralizing activity of humanized anti-Abrin antibody S008. (A) S008 binds to abrin in a dose-dependent manner determined by ELISA. Absorbance values for different antibody concentrations (0.005 to 5 μg/mL) were detected at 450 nm. The EC50 value of S008 was 0.317 μg/mL, while that of 10D8 was 0.553 μg/mL, and EC50 values were calculated using GraphPad Prism’s Nonliner regression (curve fit) of XY analyses; (B) Kinetic analysis of antibody binding to abrin measured by the ForteBio method. Left: 10D8 (KD=0.2836 nmol/L); right: S008 (KD=0.2095 nmol/L). (C) Inhibition rate of protein synthesis induced by diluted recombinant abrin A chain treatment. The IC50 of protein synthesis in vitro was determined to be 0.01 μg/mL; (D) S008 and 10D8 neutralized the A chain and recovered protein synthesis in a dose-dependent manner. Left: luminescence values of 10D8 and S008. Positive control without abrin A chain, negative control without antibodies. (** P < 0.01, *** P < 0.001; ns, no significance). Right: Rates of protein synthesis by 10D8 and S008 were calculated using the equation (RLU of the experimental group)/(RLU of positive control group) ×100%. (E) Effect of different concentration of abrin on cell death. (F) S008 protected both Jurkat (left) and Vero (right) cells against abrin toxicity in a dose-dependent manner.

    Journal: Frontiers in Immunology

    Article Title: A Novel Humanized Anti-Abrin A Chain Antibody Inhibits Abrin Toxicity In Vitro and In Vivo

    doi: 10.3389/fimmu.2022.831536

    Figure Lengend Snippet: Binding and neutralizing activity of humanized anti-Abrin antibody S008. (A) S008 binds to abrin in a dose-dependent manner determined by ELISA. Absorbance values for different antibody concentrations (0.005 to 5 μg/mL) were detected at 450 nm. The EC50 value of S008 was 0.317 μg/mL, while that of 10D8 was 0.553 μg/mL, and EC50 values were calculated using GraphPad Prism’s Nonliner regression (curve fit) of XY analyses; (B) Kinetic analysis of antibody binding to abrin measured by the ForteBio method. Left: 10D8 (KD=0.2836 nmol/L); right: S008 (KD=0.2095 nmol/L). (C) Inhibition rate of protein synthesis induced by diluted recombinant abrin A chain treatment. The IC50 of protein synthesis in vitro was determined to be 0.01 μg/mL; (D) S008 and 10D8 neutralized the A chain and recovered protein synthesis in a dose-dependent manner. Left: luminescence values of 10D8 and S008. Positive control without abrin A chain, negative control without antibodies. (** P < 0.01, *** P < 0.001; ns, no significance). Right: Rates of protein synthesis by 10D8 and S008 were calculated using the equation (RLU of the experimental group)/(RLU of positive control group) ×100%. (E) Effect of different concentration of abrin on cell death. (F) S008 protected both Jurkat (left) and Vero (right) cells against abrin toxicity in a dose-dependent manner.

    Article Snippet: IC50 values were calculated using GraphPad Prism’s Nonliner regression (curve fit) of XY analyses with the formula Y=Bottom+(Top-Bottom)/(1 + 10^((LogIC50-X) ×HillSlope)).

    Techniques: Binding Assay, Activity Assay, Enzyme-linked Immunosorbent Assay, Inhibition, Recombinant, In Vitro, Positive Control, Negative Control, Concentration Assay