xy analyses – nonlinear regression (curve fit) Search Results


nonliner regression (curve fit) of xy analyses  (GraphPad Software Inc)
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GraphPad Software Inc nonliner regression (curve fit) of xy analyses
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.
Nonliner Regression (Curve Fit) Of Xy Analyses, supplied by GraphPad Software Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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xy analyses – nonlinear regression (curve fit)  (GraphPad Software Inc)
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GraphPad Software Inc xy analyses – nonlinear regression (curve fit)
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.
Xy Analyses – Nonlinear Regression (Curve Fit), supplied by GraphPad Software Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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xy analyses – nonlinear regression (curve fit) - by Bioz Stars, 2026-03
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nonlinear regression analysis of the dose-response curves using prism  (GraphPad Software Inc)
90
GraphPad Software Inc nonlinear regression analysis of the dose-response curves using prism
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.
Nonlinear Regression Analysis Of The Dose Response Curves Using Prism, supplied by GraphPad Software Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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prism’s nonliner regression  (GraphPad Software Inc)
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GraphPad Software Inc prism’s nonliner regression
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 <t>Nonliner</t> 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.
Prism’s Nonliner Regression, supplied by GraphPad Software Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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prism’s nonliner regression - by Bioz Stars, 2026-03
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nonlinear regression analyses of competitive curves using prism  (GraphPad Software Inc)
90
GraphPad Software Inc nonlinear regression analyses of competitive curves using prism
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 <t>Nonliner</t> 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.
Nonlinear Regression Analyses Of Competitive Curves Using Prism, supplied by GraphPad Software Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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nonlinear regression analyses of competitive curves using prism - by Bioz Stars, 2026-03
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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: 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

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