Figure 3
Figure 3. Binding affinity of anti-AP-FXIII monoclonal antibodies as measured by SPR. Sensorgrams of time (seconds) versus RUs are shown. (A) Binding of AP-FXIII-Val to mAb-6B11. The curves represent the association and dissociation rates of AP-FXIII-Val at the following concentrations: 2.5 (green), 5 (pink), 7.5 (cyan), 10 (magenta), 12 (dark blue), and 16nM (brown). (B) Binding of AP-FXIII-Val to mAb-1286 measured at the following concentrations: 5 (magenta), 7.5 (pink), 10 (green), 12.5 (cyan), 15 (dark blue), and 17.5nM brown). (C) Binding affinity data for mAb-6B11 and mAb-1286 and both AP-FXIII genotypes. The association rate constant ka, the dissociation rate constant kd and the equilibrium dissociation constant KD = kd/ka of 2 independent analyses (1st and 2nd) are shown, together with the average KD and range of variation.

Binding affinity of anti-AP-FXIII monoclonal antibodies as measured by SPR. Sensorgrams of time (seconds) versus RUs are shown. (A) Binding of AP-FXIII-Val to mAb-6B11. The curves represent the association and dissociation rates of AP-FXIII-Val at the following concentrations: 2.5 (green), 5 (pink), 7.5 (cyan), 10 (magenta), 12 (dark blue), and 16nM (brown). (B) Binding of AP-FXIII-Val to mAb-1286 measured at the following concentrations: 5 (magenta), 7.5 (pink), 10 (green), 12.5 (cyan), 15 (dark blue), and 17.5nM brown). (C) Binding affinity data for mAb-6B11 and mAb-1286 and both AP-FXIII genotypes. The association rate constant ka, the dissociation rate constant kd and the equilibrium dissociation constant KD = kd/ka of 2 independent analyses (1st and 2nd) are shown, together with the average KD and range of variation.

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