Recombinant Mouse Anti-Thrombopoietin Antibody scFv Fragment (TN1) (CAT#: PABX-178-S (P))

Figure 1 Results of TN1-Fab–hTPO163 binding measured using ITC.

(A) Titration calorimetry signals of TN1-Fab–hTPO163 binding reaction (lower line) with corresponding blank titration (upper line) at 298 K. (B) Integrated heat profile of the calorimetric titration at 298 K. Solid circles are integrated data. Solid line is a best-fit using a 1:1 binding model. (C) Temperature dependence plot of ∆Hobs, ∆G0, and -T∆S0. ∆G0 and -T∆S0 values were calculated using Equations (1) and (2). (D) –R ln Ka versus 1 / T plot. A linear least square fitting (dash line) by Equation (3) yields a slope of 24.4 kJ mol-1.

Arai, S., Shibazaki, C., Adachi, M., Honjo, E., Tamada, T., Maeda, Y., ... & Kuroki, R. (2016). An insight into the thermodynamic characteristics of human thrombopoietin complexation with TN1 antibody. Protein Science, 25(10), 1786-1796.

Figure 2 The overall structure of TN1-Fab.

(A) and (B) show the free TN1-Fab (PDB ID: 2ZKH, this work) and TN1-Fab–hTPO163 complex (PDB ID: 1V7M), respectively. For free TN1-Fab, the heavy and light chains are represented by red and yellow, respectively. For the TN1-Fab–hTPO163 complex, the heavy and light chains of TN1-Fab are represented by blue and green, respectively, and hTPO163 is depicted in gray. The dotted lines show the two pseudo-dyad axes generated by the superposition of CL on to CH1, and of VL on to VH.

Arai, S., Shibazaki, C., Adachi, M., Honjo, E., Tamada, T., Maeda, Y., ... & Kuroki, R. (2016). An insight into the thermodynamic characteristics of human thrombopoietin complexation with TN1 antibody. Protein Science, 25(10), 1786-1796.