Recombinant Human Anti-HGFA Antibody (Fab40.deltaTrp) (CAT#: PABX-083)

Figure 1 Superposition of the 99-loop of HGFA/Fab40.DTrp with the 99-loop of HGFA.

The conformation of the 99-loop (mustard) reverts almost back to the competent state in the Fab40.DTrp/HGFA complex structure. The CDR-H3 loop of Fab40. DTrp is highlighted in stick representation (orange).

Ganesan, R., Eigenbrot, C., Wu, Y., Liang, W. C., Shia, S., Lipari, M. T., & Kirchhofer, D. (2009). Unraveling the allosteric mechanism of serine protease inhibition by an antibody. Structure, 17(12), 1614-1624.

Figure 2 Effects of Active Site Inhibitors on Antibody Binding to HGFA.

(A, B, E, F) Surface plasmon resonance (BIAcore) measurements of binding to immobilized antibodies, Ab40 (A, B) or Ab40.DTrp (E, F), after coinjection of HGFA (A and E) or HGFA-KQLR (B and F) complex. (C) Competition binding (BIAcore) of HGFA to immobilized Ab40 in presence of different concentrations of KD1. (D) Competition binding ELISA measuring binding of HGFA to biotinylated KD1 in the presence of increasing antibody concentrations. Error bars represent SD.

Ganesan, R., Eigenbrot, C., Wu, Y., Liang, W. C., Shia, S., Lipari, M. T., & Kirchhofer, D. (2009). Unraveling the allosteric mechanism of serine protease inhibition by an antibody. Structure, 17(12), 1614-1624.

Figure 3 Partial inhibition of chromogenic substrate, S-2266 hydrolysis (expressed as HGFA fractional activity ni /no) by Ab40 and lack of inhibition by Ab40.DTrp.

Error bars represent standard deviation (SD).

Ganesan, R., Eigenbrot, C., Wu, Y., Liang, W. C., Shia, S., Lipari, M. T., & Kirchhofer, D. (2009). Unraveling the allosteric mechanism of serine protease inhibition by an antibody. Structure, 17(12), 1614-1625.