Recombinant Human Anti-TF Antibody scFv Fragment (D3h44) (CAT#: PABX-177-S (P))

Figure 1 Binding of anti-TF antibodies to 6A6 antibody coated on the ELISA plate.

All antibodies analyzedwere antibody Fabs except the Herceptinw antibody, which is a full-length human antibody specific for the HER2 receptor. D3Ch is a chimeric antibody consisting of the D3H44 constant domains and murine D3 variable domains. D3H13 and D3H18 are variants of the D3H44 antibody.19 The two chimeric antibodies huVLmuVH and muVLhuVH are composed of the same D3H44 constant domains, but they combine a human and a murine variable domain. The Herceptinw antibody is identical with D3H44 except in the antigen combining region.

Eigenbrot, C., Meng, Y. G., Krishnamurthy, R., Lipari, M. T., Presta, L., Devaux, B., ... & Kirchhofer, D. (2003). Structural insight into how an anti-idiotypic antibody against D3H44 (anti-tissue factor antibody) restores normal coagulation. Journal of molecular biology, 331(2), 433-446.

Figure 2 Neutralization of D3H44 by 6A6.

Figure 2. Neutralization of D3H44 by 6A6 in TF/F.VIIa-mediated activation of F.X. 10 nM D3H44 (F(ab')2,Fab or IgG4b) was incubated with mTF1 – 263, F.VIIa(0.02 nM) and increasing concentrations of 6A6 antibodyfor 25 minutes in HBSA buffer. F.X (200 nM) was added and at various time-points reaction aliquots were withdrawn and analyzed for F.Xa in a second stage chromogenic substrate assay. The linear rates of initial of F.Xa formation were determined and are expressed as fractional activities (vi=vo): Open circles, D3H44-F(ab')2; triangles, D3H44-IgG4b; filled circles, D3H44-Fab; squares, 5G6 antibody.

Eigenbrot, C., Meng, Y. G., Krishnamurthy, R., Lipari, M. T., Presta, L., Devaux, B., ... & Kirchhofer, D. (2003). Structural insight into how an anti-idiotypic antibody against D3H44 (anti-tissue factor antibody) restores normal coagulation. Journal of molecular biology, 331(2), 433-446.

Figure 3 Open book views of the solvent-accessible surfaces buried in the (a) 6A6-Fab/D3H44-Fab and (b) TF/D3H44-Fab complexes.

Open book views of the solvent-accessible surfaces buried in the (a) 6A6-Fab/D3H44-Fab and (b) TF/D3H44-Fab complexes. The contact zones are colored by electrostatic potential (blue positive, red negative).

Eigenbrot, C., Meng, Y. G., Krishnamurthy, R., Lipari, M. T., Presta, L., Devaux, B., ... & Kirchhofer, D. (2003). Structural insight into how an anti-idiotypic antibody against D3H44 (anti-tissue factor antibody) restores normal coagulation. Journal of molecular biology, 331(2), 433-446.