Recombinant Mouse Anti-VEGF Antibody Fab Fragment (Fab-12) (CAT#: PABX-185-F (E))

Figure 1 Binding specificities and receptor blocking activities of the phage-derived antibodies.

A, sequences of four different phage clones initially identified were compared with template h4D5. Shaded residues were not randomized in the antibody libraries. The relative affinities for h-VEGF and m-VEGF were measured with competitive ELISA (EC50). The receptor blocking activities of the four clones were screened by measuring phage binding to m-VEGF-coated wells in the presence of either serial dilutions of VEGFR2 ECD (VEGFR2D1–7) (B) or second Ig domain of VEGFR1 ECD (VEGFR1D2) (C). D, binding specificities of G6 or B20-4 Fabs were measured by binding to h-VEGF (VEGF-A)-, m-VEGF-, h-PlGF-, m-PlGF-, m-VEGF-D-, or h-VEGF-B-coated wells, and bound Fab was detected. E, receptor blocking of Fab was confirmed by the binding of biotinylated m-VEGF to immobilized VEGFR2D1–7 in the presence of increasing concentration of G6, B20-4, Fab-12 (Fab of Avastin), or Y0317.

Liang, W. C., Wu, X., Peale, F. V., Lee, C. V., Meng, Y. G., Gutierrez, J., ... & Fuh, G. (2006). Cross-species vascular endothelial growth factor (VEGF)-blocking antibodies completely inhibit the growth of human tumor xenografts and measure the contribution of stromal VEGF. Journal of Biological Chemistry, 281(2), 951-961.