Recombinant Mouse Anti-αVβ3 Ectodomain Antibody Fab Fragment (17E6) (CAT#: PABX-191-F (E))

Figure 1 Effect of 17E6 on binding of FN to αVβ3.

Histograms (mean ± S.D.; n = 3) show relative binding of Alexa Fluor 488-labeled FN10 or FN9–10 (fl-FN) to αVβ3 stably expressed on K562, measured by flow cytometry. p values are shown above the histograms. Binding was carried out in 1 mm of Ca²⁺/plus 1 mm Mg²⁺ or 1 mm Mn²⁺ in the absence (−) or presence (+) of unlabeled 17E6 Fab.

Mahalingam, B., Van Agthoven, J. F., Xiong, J. P., Alonso, J. L., Adair, B. D., Rui, X., ... & Goodman, S. L. (2014). Atomic basis for the species-specific inhibition of αV integrins by mAb 17E6 is revealed by the crystal structure of αVβ3 ectodomain-17E6 Fab complex. Journal of Biological Chemistry, jbc-M113.

Figure 3 ELISA of 17E6 and fragments on purified αvβ3.

Intact 17E6 (triangles) its F(ab')2 (circles) or F(ab') (boxes) fragments at the indicated concentrations were allowed to bind plates coated at 1 mg mL^-1 with αvβ3 and bound antibody was detected. Vertival axis: optical density (OD) at 450 nm; horizontal axis: antibody (log10 µg/ml).

Figure 4 Cell attachment mediated by αvβ1 and αvβ5 but not by αvβ3 is blocked by 17E6 F(ab').

During M21 cell attachment to vitronectin, 17E6 F(ab') fragments or intact AP3 antibody at 0 (circle), 0.1(inverted triangles), 1.0 (boxes), or 10 µg/µl (triangles) were coincubated with the indicated concentrations of cross-linking anti-mouse second layer antibody. The cross linker showed identical ELISA affinities for 17E6 F(ab') and AP3, (not shown). Vertical axis: optical density (OD) at 405 nm; horizontal axis: Goat anti mouse antibody concentration (µg/ml).