Recombinant Mouse Anti-AaHI Antibody (Fab9C2) (CAT#: PABX-005)

Figure 1 Analysis of the protein L-purified rFab 9C2 preparation.

Western blot (C) analysis under nonreducing (lanes 1–3) and reducing (lane 4) conditions. Lane 1: molecular weight markers; lane 2: periplasmic proteins from induced bacteria; lanes 3 and 4: protein L-purified rFab preparation.

Aubrey, N., Muzard, J., Peter, J. C., Rochat, H., Goyffon, M., Devaux, C., & Billiald, P. (2004). Engineering of a recombinant Fab from a neutralizing IgG directed against scorpion neurotoxin AahI, and functional evaluation versus other antibody fragments. Toxicon, 43(3), 233-241.

Figure 2 Functional quality of the purified Fabs.

A, shown is ELISA analysis of binding of coated AahI, AahII, and AahIII by IgG4C1 and IgG9C2 (direct binding; squares) and by Fab4C1 and Fab9C2 (competitive binding; circles). The competition assays used IgG9C2 at 10⁻⁸ and IgG4C1 at 10⁻⁷ M. In each case, the Fab concentration at the intersect of the direct and competition curves, close to the IgG EC₅₀ value, assess for Fab retention of the IgG binding capacity.

Fabrichny, I. P., Mondielli, G., Conrod, S., Martin-Eauclaire, M. F., Bourne, Y., & Marchot, P. (2012). Structural insights into antibody sequestering and neutralizing of Na+ channel α-type modulator from old world scorpion venom. Journal of Biological Chemistry, 287(17), 14136-14148.