Recombinant Mouse Anti-Progesterone  Antibody Fab Fragment (DB3) (CAT#: PABX-159-F (E))

Figure 1 Structure of the DB4 combining site.

(A) Crystal structure of the complex between DB3 and progesterone (Arevalo et al.1994a) showing some of the contact residues. Light and the heavy chains are in blue and purple, respectively; steroid oxygen atoms in red; steroid A-ring asterisked. (B) Mode

He, M., Hamon, M., Liu, H., Corper, A. L., & Taussig, M. J. (2006). Effects of mutation at the D‐JH junction on affinity, specificity, and idiotypy of anti‐progesterone antibody DB3. Protein science, 15(9), 2141-2149.

Figure 2 Western blot of wild type and mutants of DB4 VH/K.

Samples were run on 11% SDS-PAGE and electrotransferred to an Immobilon-P membrane (PVDF); the blot was probed with HRP-coupled sheep antimouse k.

He, M., Hamon, M., Liu, H., Corper, A. L., & Taussig, M. J. (2006). Effects of mutation at the D‐JH junction on affinity, specificity, and idiotypy of anti‐progesterone antibody DB3. Protein science, 15(9), 2141-2149.

Figure 3 Binding specificity of wild-type DB3 VH/K and the TrpH101Arg mutant for progesterone derivatives.

Binding to progesterone-BSA of wild-type DB3 VH/K (A) and the TrpH100Arg mutant (B) was carried out in the presence of free progesterone-3-CMO (C3-CMO), progesterone-6-HMS (C6-HMS), progesterone-11a-HMS (C11a-HMS),or progesterone-21-HMS (C22-HMS). ResultsȔ

He, M., Hamon, M., Liu, H., Corper, A. L., & Taussig, M. J. (2006). Effects of mutation at the D‐JH junction on affinity, specificity, and idiotypy of anti‐progesterone antibody DB3. Protein science, 15(9), 2141-2150.