Mouse Anti-Carbohydrate Recombinant Antibody (clone SE155-4) (CAT#: PABZ-018)

Figure 1 Scatchard plots for the determination of affinities from equilibrium binding.

A, monomeric wild-type scFv. B, dimeric B5-1. C, Se155-4 IgG.

MacKenzie, C. R., Hirama, T., Deng, S. J., Bundle, D. R., Narang, S. A., & Young, N. M. (1996). Analysis by surface plasmon resonance of the influence of valence on the ligand binding affinity and kinetics of an anti-carbohydrate antibody. Journal of Biological Chemistry, 271(3), 1527-1533.

Figure 2 Relative response versus time for the binding to immobilized BSA-O-polysaccharide of wild-type Se155-4 scFv containing trace amounts of dimer

(A), monomeric wild-type scFv obtained by size-exclusion HPLC (B), and mutant B5-1, which exists almost entirely in the dimeric form (C). The concentrations are (from bottom to top) 1, 1.5, 2, 3, and 5 μM in A; 0.2, 0.4, 0.8, 1.2, and 1.6 μM in B; and 20, 40, 80, 120, and 200 nM in C.

MacKenzie, C. R., Hirama, T., Deng, S. J., Bundle, D. R., Narang, S. A., & Young, N. M. (1996). Analysis by surface plasmon resonance of the influence of valence on the ligand binding affinity and kinetics of an anti-carbohydrate antibody. Journal of Biological Chemistry, 271(3), 1527-1533.

Figure 4 ELISA assays of wild-type and Cys94 modified forms of Se155-4.

IgG (filled square); unmodified scFv S94C (open square); S94C modified with iodoacetamide (filled triangle); scFv S94C modified with IANDB (filled inverted triangle); scFv S94C modified with Fe-BABE (open circle).

Young, N. M., Watson, D. C., Cunningham, A. M., & MacKenzie, C. R. (2014). The intrinsic cysteine and histidine residues of the anti-Salmonella antibody Se155-4: a model for the introduction of new functions into antibody-binding sites. Protein Engineering, Design & Selection, 27(10), 383-390.