Mouse Anti-FMDV VP1 Recombinant Antibody (clone 4C4) (CAT#: HPAB-S0194-YC)

Figure 1 Correlation between thermodynamic affinity constant K_D and rate dissociation constant k_d.

Affinities of the different peptide analogues towards a same mAb, whether it was SD6, 4C4 or 3E5, were mainly determined by the dissociation rate constant, k_d.

Gomes, P., Giralt, E., & Andreu, D. (2000). Molecular analysis of peptides from the GH loop of foot-and-mouth disease virus C-S30 using surface plasmon resonance: a role for kinetic rate constants. Molecular Immunology, 37(16), 975-985.

Figure 2 (a) Neutralisation of FMDV as a function of the antibody 4C4-to-virion input ratio. (b) Neutralisation by antibody 4C4 fragments. The molar amounts of MAb Fab2 and Fab are indicated on the abscissa.

The neutralisation profile of FMDV C-S8c1 by MAb 4C4 indicates a reduction of 90% of infectivity over an antibody-to-virus input ratio of ~60. The neutralisation activity of the purified monovalent Fab was compared with that of the purified Fab2 and the intact MAb and no significant differences were found.

Verdaguer, N., Schoehn, G., Ochoa, W. F., Fita, I., Brookes, S., King, A., ... & Hewat, E. A. (1999). Flexibility of the major antigenic loop of foot-and-mouth disease virus bound to a Fab fragment of a neutralising antibody: structure and neutralisation. Virology, 255(2), 260-268.