Mouse Anti-HIV-1 p24 Recombinant Antibody (clone CB4-1) (CAT#: PABW-069)

Figure 1 Deconvolution of the excess heat capacity functions of CB4-1 (A), Fab CB4-1 (B) and Fc CB4-1 (C).

Solid curves represent baseline corrected experimental endotherms and dashed curves show the component two-state transitions obtained by deconvolution. The transitions of CB4-1 are numbered from 1 to 5. The sums of the component transitions shown as dashed lines closely ¢t the experimental curves.

Welfle, K. , Misselwitz, R. , Hausdorf, G. , Höhne W, & Welfle, H. . (1999). Conformation, ph-induced conformational changes, and thermal unfolding of anti-p24 (hiv-1) monoclonal antibody cb4-1 and its fab and fc fragments. Biochimica Et Biophysica Acta, 1431(1), 120.

Figure 2 Dissociation Constants of CB4-1 Interacting with UmuD and Candiapepsin and Influences of CB4-1 Mutations on Peptide and Protein Recognition.

(A) Inhibition of CB4-1-p24 interaction by p24, UmuD, and candidapepsin determined by competitive ELISA. Soluble proteins compete with solid phase-adsorbed p24 for CB4-1 binding. 1/c (c = concentration of the inhibitors) is plotted versus E0/(E0-EX) (E = extinction with no inhibitor (0) and various inhibitor concentrations [x]). The slope of the fitted curves correspond to the inhibition constants (Friguet et al. 1985).

(B) BIAcore measurements of UmuD interacting with solid phase-linked CB4-1. Overlay plot of various concentrations of UmuD (50 μM, 12.5 μM, 3.1 μM, and 0.78 μM [sensograms 1–4, respectively]) captured by CB4-1-coated chips. Samples were injected at t = 0 s. Dissociation started at t = 300 s. The association rate constant kon was determined as 3.0 × 103 M-1s-1, the dissociation rate constants koff as 6.0 × 103 s-1 resulting in Kd = 2.0 × 10−6 M.

(C) CB4-1 single chain mutants VL:Phe94Ala and VH:Tyr32Ala as well as the wild-type CB4-1 single chain Fv fragment (wt) were tested for their ability to recognize immobilized peptide 1 (GATPEDLNQKLAGN) and peptide 2 (GLYEWGGARITNTD) as well as alcohol dehydrogenase (supertope 1-derived) and candidapepsin (supertope 2-derived). Binding of the CB4-1 single chains carrying the c-myc-tag were detected using the anti-c-myc antibody 9E10 and a peroxidase-conjugated anti-mouse antibody.

Kramer, A. . (1997). Molecular basis for the binding promiscuity an anti-p24 (hiv-1) monoclonal antibody. Cell, 91(6), 799-809.