Recombinant Human Antibody (19.3H-L3) is capable of binding to HIV-1 gp120, expressed in HEK 293 cells. Expressed as the combination of a heavy chain (HC) containing VH from anti-HIV-1 gp120 mAb and CH1-3 region of human IgG and a light chain (LC) encoding VL from anti-HIV-1 gp120 proteins mAb and CL of human light chain. Exists as a disulfide linked dimer of the HC and LC hetero-dimer under non-reducing condition. Crystal structures revealed flat epitope contact surfaces, where minimal light chain mutation in 19.3H-L3 allowed for additional antigenic interactions.
Figure 1 gp120 binding by and competition of R880F mAbs 19.3H-L1 and 19.3H-L3.
The baseline binding of four biotinylated mAbs, 19.3H-L1, 19.3H-L3, 6.4C, or PGT128, was evaluated by ELISA with three R880F gp120 proteins: (A) wild-type 0-A6/B24, (B) point mutant 0-A6/B24 I295R, and (C) point mutant 0-A6/B24 E338K. R880F mAbs 19.3H-L1 and 19.3H-L3 were then competed with themselves, each other, and the negative control antibody, 6.4C. For the competition ELISAs, plates were coated with wild-type R880F 0-A6/B24 gp120 protein, pre-incubated with serially-diluted 19.3H-L1, 19.3H-L3, or 6.4C, washed, and then incubated with 1 µg/ml biotinylated 19.3H-L1 (D) or 19.3H-L3 (E). From data in (A), 1 µg/ml was selected as a point of non-saturated binding. The horizontal dashed lines in (D) and (E) represent 100% binding of biotinylated 19.3H-L1 or 19.3H-L3, at 1 µg/ml in the absence of competitor, respectively. Optical density values at 450 nm are depicted on the vertical axis; mAb concentrations (in µg/ml) are plotted along the horizontal axis in a logarithmic fashion. Error bars demonstrate the standard error of the mean of two independent experiments.
Murphy, M. K., Yue, L., Pan, R., Boliar, S., Sethi, A., Tian, J., ... & Goepfert, P. A. (2013). Viral escape from neutralizing antibodies in early subtype A HIV-1 infection drives an increase in autologous neutralization breadth. PLoS pathogens, 9(2), e1003173.
Figure 2 Heterologous neutralization breadth in R880F.
The two R880F mAbs, 19.3H-L1 (A) and 19.3H-L3 (B), in conjunction with 16-month (C) and 3-year (D) autologous plasma were evaluated for cross-neutralizing capacity against virions pseudotyped with fourteen heterologous HIV-1 Envs from three clades (A/C recombinant and subtype A Envs = lavender, subtype B Envs = coral, subtype C Envs = teal).
Murphy, M. K., Yue, L., Pan, R., Boliar, S., Sethi, A., Tian, J., ... & Goepfert, P. A. (2013). Viral escape from neutralizing antibodies in early subtype A HIV-1 infection drives an increase in autologous neutralization breadth. PLoS pathogens, 9(2), e1003173.
This is a product of Creative Biolabs' Hi-Affi™ recombinant antibody portfolio, which has several benefits including:
• Increased sensitivity
• Confirmed specificity
• High repeatability
• Excellent batch-to-batch consistency
• Sustainable supply
• Animal-free production
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CAT | Product Name | Application | Type |
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PABL-380 | Human Anti-HIV-1 gp120 Recombinant Antibody (clone VRC06) | FC, Neut, FuncS | Human IgG |
PABL-520 | Human Anti-HIV-1 gp120 Recombinant Antibody (clone 44-VRC13.01) | Neut | Human IgG |
PABL-521 | Human Anti-HIV-1 gp120 Recombinant Antibody (PABL-521) | ELISA, Neut | Human IgG |
PABL-522 | Human Anti-HIV-1 gp120 Recombinant Antibody (clone 45-VRC01.H5.F-185917) | WB, FuncS | Human IgG |
PABL-523 | Human Anti-HIV-1 gp120 Recombinant Antibody (clone 8ANC131) | WB, FuncS | Human IgG |
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