Recombinant Human Antibody (5J7) is capable of binding to DENV E proteins, expressed in HEK 293 cells. Expressed as the combination of a heavy chain (HC) containing VH from anti-DENV E proteins mAb and CH1-3 region of human IgG1 and a light chain (LC) encoding VL from anti-DENV E proteins mAb and CL of human kappa light chain. Exists as a disulfide linked dimer of the HC and LC hetero-dimer under non-reducing condition. This antibody is exceptionally potent, neutralizing 50% of virus at nanogram-range antibody concentration.
Figure 1 Serotype-specific strongly neutralizing E protein binding human MAbs.
(A) The ability of purified human MAb 5J7 to neutralize the four serotypes of DENV is shown over a concentration range. (B) The ability of purified human MAb 2D22 to neutralize the four serotypes of dengue virus is shown over a concentration range. (C) Purified human MAb 5J7 neutralization of serotype 3 virus over a detailed, broader range of halving dilutions. (D) Purified human MAb 2D22 neutralization of serotype 2 virus over a detailed range of halving dilutions. Flow cytometric neutralization assays were performed using U937-DC-SIGN cells.
Smith, S.A., Zhou, Y., Olivarez, N.P., et al. Persistence of Circulating Memory B Cell Clones with Potential for Dengue Virus Disease Enhancement for Decades following Infection. Journal of Virology, 2665-2675.
Figure 2 ELISA of sE-cvD from DENV serotypes 2, 3 and 4 and ZIKV with the indicated mAbs (left panel). Control antigens, 4DIII, 4DI/DII and 4sE wt were also reacted with the same set of antibodies (right panel).
Slon Campos, J.L., Marchese, S., Rana, J., Mossenta, M., Poggianella, M., Bestagno, M., Burrone, O.R. (2017). Temperature-dependent folding allows stable dimerization of secretory and virus-associated E proteins of Dengue and Zika viruses in mammalian cells. Scientific Report, 7(966).
Figure 3 Cytofluorimetric analysis of HEK-293T cells transfected with the membrane display sE-cvD versions of all four DENV serotypes and ZIKV at 37 °C or 28 °C and reacted with the indicated mAbs. Mock-transfected HEK-293T cells incubated with each mAb served as controls.
Slon Campos, J.L., Marchese, S., Rana, J., Mossenta, M., Poggianella, M., Bestagno, M., Burrone, O.R. (2017). Temperature-dependent folding allows stable dimerization of secretory and virus-associated E proteins of Dengue and Zika viruses in mammalian cells. Scientific Report, 7(966).
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CAT | Product Name | Application | Type |
---|---|---|---|
PABL-063 | Recombinant Human Anti-DENV E proteins Antibody | WB, Neut, FuncS | IgG |
PABL-064 | Recombinant Human Anti-DENV E proteins Antibody (1F4) | Neut, FuncS | IgG |
PABL-065 | Recombinant Human Anti-DENV E proteins Antibody (PABL-065) | WB, BL, FuncS | IgG |
PABL-066 | Recombinant Chimpanzee Anti-DENV E proteins Antibody (5H2) | WB, ELISA, FuncS | IgG |
PABL-068 | Recombinant Mouse Anti-DENV E proteins Antibody (Ab513) | WB, ELISA, Neut, FuncS | IgG |
To accurately reference this product in your publication, please use the following citation information:
(Creative Biolabs Cat# PABL-067, RRID: AB_3111624)
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For research use only. Not intended for any clinical use. No products from Creative Biolabs may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative Biolabs.
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