This product is a recombinant Mouse antibody that can recognize EBV gH/gL. E1D1 partially blocks membrane fusion with epithelial cells, but not B cells.
Figure 1 gHgL mutant surface expression and conformation was monitored using anti-gHgL E1D1, CL40 and CL59 monoclonal antibodies and HL800 polyclonal serum using a cell ELISA assay.
The results are expressed as % change in antibody binding relative to wt, with most antibodies showing no changes in binding to the mutants relative to the wt gHgL (values near zero represent wt binding). E1D1 binding is selectively lost for mutations in gl residues gl:L74, glL:176 and glL:Y131. n.d., not detected. A western blot of the gi N69 glycosylation mutants detected using a polyclonal anti-gHgL antibody (rabbit) is shown adjacent to the antibody binding data, with monoclonal anti-GAPDH blots shown as a loading control. The gel shows the expected shift in molecular weight of the gl mutants due to loss of glycan at the mutated NXS motif.
Sathiyamoorthy, K., Hu, Y. X., Möhl, B. S., Chen, J., Longnecker, R., & Jardetzky, T. S. (2016). Structural basis for Epstein–Barr virus host cell tropism mediated by gp42 and gHgL entry glycoproteins. Nature communications, 7, 13557.
Figure 2 Isolated mAb Neutralizes EBV Infection in B Cells.
Serial dilutions of the indicated antibodies were evaluated for their ability to neutralize B95.8/F EBV infection of B (Raji) cells. AntigH/gL antibodies are shown in shades of blue, anti-gB antibodies are shown in shades of red, and the anti-gp350 antibody (72A1) is shown in gray. The human or murine origins of the antibodies are indicated in the legend. Data points are mean ± SD of duplicate wells. Representative curves from 2 to 6 replicates are shown.
Snijder, J., Ortego, M. S., Weidle, C., Stuart, A. B., Gray, M. D., McElrath, M. J., ... & McGuire, A. T. (2018). An antibody targeting the fusion machinery neutralizes dual-tropic infection and defines a site of vulnerability on Epstein-Barr virus. Immunity, 48(4), 799-811.
Figure 3 Inhibition of fusion activity by E1D1 mAb and Fab.
The x-axis indicates the amount of purified E1D1 antibody expressed as a final concentration of E1D1 mAb or Fab as present in a luciferase based cell–cell fusion assay using epithelial cells. No gH and gL plasmids transfected serves as the negative control denoted as neg. ctrl.
Sathiyamoorthy, K., Hu, Y. X., Möhl, B. S., Chen, J., Longnecker, R., & Jardetzky, T. S. (2016). Structural basis for Epstein–Barr virus host cell tropism mediated by gp42 and gHgL entry glycoproteins. Nature communications, 7, 13557.
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 |
---|---|---|---|
PABC-311 | Recombinant Human Anti-EBV gH/gL Antibody (AMMO1) | ELISA, BLI, Neut | Human IgG |
PABC-419 | Recombinant Mouse Anti-EBV gH/gL Antibody (CL40) | ELISA, Inhib, FC, Neut | Mouse IgG1 |
PABC-523 | Mouse Anti-EBV gH/gL Recombinant Antibody (clone CL59) | ELISA, FC, Neut, Inhib | Mouse IgG1 |
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For Research Use Only. Not For Clinical Use.
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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