Recombinant Human Antibody (IGH526) is capable of binding to HCV E1, expressed in HEK 293 cells. Expressed as the combination of a heavy chain (HC) containing VH from anti-HCV E1 mAb and CH1-3 region of human IgG1 and a light chain (LC) encoding VL from anti-HCV E1 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 neutralizing antibody bound to a discontinuous epitope, but with a major component corresponding to E1 residues 314–324.
Figure 2 (a) Neutralization of HCV by mAb IGH526. The mAbneutralized HCV pseudotype virus particles (HCVpp) displaying the genotype 1a E1E2, but not the control envelopeglycoprotein G from vesicular stomatitis virus (VSVpp). mAbs AR3A and AR4A are control neutralizing mAbs to E2 andE1E2 complex, respectively.
Kong, L., Kadam, R. U., Giang, E., Ruwona, T. B., Nieusma, T., Culhane, J. C.,... & Law, M. (2015). Structure of hepatitis C virus envelope glycoprotein E1 antigenic site 314–324 in complex with antibody IGH526. Journal of molecular biology,427(16), 2617-2628.
Figure 3 (b) Binding of mAb IGH526 to E1E2 in ELISA can be blocked effectively by peptide H312(HITGHRMAWDMMMNWS) or NIH 6971 (YPGHITGHRMAWDMMMNW).
Kong, L., Kadam, R. U., Giang, E., Ruwona, T. B., Nieusma, T., Culhane, J. C.,... & Law, M. (2015). Structure of hepatitis C virus envelope glycoprotein E1 antigenic site 314–324 in complex with antibody IGH526. Journal of molecular biology,427(16), 2617-2628.
Figure 4 (c) Binding of mAb IGH526 to E1E2 in ELISA.E1E2 antigens expressed in 293T cells in their native (closed symbols) or reduced (open symbols) form were capturedonto microwells by lectin. The control mAbs A4 and AR3A recognize a continuous E1 epitope and a discontinuous E2epitope, respectively.
Kong, L., Kadam, R. U., Giang, E., Ruwona, T. B., Nieusma, T., Culhane, J. C.,... & Law, M. (2015). Structure of hepatitis C virus envelope glycoprotein E1 antigenic site 314–324 in complex with antibody IGH526. Journal of molecular biology,427(16), 2617-2628.
Figure 5 (d) Pepscan analysis of mAb IGH526. The antibody only bound a specific E1 peptide in a libraryof overlapping peptides (18-mer, 11-residue overlap, 250 ng per well) spanning the viral structural proteins: Core, E1 andE2. mAb HCV1 is a control that binds the E2 412–423 region.
Kong, L., Kadam, R. U., Giang, E., Ruwona, T. B., Nieusma, T., Culhane, J. C.,... & Law, M. (2015). Structure of hepatitis C virus envelope glycoprotein E1 antigenic site 314–324 in complex with antibody IGH526. Journal of molecular biology,427(16), 2617-2628.
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
See more details about Hi-Affi™ recombinant antibody benefits.
Download resources about recombinant antibody development and antibody engineering to boost your research.
CAT | Product Name | Application | Type |
---|---|---|---|
PSBL-117 | Recombinant Human Anti-HCV E1 Antibody scFv Fragment (IGH526) | Neut, FuncS | scFv |
CAT | Product Name | Application | Type |
---|---|---|---|
PFBL-117 | Recombinant Human Anti-HCV E1 Antibody Fab Fragment (IGH526) | Neut, FuncS | Fab |
CAT | Product Name | Application | Type |
---|---|---|---|
MHC-YF397 | B*35:01/HCV E1 (CPNSSIVY) MHC Pentamer | FCM |
There are currently no Customer reviews or questions for PABL-117. Click the button above to contact us or submit your feedback about this product.
View the frequently asked questions answered by Creative Biolabs Support.
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.
This site is protected by reCAPTCHA and the Google Privacy Policy and Terms of Service apply.