Human Anti-HCV E2 Recombinant Antibody (clone L1) (CAT#: FAMAB-0198JF)

Figure 1 Indirect immunofluorescence analysis.

Staining was performed using goat-anti human IgG immune serum coupled with fluoresceine.

Habersetzer, F., Fournillier, A., Dubuisson, J., Rosa, D., Abrignani, S., Wychowski, C., ... & Inchauspé, G. (1998). Characterization of Human Monoclonal Antibodies Specific to the Hepatitis C Virus Glycoprotein E2 within VitroBinding Neutralization Properties. Virology, 249(1), 32-41.

Figure 2 Immunoprecipitation of E2 and coprecipitation of E1 and analysis of epitope formation under under reducing and nonreducing conditions.

Expected position of HCV-specific proteins are indicated at the left of the figures.

Habersetzer, F., Fournillier, A., Dubuisson, J., Rosa, D., Abrignani, S., Wychowski, C., ... & Inchauspé, G. (1998). Characterization of Human Monoclonal Antibodies Specific to the Hepatitis C Virus Glycoprotein E2 within VitroBinding Neutralization Properties. Virology, 249(1), 32-41.

Figure 3 Percent neutralization of E2 binding by HCV-E2 HMAbs.

Various concentrations of anti-E2 HMAbs were tested for their ability to neutralize binding of purified CHO-expressed E2 protein onto MOLT-4 cells.

Habersetzer, F., Fournillier, A., Dubuisson, J., Rosa, D., Abrignani, S., Wychowski, C., ... & Inchauspé, G. (1998). Characterization of Human Monoclonal Antibodies Specific to the Hepatitis C Virus Glycoprotein E2 within VitroBinding Neutralization Properties. Virology, 249(1), 32-41.

Figure 4 Antibody response to E1, E2, and the E2 HVR-1.

Serial bleeds obtained up to 9 years postinoculation with HCV from chimpanzee x174 were examined by ELISA for reactivity to native, purified E1 and E2, and a synthetic peptide to the HVR-1.

Aytug, S., Reich, D., Sapiro, L. E., Bernstein, D., & Begum, N. (2003). Impaired IRS-1/PI3-kinase signaling in patients with HCV: a mechanism for increased prevalence of type 2 diabetes. Hepatology, 38(6), 1384-1392.