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Anti-HCV E1E2, clone AR5A, Cat. No. MABF2334, is a human recombinant monoclonal antibody that detects Hepatitis C virus E1E2 glycoprotein and is tested for use in ELISA, Immunoprecipitation, and Neutralizing Activity.
More>>Anti-HCV E1E2, clone AR5A, Cat. No. MABF2334, is a human recombinant monoclonal antibody that detects Hepatitis C virus E1E2 glycoprotein and is tested for use in ELISA, Immunoprecipitation, and Neutralizing Activity. Less<<
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Übersicht
Replacement Information
Description
Catalogue Number
MABF2334-25UL
Description
Anti-HCV E1E2 Antibody, clone AR5A
Alternate Names
Hepatitis C virus envelope protein
gp35/gp70
gp32/gp68
Background Information
Hepatitis C virus (HCV) is a small (~55-65 nm), enveloped, positive-sense single-stranded RNA virus that is a causative factor for hepatitis C and hepatocellular carcinoma. HCV expresses several proteins that promote viral replication. Genome polyprotein of HCV is a core protein that packages viral RNA to form a viral nucleocapsid, and promotes virion budding. It also modulates viral translation initiation by interacting with HCV IRES and 40S ribosomal subunit. It prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways and by inducing human STAT1 degradation. Envelope glycoproteins E1 (aa 192-383) and E2 (aa 384-746) of HCV are single-pass type I membrane proteins that form a heterodimer by non-covalent interaction of their transmembrane domains, which is involved in virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane. The C-terminal transmembrane domain of E1 and E2 acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase. After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor. A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain. The E2 antigenic site localized to amino acids 412-423 is reported to be highly conserved and is considered as an ideal target for cross neutralization of HCV genotypes. Clone AR5A is derived from Fab clone V1 and is shown to bind only to the folded E1E2 complex with high affinity (0.1 nM) and arginine 639 is critical for its binding. It can neutralize HCV isolates from multiple genotypes in both HCVpp and HCVcc systems by blocking virus attachment and entry into cells. However, it does not block E1E2 binding to CD81. (Ref.: Giang, E., et al. (2012). Proc. Natl. Acad. Sci. USA. 109(16); 6205-6210).
References
Product Information
Format
Purified
Presentation
Purified human recombinant monoclonal antibody in PBS without preservatives.
Anti-HCV E1E2, clone AR5A, Cat. No. MABF2334, is a human recombinant monoclonal antibody that detects Hepatitis C virus E1E2 glycoprotein and is tested for use in ELISA, Immunoprecipitation, and Neutralizing Activity.
Key Applications
ELISA
Immunoprecipitation
Neutralizing
Application Notes
Neutralizing: A representative lot neutralized HCV isolates from multiple genotypes in both the HCVpp and HCVcc virus systems. (Giang, E., et. al. (2012). Proc Natl Acad Sci USA 109(16):6205-10).
ELISA Analysis: A representative lot detected HCV E1E2 in ELISA applications (Giang, E., et. al. (2012). Proc Natl Acad Sci USA 109(16):6205-10).
Immunoprecipitation Analysis: A representative lot immunoprecipitated HCV E1E2 in Immunoprecipitation applications (Giang, E., et. al. (2012). Proc Natl Acad Sci USA 109(16):6205-10).
Note: Actual optimal working dilutions must be determined by end user as specimens, and experimental conditions may vary with the end user
Biological Information
Immunogen
Antibody Fab fragment V1 expressed in E. coli, purified, and converted into full-length IgG1 molecules in CHO-K1 cells.
Epitope
Discontinuous; E1E2 complex
Clone
AR5A
Concentration
0.5 mg/mL. Please refer to guidance on suggested starting dilutions and/or titers per application and sample type.
Host
Human Recombinant
Specificity
Clone AR5A is a recombinant antibody produced from Fab fragment V1, expressed in E.coli and converted into full-length IgG1 in CHO-K1 cells. It detects Hepatitis C virus envelope protein E1E2 complex.
Evaluated by ELISA in lysate from 293T cells transfected with H77E1E2.
ELISA Analysis: A x/2 of this antibody detected Hepatitis C virus E1E2 glycoprotein in lysate from HEK293 cells transfected with H77E1E2, but not in control cell lysate..
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage and Shipping Information
Storage Conditions
Stable for 1 year at -10°C to -25°C from date of receipt. Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.
Human broadly neutralizing antibodies to the envelope glycoprotein complex of hepatitis C virus Erick Giang 1 , Marcus Dorner, Jannick C Prentoe, Marlène Dreux, Matthew J Evans, Jens Bukh, Charles M Rice, Alexander Ploss, Dennis R Burton, Mansun Law Proc Natl Acad Sci U S A
109(16)
6205-10
2011
Hepatitis C virus (HCV) infects ∼2% of the world's population. It is estimated that there are more than 500,000 new infections annually in Egypt, the country with the highest HCV prevalence. An effective vaccine would help control this expanding global health burden. HCV is highly variable, and an effective vaccine should target conserved T- and B-cell epitopes of the virus. Conserved B-cell epitopes overlapping the CD81 receptor-binding site (CD81bs) on the E2 viral envelope glycoprotein have been reported previously and provide promising vaccine targets. In this study, we isolated 73 human mAbs recognizing five distinct antigenic regions on the virus envelope glycoprotein complex E1E2 from an HCV-immune phage-display antibody library by using an exhaustive-panning strategy. Many of these mAbs were broadly neutralizing. In particular, the mAb AR4A, recognizing a discontinuous epitope outside the CD81bs on the E1E2 complex, has an exceptionally broad neutralizing activity toward diverse HCV genotypes and protects against heterologous HCV challenge in a small animal model. The mAb panel will be useful for the design and development of vaccine candidates to elicit broadly neutralizing antibodies to HCV.
