Recombinant Hepatitis C virus Core antigen, contains the full-length HCV NS3 (c33c) immunodominant region (a.a. 1192-1459) and a GST fusion partner, was expressed in E. coli, and puried in vitro using conventional chromatography techniques.
> 95% pure (10% PAGE coomassie staining). GS-4B Sepharose Affinity Purification
25mM Tris-HCl, 1mM EDTA, 1.5M urea containing 50% glycerol
2-8°C short term, -20°C long term
The hepatitis C virus (HCV) core protein represents the first 191 amino acids of the viral precursor polyprotein and is cotranslationally inserted into the membrane of the endoplasmic reticulum. Hepatitis C virus (HCV) core is a viral structural protein; it also participates in some cellular processes, including transcriptional regulation. However the mechanisms of core-mediated transcriptional regulation remain poorly understood. Hepatitis C virus (HCV) core protein is thought to contribute to HCV pathogenesis through its interaction with various signal transduction pathways. In addition, HCV core antigen is a recently developed marker of hepatitis C infection. The HCV core protein has been previously shown to circulate in the bloodstream of HCV-infected patients and inhibit host immunity through an interaction with gC1qR.
The nonstructural protein NS3 of the hepatitis C virus (HCV) is indispensable for virus replication and a multifunctional enzyme that contains three catalytic activities such as serine protease, helicase, and NTPase. The N-terminal domain of the protein contains protease activity and the C-terminal domain contains nucleotide triphosphatase and RNA helicase activity. It has been shown that NS2/3 cleavage is mediated by NS2-3 protease, whereas NS3 serine protease is responsible for the other four cleavage sites of the nonstructural (NS) region.
HCV NS3 transactivated protein; NS 3; NS3; NS3P; p70; Serine protease/NTPase/helicase; Hepatitis C Virus NS3; Flaviviridae; Hepacivirus; Hepatitis C virus; HCV NS-3