(Hepatitis C Virus Non-Structural protein, Subtype 1a)
recombinant, E. coli
For in vitro use only!
Shipping: shipped on blue ice
Storage Conditions: store at -20 °C
avoid freeze/thaw cycles
Shelf Life: 12 months
Purity: > 95 % (SDS-PAGE)
Form: liquid (Supplied in 25 mM Tris-HCl pH 8.0, 0.2% Triton-X 100, 1.5 M urea and 50% glycerol)
Antigen in ELISA and Western blots, excellent antigen for detection of HCV with minimal specificity problems.
The protein contains the HCV NS3 (c33c) immunodominant region, amino acids 1359-1456. Hepatitis C NS3 protein is purified by proprietary chromatographic techniques.
Background: 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. Immunoblot analysis on serum samples from 90 patients with chronic hepatitis C virus infection revealed four putative immunogenic regions within the NS3 protein of the virus: E (around amino acids 1250/1251), A (within amino acids 1250-1334), A/B (around amino acids 1323 and 1334), and B/C (around amino acids 1407 and 1412). Among them, region E was most immunodominant, and region A was recognized much less frequently by patients with cirrhosis than by those with chronic hepatitis.
Specificity: Immunoreactive with sera of HCV-infected individuals.
Gal-Tanamy et al. (2005) HCV NS3 serine protease-neutralizing single-chain antibodies isolated by a novel genetic screen. J. Mol. Biol. 347:991.
Duan et al. (2004) Antiviral compounds from traditional Chinese medicines Galla Chinese as inhibitors of HCV NS3 protease. Bioorg. Med. Chem. Lett. 14:6041.
Sun et al. (2004) P4 cap modified tetrapeptidyl alpha-ketoamides as potent HCV NS3 protease inhibitors. Bioorg. Med. Chem. Lett. 14:4333.
Nizi et al. (2004) Capped dipeptide phenethylamide inhibitors of the HCV NS3 protease. Bioorg. Med. Chem. Lett. 14:2151.
Liu et al. (2003) Double-stranded DNA-induced localized unfolding of HCV NS3 helicase subdomain 2. Protein Sci. 12:2757.
Hedge et al. (2003) Two antiviral compounds from the plant Stylogne cauliflora as inhibitors of HCV NS3 protease. Bioorg. Med. Chem. Lett. 13:2925.