Hepatitis C Virus NS3, Subtype 1b, aa1359-1459, Recombinant (HCV)

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 aa1250/ 1251), A (within aa1250-1334), A/B (around aa1323 and 1334), and B/C (around aa1407 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\n\nE. coli derived recombinant from HCV subtype 1b. The protein contains the full-length HCV NS3 (c33c) immunodominant region, aa1359-1459.\n\nApplications: \nRecombinant HCV NS3 Antigen may be used in ELISA and Western Blots, excellent for detection of HCV with minimal specificity problems. Immunoreactive with sera of HCV-infected individuals.\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. For long-term storage, store at -20 degrees C. Aliquots are stable for at least 6 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

H1920-23P

Size

100ug

Form

Supplied as a liquid in 25mM Tris-HCl, 1mM EDTA, 1.5M urea and 50% glycerol.

Purity

Purified by proprietary chromatographic techniques. (same/more than) 95% pure as determined by 10% PAGE (coomassie staining) and RP-HPLC.

References

1. Interaction between the HCV NS3 protein and the host TBK1 protein leads to inhibition of cellular antiviral responses.Hepatology 2005 May;41(5):1004-12.\n2. HCV NS3 serine protease-neutralizing single-chain antibodies isolated by a novel genetic screen. J Mol Biol 2005 Apr 15;347(5):991-1003.\n3. Antiviral compounds from traditional Chinese medicines Galla Chinese as inhibitors of HCV NS3 protease. Bioorg Med Chem Lett 2004 Dec 20;14(24):6041-4.\n4. P4 cap modified tetrapeptidyl alpha-ketoamides as potent HCV NS3 protease inhibitors. Bioorg Med Chem Lett 2004 Aug 16;14(16):4333-8.\n5. Capped dipeptide phenethylamide inhibitors of the HCV NS3 protease. Bioorg Med Chem Lett 2004 May 3;14(9):2151-4.\n6. Double-stranded DNA-induced localized unfolding of HCV NS3 helicase subdomain 2. Protein Sci 2003 Dec;12(12):2757-67.