Hepatitis C Virus NS3, c33c, aa1359-1456, Genotype 5, 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 aa 1250/ 1251), A (within aa 1250-1334), A/B (around aa 1323 and 1334), and B/C (around aa 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.\n\nRecombinant, from HCV subtype 5. The protein contains the HCV NS3 (c33c) immunodominant regions, amino acids 1359-1459.\n\nSpecificity:\nImmunoreactive with sera of HCV-infected individuals\n\nApplications:\nRecombinant HCV NS3 Antigen may be used in ELISA and Western Blot, excellent for detection of HCV with minimal specificity problems.\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

H1920-23L1

Size

100ug

Form

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

Purity

(same/more than) 95% by RP-HPLC, FPLC, or reducing/non-reducing SDS-PAGE Silver Stain. Chromatographically purified.

References

1. Capped dipeptide phenethylamide inhibitors of the HCV NS3 protease. Nizi E, Koch U, Marchetti A, Gardelli C, Bioorg Med Chem Lett 2004 May 3;14(9):2151-4 2. Double-stranded DNA-induced localized unfolding of HCV NS3 helicase subdomain 2. Liu D, Windsor WT, Protein Sci 2003 Dec;12(12):2757-67 3. Two antiviral compounds from the plant Stylogne cauliflora as inhibitors of HCV NS3 protease. Hegde VR, Pu H, Das PR, Chan TM, Bioorg Med Chem Lett 2003 Sep 1;13(17):2925-8 4. In vitro selection of RNA aptamers against HCV-NS3 helicase and their structural similarity with 3'(+)UTR of HCV. Nishikawa S, Nishikawa F, Nucleic Acids Res Suppl 2003;(3):241-2 5. Analysis of aptamer binding site for HCV-NS3 protease by alanine scanning mutagenesis. Hwang J, Fauzi H, Sekiya S, Nishikawa S, Nucleic Acids Symp S er 2000;(44):253-4 6. Novel, potent phenethylamide inhibitors of the hepatitis C virus (HCV) NS3 protease: probing the role of P2 aryloxyprolines with hybrid structures. Orvieto F, Koch U, Muraglia E, Bioorg Med Chem Lett 2003 Aug 18;13(16):2745-8.