Certificate of Analysis and Data Sheet

Source:
E.Coli

Catalog No.
HCV-254

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 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

Description :

E.coli derived recombinant from HCV subtype 3. The protein contains the HCV NS3 (c33c) immunodominant region, amino acids 1359-1456. Hepatitis C Virus NS3 proteins are purified by proprietary chromatographic techniques.

Purification method:

Purified by proprietary chromatographic technique.

Purity:

Recombinant HCV NS3 is >95% pure as determined by 10% PAGE (coomassie staining) and RP-HPLC.

Formulation:

1mg/ml in 25mM Tris-HCl, 1mM EDTA, 1,5M urea and 50% glycerol.

Storage:

Recombinant HCV NS3 is shipped at ambient temperature. Upon arrival, Store at -20C.

Stability:

Recombinant HCV NS3 is stable 5 years frozen, One month in solution at room temperature.

Specificity:

Immunoreactive with sera of HCV-infected individuals

Application:

Recombinant HCV NS3 Antigen may be used in ELISA and Western blots, excellent for detection of HCV with minimal specificity problems.

Usage:

This material is offered by ProSpec-TechnoGene for research, laboratory or further evaluation purposes.

Latest Publications:

1. RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP.
Nature 2006 Jan 5;43 9(7072):105-8
2. Discovery of small-molecule inhibitors of HCV NS3-4A protease as potential therapeutic agents against HCV infection.
Curr Med Chem 2005;12(20):2317-42
3. Synthesis and biological activity of macrocyclic inhibitors of hepatitis C virus (HCV) NS3 protease.
Bioorg Med Chem Lett 2005 Oct 15;15(20):4475-8
4. Investigation of glycine alpha-ketoamide HCV NS3 protease inhibitors: effect of carboxylic acid isosteres.
Bioorg Med Chem Lett 2005 Aug 1;15(15):3487-90
5. In teraction between the HCV NS3 protein and the host TBK1 protein leads to inhibition of cellular antiviral responses.
Hepatology 2005 May;41(5):1004-12
6. Rational design of dual-functional aptamers that inhibit the protease and helicase activities of HCV NS3.
J Biochem (Tokyo) 2005 Mar;137(3):339-47