Protein

HCV NS3/4A protease genotype 1b, recombinant

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  • Cat.Number : AS-61017-5
  • Availability :
    In stock
  • Shipping conditions : Ice delivery fees must be applied

Size

Quantity

NS3 protease of hepatitis C virus (HCV), located on the N-terminal domain of HCV NS3, is responsible for the cleavage at the NS3/NS4A, NS4A/NS4B, NS4B/NS5A, and NS5A/NS5B sites of the nonstructural protein. The HCV NS3 is a chymotrypsin-like serine protease. It requires a cofactor, a 54 amino acid NS4 protein, to reach its optimal activity. The X-ray crystal structure studies show that NS3 forms a tight non-covalent complex with NS4. The NS3/4A protease is essential for viral replication and the formation of infectious viral particles, and thus has been considered as one of the most attractive targets for anti-HCV therapy.

The recombinant HCV NS3/4A protease (genotype 1b, strain: HC-J4; NCBI Accession: AF054247) was expressed in E. Coli. HCV NS3/4A protease is a 217 amino acid fusion protein (22.7 kDa) with NS4A co-factor fused to the N-terminus of NS3 protease domain. Therefore, HCV NS3/4A protease is in active form and the pre-activation by pep4A or pep4AK is not necessary. 5-20 ng of HCV NS3/4A protease is sufficient for FRET-based activity assays (SensoLyte® HCV protease assay).

Specifications

Chemistry
Molecular Mass/ Weight
  • 22.7 kDa
Modification
Conjugation
  • Unconjugated
Quantity & Purity
Concentration
  • lot dependent
Storage & stability
Form
  • In solution
Storage Buffer
  • 20 mM Tris-HCl, pH 8.0, 20% Glycerol, 100 mM KCl, 1 mM DTT and 0.2 mM EDTA.
Storage Conditions
  • Store at -80 ºC. Avoid repeated freeze-thaw cycles.
Activity
Application
Biomarker Target
Unit definition
  • One unit of protease hydrolyzes 1 picomole of 5-FAM/QXL™ FRET substrate per minute at pH 7.5 at 25°C.
Specificity
  • recombinant HCV NS3/4A protease (genotype 1b, strain: HC-J4; NCBI Accession: AF054247)
Research Area
Sub-category Research Area
Usage
  • Research use
Source
Host
Source / Species
  • Hepatitis C Virus

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Citations

HCV Protease Inhibitory, Cytotoxic and Apoptosis-Inducing Effects of Oleanolic Acid Derivatives

J Pharm Pharm Sci. . 2009 Jan 01 ; 12(3) 243 | DOI : 10.18433/j3dw2d

  • C. Ma
  • et al

Inhibitory effects of antrodins A-E from Antrodia cinnamomea and their metabolites on hepatitis C virus protease

Phytother Res. . 2009 Apr 01 ; 23(4) 582 | DOI : 10.1002/ptr.2657

  • D.T. Phuong
  • et al

Development of a cell-based hepatitis C virus infection fluorescent resonance energy transfer assay for high-throughput antiviral compound screening.

Antimicrob Agents Chemother. . 2009 Jul 20 ; 53(10) 4311 | DOI : 10.1128/AAC.00495-09

  • X. Yu
  • et al

Triterpenes from Cynomorium songaricium--analysis of HCV protease inhibitory activity, quantification, and content change under the influence of heating.

J Nat Med . 2008 Jul 04 ; 63(1) 9 | DOI : 10.1007/s11418-008-0267-7

  • C. Ma
  • et al

Hepatitis C Virus NS2 Protein Contributes to Virus Particle Assembly via Opposing Epistatic Interactions with the E1-E2 Glycoprotein and NS3-NS4A Enzyme Complexes

J Virol. . 2009 Jun 10 ; 83(17) 8379 | DOI : 10.1128/JVI.00891-09

  • T. Phan
  • et al