HCV Proteases - Wild-Type & Mutated


HCV Proteases - Wild-Type & Mutated

The Hepatitis C Virus (HCV) NS3/4A serine protease, essential for HCV replication and the formation of infectious viral particles, is considered one of the most attractive targets for anti-HCV therapy. Effective HCV protease inhibitors (PIs) such as VX-951 and BILN 20612,3 have been found to reduce viral load; however, due to poor fidelity of the viral reverse transcriptase and RNA-dependent RNA polymerase, drug resistant mutations, consisting of single or multiple amino acid substitutions, have been identified in several labs and found to confer resistance to PIs. AnaSpec is pleased to present an important new addition to the arena of HCV research – our latest line of mutated HCV proteases.

The producer of the world’s most sensitive HCV NS3/4A FRET substrate, AnaSpec introduces a new series of mutated HCV NS3 serine proteases to complement our popular wild-type protease. These mutants provide researchers with additional tools with which to assess the implications and explore a response to the emergence of PI resistant NS3 proteases.

Both wild-type and mutated proteases are recombinant fusion proteins with an NS3 protease domain and a fragment of the NS4A protein fused to its N-terminus. As a result of this fusion, these proteins are already in the active form, which makes pre-activation by pep4A or pep4AK unnecessary. Only a minimal amount of protease is needed (50-100 ng) to perform AnaSpec’s FRET-based activity assays - EnzoLyte™ HCV Protease Assay Kits.

On-line listings of recombinant NS3/4A proteases:
  • Wild-type
  • Mutated
  • NS3 Protease Inhibitors

  • To request AnaSpec’s newest 2006-2008 Peptides catalog, click here.

    References:
    1. Lin, K. et al., Antimicrob. Agents Chemother. 50, 1813-1822 (2006).
    2. Faucher, A.M. et al., Org.Lett. 6, 2901-2904 (2004).
    3. Hinrichsen, H. et al., Gastroenterology 127, 1347-1355 (2004).