Product category:
Proteomics
News Release from: AnaSpec | Subject: Mutated HCV proteases
Edited by the Laboratorytalk Editorial
Team on 19 July 2006
HCV proteases - wild-type and 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-95(1) and BILN 2061(2,3) 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 Continuing to support advances in HCV research, AnaSpec has added a new line of mutated HCV proteases to its protease collection
This article was originally published on Laboratorytalk on 7 Jun 2006 at 8.00am (UK)
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Reagents kits for study of protein phosphorylation
Cellular phosphorylation is a reversible covalent modification of a protein or lipid that modifies the activity of the phosphorylated molecule by inducing conformational changes within the molecule
The producer of the world's most sensitive HCV NS3/4A FRET substrate, AnaSpec offers a series of mutated HCV NS3 serine proteases to complement its popular wild-type proteases.
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 (50-100ng) to perform AnaSpec's Fret-based activity assays.
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