After signing up, you'll start to receive regular news updates from us.
AnaSpec Unveils HCV Proteases
Complete the form below to unlock access to ALL audio articles.
AnaSpec has added a line of mutated HCV proteases to its protease collection, continuing to support advances in HCV research.
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 and BILN 2061 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 offers a series of mutated HCV NS3 serine proteases to complement its wild-type proteases.
These mutants are designed to 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.
A minimal amount of protease is needed (50-100 ng) to perform AnaSpec’s FRET-based activity assays.
