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AnaSpec's 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.
AnaSpec's HCV Proteases - Wild-Type & Mutated

 

NewswireToday - /newswire/ - San Jose, CA, United States, 2006/07/17 - 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..

   
 
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AnaSpec, Inc. is a leading provider of integrated proteomics solutions for worldwide life science research. With a vision for innovation through synergy, AnaSpec offers expertise in three primary technologies: peptides, detection reagents, and combinatorial chemistry. AnaSpec carries a broad product line of biochemicals and reagents for basic research, high-throughput screening and drug discovery. In conjunction, AnaSpec provides premier custom services including peptide synthesis, antibody production, and assay development. AnaSpec holds a California Drug Manufacturing License (License #41747) and a FDA Registration for GMP Drug Manufacturing (Registration #2951078).

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.

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 (50-100 ng) to perform AnaSpec’s FRET-based activity assays.

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).

 
 
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Written by / Agency / Source: AnaSpec, Inc.

 
 

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AnaSpec's HCV Proteases - Wild-Type & Mutated

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Publisher Contact: Debra Thai 
408-452-5055 info[.]anaspec.com
 
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IMPORTANT INFORMATION: Issuance, publication or distribution of this press release in certain jurisdictions could be subject to restrictions. The recipient of this press release is responsible for using this press release and the information herein in accordance with the applicable rules and regulations in the particular jurisdiction. This press release does not constitute an offer or an offering to acquire or subscribe for any AnaSpec, Inc. securities in any jurisdiction including any other companies listed or named in this release.

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