Image of a kit SensoLyte 490 HCV Protease Assay Kit Fluorimetric 200 assays
Assay-kits

SensoLyte® 490 HCV Protease Assay Kit Fluorimetric 200 assays - 1 kit

€582.00
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  • Cat.Number : AS-72087
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HCV protease is identified as an important drug-screening target. The SensoLyte® 490 HCV Protease Assay Kit uses an optimized FRET peptide substrate for the continuous measurement of HCV NS3/4a activity. This FRET substrate is cleaved specifically by HCV NS3/4a protease thereby liberating the C-terminal peptide-fluorophore fragment from the proximity quenching effect of the dark quencher, resulting in a more than 10-fold increase in fluorescence. This assay can detect HCV NS3/4a protease activity at 1 pmole.

Specifications

Packaging
Kits components
  • Component A: HCV NS3/4A protease substrate EDANS/DABCYL FRET peptide, Ex/Em=340 nm/490 nm upon cleavage: 250 µL Component B: EDANS, fluorescence reference standard Ex/Em=340 nm/490 nm: 100 µM DMSO solution, 10 µL Component C: 2X Assay buffer: 25 mL Component D: Stop solution: 15 mL Component E: DTT: 1 M, 1 mL component F: Pep4AK HCV NS3 protease cofactor: 150 µL, 600 µM
Properties
Absorbance (nm)
  • 340
Emission (nm)
  • 490
Storage & stability
Storage Conditions
  • Store all components at -20°C. Components C and D can be stored at room temperature for convenience. Protect Components A and B from light.
Activity
Application
Biomarker Target
Detection Method
Detection Limit
  • 1 pmole
Research Area
Sub-category Research Area
Usage
  • Research use
Codes
Code Nacres
  • NA.32

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Citations

2-Arylmethylaminomethyl-5,6-dihydroxychromone derivatives with selective anti-HCV activity.

Bioorg Med Chem Lett. . 2011 Apr 20 ; 21(11) 3202 | DOI : 10.1016/j.bmcl.2011.04.055

  • H.R. Park
  • et al

Ceestatin, a novel small molecule inhibitor of hepatitis C virus replication, inhibits 3-hydroxy-3-methylglutaryl-coenzyme A synthase

J Infect Dis . 2011 Aug 15 ; 204(4) 609 | DOI : 10.1093/infdis/jir303

  • L.F. Peng
  • et al

A method to simultaneously monitor hepatitis C virus NS3 helicase and protease activities

Methods Mol Biol. . 2010 Jan 01 ; 587 223 | DOI : 10.1007/978-1-60327-355-8_16

  • D.N. Frick
  • et al