HCV Protease FRET Substrate

<strong>HCV Protease FRET Substrate</strong>_x000D_ <strong>Catalog number:</strong> B2011439_x000D_ <strong>Lot number:</strong> Batch Dependent_x000D_ <strong>Expiration Date:</strong> Batch dependent_x000D_ <strong>Amount:</strong> 1 mg_x000D_ <strong>Molecular Weight or Concentration:</strong> 1548.6 g/mol_x000D_ <strong>Supplied as:</strong> Lyophilized_x000D_ <strong>Applications:</strong> molecular tool for various biochemical applications_x000D_ <strong>Storage:</strong> -20 °C_x000D_ <strong>Keywords:</strong> FRET S1_x000D_ <strong>Grade:</strong> Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity &gt;18 MΩ-cm) and are filtered through 0.22 um._x000D_ _x000D_ <strong>References:</strong>_x000D_ 1: Matthew AN, Zephyr J, Nageswara Rao D, Henes M, Kamran W, Kosovrasti K, Hedger AK, Lockbaum GJ, Timm J, Ali A, Kurt Yilmaz N, Schiffer CA. Avoiding Drug Resistance by Substrate Envelope-Guided Design: Toward Potent and Robust HCV NS3/4A Protease Inhibitors mBio. 2020 Mar 31;11(2):e00172-20._x000D_ 2: Lin C. HCV NS3-4A Serine Protease In: Tan SL, editor. Hepatitis C Viruses: Genomes and Molecular Biology. Norfolk (UK): Horizon Bioscience; 2006. Chapter 6._x000D_ 3: Zhu H, Briggs JM. Mechanistic role of NS4A and substrate in the activation of HCV NS3 protease Proteins. 2011 Aug;79(8):2428-43._x000D_ 4: Özen A, Prachanronarong K, Matthew AN, Soumana DI, Schiffer CA. Resistance outside the substrate envelope: hepatitis C NS3/4A protease inhibitors Crit Rev Biochem Mol Biol. 2019 Feb;54(1):11-26._x000D_ 5: Dultz G, Shimakami T, Schneider M, Murai K, Yamane D, Marion A, Zeitler TM, Stross C, Grimm C, Richter RM, Bäumer K, Yi M, Biondi RM, Zeuzem S, Tampé R, Antes I, Lange CM, Welsch C. Extended interaction networks with HCV protease NS3-4A substrates explain the lack of adaptive capability against protease inhibitors J Biol Chem. 2020 Oct 2;295(40):13862-13874._x000D_ 6: Ozdemir Isik G, Ozer AN. Prediction of substrate specificity in NS3/4A serine protease by biased sequence search threading J Biomol Struct Dyn. 2017 Apr;35(5):1102-1114._x000D_ 7: Tran HTL, Morikawa K, Anggakusuma, Zibi R, Thi VLD, Penin F, Heim MH, Quadroni M, Pietschmann T, Gouttenoire J, Moradpour D. OCIAD1 is a host mitochondrial substrate of the hepatitis C virus NS3-4A protease PLoS One. 2020 Jul 22;15(7):e0236447._x000D_ 8: Jindal G, Mondal D, Warshel A. Exploring the Drug Resistance of HCV Protease J Phys Chem B. 2017 Jul 20;121(28):6831-6840._x000D_ 9: Zephyr J, Kurt Yilmaz N, Schiffer CA. Viral proteases: Structure, mechanism and inhibition Enzymes. 2021;50:301-333._x000D_ <a href="https://pubmed.ncbi.nlm.nih.gov/23137809">10: Kang X, Chen X, He Y, Guo D, Guo L, Zhong J, Shu HB. DDB1 is a cellular substrate of NS3/4A protease and required for hepatitis C virus replication Virology. 2013 Jan 20;435(2):385-94. </a>_x000D_ _x000D_ <strong>Products Related to HCV Protease FRET Substrate can be found at</strong> <a href="https://moleculardepot.com/product-category/Substrates/"> Substrates</a>