Boc-Val-Pro-Arg-AMC . HCl

Boc-Val-Pro-Arg-7-amido-4-methylcoumarin CAS: 70375-24-5 , 65147-04-8 (free base) Appearance: Solid lyophilized powder. Solubility: Soluble in water (10mg/ml). Soluble in 5% acetic acid. InChi Key: ROQGJTZGLVLVIN-UHFFFAOYSA-N Smiles: O=C1C=C(C)C2=CC=C(NC(C(CCCNC(N)=N)NC(C3N(C(C(NC(OC(C)(C)C)=O)C(C)C)=O)CCC3)=O)=O)C=C2O1.Cl Boc-Val-Pro-Arg-AMC is a sensitive fluorogenic peptide substrate for alpha-thrombin (Km = 21 µM, kcat = 109 s-1) and the alpha-thrombin-staphylocoagulase complex (Km = 25 µM, kcat = 89 s-1). It also serves as a substrate vor Kallikrein 5 and 8. Activity is quantified by the release of free fluorescent 7-amino-4-methylcoumarin (AMC) which excites at 360-380nm and emits at 440-460nm when interacting with a target enzyme. This substrate has also been used for the rapid detection of MRSA (methicillin-resistant Staphylococcus aureus). Product References New fluorogenic substrates for alpha-thrombin, factor Xa, kallikreins, and urokinase: T. Morita, et al., J. Biochem. 82, 1495 (1977) Difference in enzymatic properties between alpha-thrombin-staphylocoagulase complex and free alpha-thrombin: S. Kawabata, et al., J. Biochem. 97, 1073 (1985) Evaluation of tube coagulase and a fluorogenic substrate for rapid detection of methicillin-resistant Staphylococcus aureus from selective enrichment broth in an outbreak of EMRSA 15: M. Ford, et al., J. Hosp. Infect. 41, 133 (1999) Biochemical and Enzymatic Characterization of Human Kallikrein 5 (hK5), a Novel Serine Protease Potentially Involved in Cancer Progression: I.P. Michael, et al., J. Biol. Chem. 280, 14628 (2005) Activation and enzymatic characterization of recombinant human kallikrein 8: T. Kishi, et al., Biol. Chem. 387, 723 (2006)