benzyl N-[(2S)-1-[[(2S)-5-(diaminomethylideneamino)-1-[(4-methyl-2-oxochromen-7-yl)amino]-1-oxopentan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]carbamate:hydrochloride

benzyl N-[(2S)-1-[[(2S)-5-(diaminomethylideneamino)-1-[(4-methyl-2-oxochromen-7-yl)amino]-1-oxopentan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]carbamate:hydrochloride Chemische Eigenschaften,Einsatz,Produktion Methoden

• Beschreibung

  Z-Phe-Arg-AMC (70382-26-2) is a fluorogenic substrate1 for the following cathepsins (kcat/Km in M-1s-1): B (105)2, C/DPP-I (104)3, F (106)4, K/O2 (105)3, L (106)3, L2/V (105)5, O6, S (104)7, X/Z (104)8. The peptide is also cleaved by plasma kallikrein and kallikrein 89, and papain (kcat/Km=105 M-1s-1).3?Excitation: 365nm, Emission: 440nm.5

• Verwenden

  Z-Phe-Arg 7-amido-4-methylcoumarin hydrochloride has been used:
  
  • as a fluorogenic substrate in actinidin inhibition assay
  • as a kallikrein substrate
  • as a trypsin substrate for fluorometric assay
  • as a cathepsin-L substrate
  
  

• Allgemeine Beschreibung

  Substrate for fluorogenic assay of plasma and glandular kallikreins. Also serves as a substrate for cathepsin B, cathepsin L, and papain.

• Biochem/physiol Actions

  Z-Phe-Arg 7-amido-4-methylcoumarin (Z-FR-AMC) proteolytic lysis by proteases leads to the liberation of AMC resulting in increased fluorescence in the enzymatic reaction.

• Einzelnachweise

  Tavares et al. (2004), Design of potent, selective, and orally bioavailable inhibitors of cysteine protease cathepsin k; J. Med. Chem., 47 588 Therrien et al. (2001), Cathepsins X and B can be differentiated through their respective mono- and dipeptidyl carboxypeptidase activities; Biochemistry, 40 2702 N?gler et al. (1999), Interdependency of sequence and positional specificities for cysteine proteases of the papain family; Biochemistry, 38 4868 Wang et al. (1998), Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization; J. Biol. Chem., 273 32000 Br?mme et al. (1999), Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization and chromosomal localization; Biochemistry, 38 2377 Velasco et al. (1994), Human cathepsin O. Molecular cloning from a breast carcinoma, production of the active enzyme in Escherichia coli, and expression analysis in in human tissues; J. Biol. Chem., 269 27136 Kopitar et al. (1996), Folding and activation of human procathepsin S from inclusion bodies produced in Escherichia coli; Eur. J. Biochem., 236 558 Klemen?i? et al. (2000), Biochemical characterization of human cathepsin X revealed that the enzyme is an exopeptidase, acting as carboxymonopeptidase or carboxydipeptidase; Eur. J. Biochem., 267 5404 Kishi et al. (2006), Activation and enzymatic characterization of recombinant human kallikrein 8; Biol. Chem., 387 723

benzyl N-[(2S)-1-[[(2S)-5-(diaminomethylideneamino)-1-[(4-methyl-2-oxochromen-7-yl)amino]-1-oxopentan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]carbamate:hydrochloride Anbieter Lieferant Produzent Hersteller Vertrieb Händler.

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70382-26-2, benzyl N-[(2S)-1-[[(2S)-5-(diaminomethylideneamino)-1-[(4-methyl-2-oxochromen-7-yl)amino]-1-oxopentan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]carbamate:hydrochloride Verwandte Suche: