| Identification | Back Directory | [Name]
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 | [CAS]
70382-26-2 | [Synonyms]
Z-Phe-Arg-7-amido-4-methylcoumarin, Hydrochloride - CAS 70382-26-2 - Calbiochem
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 | [Molecular Formula]
C33H37ClN6O6 | [MOL File]
70382-26-2.mol | [Molecular Weight]
649.15 |
| Chemical Properties | Back Directory | [storage temp. ]
-20°C | [solubility ]
Soluble in DMSO (50 mg/ml) | [form ]
White to off-white solid | [color ]
White | [Water Solubility ]
5% acetic acid: 1mg/mL
DMSO: 1mg/mL
water: 1mg/mL | [Stability:]
Stable for 2 years from date of purchase as supplied. Solutions in DMSO may be stored at -20°C for up to 3 months. Protect from light! |
| Hazard Information | Back Directory | [Description]
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 | [Uses]
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
| [General Description]
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. | [References]
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 |
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