| Identification | Back Directory | [Name]
Z-LEU-ARG-7-AMINO-4-METHYLCOUMARIN | [CAS]
156192-32-4 | [Synonyms]
Z-LEU-ARG-AMC
Z-LEU-ARG-AMC HYDROCHLORIDE
Z-LEU-ARG-7-AMINO-4-METHYLCOUMARIN
CBZ-Leu-Arg-AMC hydrochloride salt
Benzyloxycarbonyl-L-leucyl-L-arginine 4-methylcoumaryl-7-amide
L-Argininamide, N-[(phenylmethoxy)carbonyl]-L-leucyl-N-(4-methyl-2-oxo-2H-1-benzopyran-7-yl)- | [Molecular Formula]
C30H38N6O6 | [MDL Number]
MFCD07780911 | [MOL File]
156192-32-4.mol | [Molecular Weight]
578.66 |
| Chemical Properties | Back Directory | [storage temp. ]
Store at 0-5°C | [solubility ]
Soluble in DMSO | [form ]
solid | [color ]
White | [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-Leu-Arg-AMC (156192-32-4) is a sensitive Cathepsin K fluorogenic substrate (Km=8μM, kcat/Km=4 x 105 M-1s-1)1-3. It is cleaved more slowly by the following cathepsins (kcat/Km: B (105)4, F (106)4, L (106)4,5, L2/V (104)5, S (105)2,4,5. Also cleaved by malaria parasite proteases berghepain6, vivapain-2 and -37, and falcipain-1, -2, and -36,8,9. Excitation: 365nm, Emission: 440nm. | [Uses]
A sensitive fluorogenic substrate for cathepsin K | [References]
Bossard et al. (1996), Proteolytic activity of human osteoclast cathepsin K. Expression, purification, activation, and substrate identification; J. Biol. Chem. 271 12517
Br?mme et al. (1996), Human cathepsin O2, a matrix protein-degrading cysteine protease expressed in osteoclasts. Functional expression of human cathepsin O2 in Spodoptera frugiperda and characterization of the enzyme; J. Biol. Chem. 271 2126
Linnevers et al. (1997), Expression of human cathepsin K in Pichia pastoris and preliminary crystallographic studies of an inhibitor complex; Protein Sci. 6 919
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
Singh et al. (2007), A chimeric cysteine protease of Plasmodium berghei engineered to resemble the Plasmodium falciparum protease falcipain-2; Protein Eng. Des. Sel. 20 171
Na et al. (2004), Identification and biochemical characterization of vivapains, cysteine proteases of the malaria parasite Plasmodium vivax; Biochem. J. 378(Pt2) 529
Goh et al. (2005), Cysteine protease falcipain 1 in Plasmodium falciparum is biochemically distinct from its isozymes; Parasitol. Res. 97 295
Pandey et al. (2004), Independent intramolecular mediators of folding, activity, and inhibition for the Plasmodium falciparum cysteine protease falcipain-2; J. Biol. Chem. 279 3484 |
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