Basic information Safety Supplier Related

Z-LEU-ARG-7-AMINO-4-METHYLCOUMARIN

Basic information Safety Supplier Related

Z-LEU-ARG-7-AMINO-4-METHYLCOUMARIN Basic information

Product Name:
Z-LEU-ARG-7-AMINO-4-METHYLCOUMARIN
Synonyms:
  • Z-LEU-ARG-7-AMINO-4-METHYLCOUMARIN
  • Z-LEU-ARG-AMC
  • Z-LEU-ARG-AMC HYDROCHLORIDE
  • L-Argininamide, N-[(phenylmethoxy)carbonyl]-L-leucyl-N-(4-methyl-2-oxo-2H-1-benzopyran-7-yl)-
  • Benzyloxycarbonyl-L-leucyl-L-arginine 4-methylcoumaryl-7-amide
  • CBZ-Leu-Arg-AMC hydrochloride salt
CAS:
156192-32-4
MF:
C30H38N6O6
MW:
578.66
Mol File:
156192-32-4.mol
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Z-LEU-ARG-7-AMINO-4-METHYLCOUMARIN Chemical Properties

Density 
1.31±0.1 g/cm3(Predicted)
storage temp. 
Store at 0-5°C
solubility 
Soluble in DMSO
form 
solid
pka
11.13±0.46(Predicted)
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!
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Z-LEU-ARG-7-AMINO-4-METHYLCOUMARIN Usage And Synthesis

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

Z-LEU-ARG-7-AMINO-4-METHYLCOUMARINSupplier

GL Biochem (Shanghai) Ltd
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21-61263452 13641803416
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ymbetter@glbiochem.com
Shanghai Hanhong Scientific Co.,Ltd.
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Chemsky (shanghai) International Co.,Ltd
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021-50135380
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Nanjing Leon Biological Technology Co., Ltd.
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17705183659
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Nanjing Peptide Biotech Ltd.
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025-58361106-805 13082558573
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liugang@njpeptide.com