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Merck

C9521

Sigma-Aldrich

Z-Phe-Arg 7-amido-4-methylcoumarin hydrochloride

kallikrein substrate, ≥95% (HPLC), powder

Sinónimos:

Z-Phe-Arg-AMC

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About This Item

Fórmula empírica (notación de Hill):
C33H36N6O6 · HCl
Número de CAS:
Peso molecular:
649.14
MDL number:
UNSPSC Code:
12352204
PubChem Substance ID:
NACRES:
NA.32

Nombre del producto

Z-Phe-Arg 7-amido-4-methylcoumarin hydrochloride, kallikrein substrate

Quality Level

assay

≥95% (HPLC)

form

powder

concentration

≥95%

solubility

methanol: 20 mg/mL, clear, colorless

storage temp.

−20°C

SMILES string

O=C(N[C@@H](CC1=CC=CC=C1)C(N[C@@H](CCCNC(N)=N)C(NC2=CC=C(C(C)=CC(O3)=O)C3=C2)=O)=O)OCC4=CC=CC=C4.[Cl]

InChI

1S/C33H36N6O6/c1-21-17-29(40)45-28-19-24(14-15-25(21)28)37-30(41)26(13-8-16-36-32(34)35)38-31(42)27(18-22-9-4-2-5-10-22)39-33(43)44-20-23-11-6-3-7-12-23/h2-7,9-12,14-15,17,19,26-27H,8,13,16,18,20H2,1H3,(H,37,41)(H,38,42)(H,39,43)(H4,34,35,36)

InChI key

ZZGDDBWFXDMARY-UHFFFAOYSA-N

General description

Z-Phe-Arg 7-amido-4-methylcoumarin (Z-FR-AMC) is a peptidomimetic substrate for papainand other enzymes such as cathepsin K. It is also a fluorogenic synthetic peptide for the enzymes cathepsins L and B.

Application

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

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.

Substrates

A fluorogenic substrate for plasma kallikrein.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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C Illy et al.
The Journal of biological chemistry, 272(2), 1197-1202 (1997-01-10)
Within the lysosomal cysteine protease family, cathepsin B is unique due to its ability to act both as an endopeptidase and a peptidyldipeptidase. This latter capacity to remove C-terminal dipeptides has been attributed to the presence of a 20-residue insertion
P J Rosenthal
Experimental parasitology, 80(2), 272-281 (1995-03-01)
The effects of peptide proteinase inhibitors on globin hydrolysis by cultured malaria parasites were studied. All of the four cysteine proteinase inhibitors evaluated blocked globin hydrolysis, as documented by the development of a morphological abnormality in which parasite food vacuoles
R M C Deshapriya et al.
Journal of biochemistry, 147(3), 393-404 (2009-11-17)
To identify functionally essential sequences and residues of CTLA-2alpha, in vitro mutagenesis was carried out. The coefficient of inhibition (K(i)) was determined towards rabbit cathepsin L using Z-Phe-Arg-MCA as the substrate. Recombinant CTLA-2alpha inhibited the enzyme potently (K(i) = 15
Fabien Lecaille et al.
The Biochemical journal, 375(Pt 2), 307-312 (2003-07-03)
The limited availability of highly selective cathepsin substrates seriously impairs studies designed to monitor individual cathepsin activities in biological samples. Among mammalian cysteine proteases, cathepsin K has a unique preference for a proline residue at P2, the primary determinant of
H Ghoneim et al.
International journal for parasitology, 25(12), 1515-1519 (1995-12-01)
A previously described "major acidic proteinase" of adult Schistosoma mansoni, believed to play a key role in the parasite's metabolism, has been identified as a cathepsin B (Sm31). Purified Sm cathepsin B was not recognized by anti-Sm32 or anti-cathepsin L

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