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C9521

Sigma-Aldrich

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

kallikrein substrate, ≥95% (HPLC), powder

Synonym(s):

Z-Phe-Arg-AMC

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About This Item

Empirical Formula (Hill Notation):
C33H36N6O6 · HCl
CAS Number:
70382-26-2
Molecular Weight:
649.14
MDL number:
MFCD00077030
UNSPSC Code:
12352204
PubChem Substance ID:
24893165
NACRES:
NA.32
Pricing and availability is not currently available.

Product Name

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

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 papain[1]and other enzymes such as cathepsin K.[2] It is also a fluorogenic synthetic peptide for the enzymes cathepsins L and B.[3]

Application

Z-Phe-Arg 7-amido-4-methylcoumarin hydrochloride has been used:
  • as a fluorogenic substrate in actinidin inhibition assay[4]
  • as a kallikrein substrate[5]
  • as a trypsin substrate for fluorometric assay[6]
  • as a cathepsin-L substrate[7]

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.[1]

Substrates

A fluorogenic substrate for plasma kallikrein.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Certificates of Analysis (COA)

Lot/Batch Number
MKCV1775
MKCS0227
MKCP6580
MKCM1094
MKCJ7050

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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
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
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
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
Najju Ranjit et al.
Molecular and biochemical parasitology, 160(2), 90-99 (2008-05-27)
mRNAs encoding cathepsin B-like cysteine proteases (CatBs) are abundantly expressed in the genomes of blood-feeding nematodes. Recombinant CatBs have been partially efficacious in vaccine trials in animal models of hookworm infection, supporting further investigation of these enzymes as new control
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