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제품정보 (DICE 배송 시 비용 별도)
실험식(Hill 표기법):
C33H36N6O6 · HCl
CAS 번호:
Molecular Weight:
649.14
UNSPSC Code:
12352204
PubChem Substance ID:
NACRES:
NA.32
MDL number:
제품 이름
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
A fluorogenic substrate for plasma kallikrein.
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.
저장 등급
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
L Troeberg et al.
Immunopharmacology, 36(2-3), 295-303 (1997-06-01)
Anti-peptide antibodies were produced against the cysteine proteinase trypanopain-Tb from Trypanosoma brucei brucei and the effects of these antibodies on enzyme activity against carboxybenzoyl (Z)-Phe-Arg-aminomethylcoumarin (AMC) investigated. A peptide was synthesised corresponding to a region of the trypanopain-Tb active site
L Salvati et al.
European journal of biochemistry, 268(11), 3253-3258 (2001-06-08)
Cysteine proteinases are relevant to several aspects of the parasite life cycle and of parasite-host relationships. Here, a quantitative investigation of the effect of temperature and pH on the total substrate inhibition of cruzipain, the major papain-like cysteine proteinase from
Cinthia Bernardes Gomes et al.
Biochimie, 133, 28-36 (2016-12-07)
Leishmania (Viannia) braziliensis presents adaptive protease-dependent mechanisms, as cysteine proteinases B (CPB). This study investigates the expression of three cpb gene isoforms and CPB enzymatic activity during the parasite differentiation. Relative expression levels of LbrM.08.0810 gene were assessed, exhibiting a