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Merck
모든 사진(2)

주요 문서

C9521

Sigma-Aldrich

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

kallikrein substrate, ≥95% (HPLC), powder

동의어(들):

Z-Phe-Arg-AMC

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크기 선택

25 MG
₩1,013,072
100 MG
₩3,032,617

₩1,013,072


구입 가능 여부는 고객센터에 문의하십시오.


크기 선택

보기 변경
25 MG
₩1,013,072
100 MG
₩3,032,617

About This Item

실험식(Hill 표기법):
C33H36N6O6 · HCl
CAS Number:
Molecular Weight:
649.14
MDL number:
UNSPSC 코드:
12352204
PubChem Substance ID:
NACRES:
NA.32

₩1,013,072


구입 가능 여부는 고객센터에 문의하십시오.

제품명

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

Quality Level

분석

≥95% (HPLC)

양식

powder

농도

≥95%

solubility

methanol: 20 mg/mL, clear, colorless

저장 온도

−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

일반 설명

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]

애플리케이션

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]

생화학적/생리학적 작용

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]

기질

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

개인 보호 장비

Eyeshields, Gloves, type N95 (US)


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문서 라이브러리 방문

Early ontogenetic development, digestive enzymatic activity and gene expression in red sea bream (Pagrus major)
Khoa TND, et al.
Aquaculture (Amsterdam, Netherlands), 512, 734283-734283 (2019)
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
Quantification of Functional Actinidin in Whole Kiwifruit Extract Using the Selective Cysteine Proteinase Inhibitor E-64
Martin H
Journal of Food & Nutrition Research, 4(4), 243-250 (2016)
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
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

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