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Merck
CN

C9521

Z-Phe-Arg 7-酰氨基-4-甲基香豆素 盐酸盐

kallikrein substrate, ≥95% (HPLC), powder

别名:

Z-Phe-Arg-AMC

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关于此项目

经验公式(希尔记法):
C33H36N6O6 · HCl
化学文摘社编号:
分子量:
649.14
MDL编号:
UNSPSC代码:
12352204
PubChem化学物质编号:
NACRES:
NA.32
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产品名称

Z-Phe-Arg 7-酰氨基-4-甲基香豆素 盐酸盐, kallikrein substrate

质量水平

方案

≥95% (HPLC)

表单

powder

浓度

≥95%

溶解性

methanol: 20 mg/mL, clear, colorless

储存温度

−20°C

SMILES字符串

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

一般描述

Z-苯丙氨酸-精氨酸 7-氨基-4-甲基香豆素(Z-FR-AMC)是一种拟肽类底物,可用于木瓜蛋白酶和其它酶,如组织蛋白酶K。它也是组织蛋白酶L和B的荧光合成肽。
一种用于血浆激肽释放酶的荧光底物。

应用

Z-苯丙氨酸-精氨酸7-氨基-4-甲基香豆盐酸盐已被用于:
  • 作为猕猴桃碱抑制检测中的荧光底物
  • 作为血管舒缓素底物
  • 作为荧光检测的胰蛋白酶底物
  • 作为组织蛋白酶-L底物

生化/生理作用

由蛋白酶引发的Z-苯丙氨酸-精氨酸7-氨基-4-甲基香豆素(Z-FR-AMC)的蛋白水解性裂解导致AMC的释放,结果使酶反应中的荧光增强。

储存分类代码

11 - Combustible Solids

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable

个人防护装备

Eyeshields, Gloves, type N95 (US)


历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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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
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
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
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

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