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经验公式(希尔记法):
C33H36N6O6 · HCl
化学文摘社编号:
分子量:
649.14
UNSPSC Code:
12352204
PubChem Substance ID:
NACRES:
NA.32
MDL number:
产品名称
Z-Phe-Arg 7-酰氨基-4-甲基香豆素 盐酸盐, kallikrein substrate
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
assay
≥95% (HPLC)
form
powder
concentration
≥95%
solubility
methanol: 20 mg/mL, clear, colorless
storage temp.
−20°C
Quality Level
Application
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
Biochem/physiol Actions
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。
General description
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。
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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
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)
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)
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
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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