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Merck
CN

C3022

Z-Gly-Gly-Leu p-nitroanilide

protease substrate

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关于此项目

经验公式(希尔记法):
C24H29N5O7
化学文摘社编号:
分子量:
499.52
NACRES:
NA.32
PubChem Substance ID:
UNSPSC Code:
12352204
MDL number:
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InChI

1S/C24H29N5O7/c1-16(2)12-20(23(32)27-18-8-10-19(11-9-18)29(34)35)28-22(31)14-25-21(30)13-26-24(33)36-15-17-6-4-3-5-7-17/h3-11,16,20H,12-15H2,1-2H3,(H,25,30)(H,26,33)(H,27,32)(H,28,31)

SMILES string

CC(C)CC(NC(=O)CNC(=O)CNC(=O)OCc1ccccc1)C(=O)Nc2ccc(cc2)N(=O)=O

InChI key

IHRYETONKBXGOF-UHFFFAOYSA-N

assay

≥98% (TLC)

form

powder

solubility

methanol: 50 mg/mL, clear, colorless to faintly yellow

storage temp.

−20°C

General description

A sensitive chromogenic substrate for subtilisins and neutral endopeptidases.

存储类别

13 - Non Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

法规信息

常规特殊物品
此项目有

历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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Degradation of bradykinin by isolated neutral endopeptidases of brain and pituitary.
S Wilk et al.
Biochemical and biophysical research communications, 90(1), 1-6 (1979-09-12)
A new chromogenic substrate for subtilisin.
L A Lyublinskaya et al.
Analytical biochemistry, 62(2), 371-376 (1974-12-01)
B J Wagner et al.
Experimental eye research, 38(5), 477-483 (1984-05-01)
Lens neutral proteinase is thought to exhibit primarily endopeptidase activity. We have identified a synthetic endopeptidase substrate which is hydrolyzed by the bovine lens neutral proteinase preparation. Among 11 fluoro- and chromogenic endopeptidase substrates, only carbobenzoxy-glycylglycyl-L-leucyl-p-nitroanilide is effectively hydrolyzed. The
J R Arbona et al.
Journal of animal science, 71(12), 3301-3306 (1993-12-01)
Within 1 h after slaughter, two 10-g samples of longissimus muscle were obtained from four crossbred beef cattle. Samples were homogenized in three or six volumes of extraction solution that consisted of 50 mM Tris base, 10 mM EDTA, and
Ajay Kumar Shaw et al.
Journal of photochemistry and photobiology. B, Biology, 86(3), 199-206 (2006-11-18)
Enzymatic activity of a proteolytic enzyme Subtilisin Carlsberg (SC) in anionic sodium dodecyl sulfate (SDS) micellar medium has been explored and found to be retarded compared to that in bulk buffer. Circular dichroism (CD) study reveals that SDS, which is

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