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Merck
CN
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文件

525276

Sigma-Aldrich

Phosphoramidon, Disodium Salt

Inhibits some metalloendopeptidases.

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别名:
Phosphoramidon, Disodium Salt, N-(α-Rhamnopyranosyloxyhydroxyphosphinyl)-L-leucyl-L-tryptophan, 2Na
经验公式（希尔记法）:
C23H32N3O10P · 2Na
分子量:
587.47
UNSPSC代码:
12352200
NACRES:
NA.77

质量水平

100

形式

lyophilized solid

制造商/商品名称

Calbiochem®

储存条件

OK to freeze
desiccated (hygroscopic)
protect from light

颜色

white

溶解性

DMSO: 10 mg/mL
methanol: soluble
water: soluble

运输

ambient

储存温度

2-8°C

一般描述

Effective concentration: 1-10 µM.
Inhibits some metalloendopeptidases. Highly specific inhibitor of thermolysin. Inhibits the conversion of big endothelin-1 to endothelin (IC50 = 4.6 µM).

生化/生理作用

Cell permeable: no
Primary Target
thermolysin
Product does not compete with ATP.
Reversible: no
Target IC50: 4.6 µM against the conversion of big endothelin-1 to endothelin

警告

Toxicity: Standard Handling (A)

分析说明

Single spot by TLC

其他说明

Balwierczxak, J.L., et al. 1995. Biochem. Pharmacol. 49, 291.
Howell, S., et al. 1993. Biochem. J. 290, 159.

法律信息

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

WGK

WGK 1

闪点(°F)

Not applicable

闪点(°C)

Not applicable

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J L Balwierczak et al.
Biochemical pharmacology, 49(3), 291-296 (1995-01-31)
The enzyme responsible for the conversion of exogenous big endothelin-1 to endothelin-1 by porcine coronary arterial smooth muscle has been shown to be a metalloprotease. The potencies of eight metalloprotease inhibitors for this endothelin-converting enzyme were determined. CGS 25015, CGS
Jan Perner et al.
Frontiers in cellular and infection microbiology, 10, 563349-563349 (2020-12-15)
During feeding on vertebrate hosts, ticks secrete saliva composed of a rich cocktail of bioactive molecules modulating host immune responses. Although most of the proteinaceous fraction of tick saliva is of little immunogenicity, repeated feeding of ticks on mammalian hosts
S Howell et al.
The Biochemical journal, 290 ( Pt 1), 159-164 (1993-02-15)
Five membrane peptidase activities have been identified on cultured human osteoblast-like cells. These consisted of the four exopeptidases aminopeptidase-A, aminopeptidase-N, aminopeptidase-W and carboxypeptidase-M, and the endopeptidase, endopeptidase-24.11. The presence of endopeptidase-24.11 was confirmed immunochemically by immunofluorescent staining and by enzyme-linked

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