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Merck
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Key Documents

525276

Sigma-Aldrich

Phosphoramidon, Disodium Salt

Inhibits some metalloendopeptidases.

别名:

Phosphoramidon, Disodium Salt, N-(α-Rhamnopyranosyloxyhydroxyphosphinyl)-L-leucyl-L-tryptophan, 2Na

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About This Item

经验公式（希尔记法）:
C23H32N3O10P · 2Na
分子量:
587.47
分類程式碼代碼:
12352202
NACRES:
NA.77

品質等級

100

形狀

lyophilized solid

製造商／商標名

Calbiochem®

儲存條件

OK to freeze
desiccated (hygroscopic)
protect from light

顏色

white

溶解度

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

運輸包裝

ambient

儲存溫度

2-8°C

一般說明

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)

分析報告

Single spot by TLC

其他說明

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

法律資訊

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

儲存類別代碼

11 - Combustible Solids

水污染物質分類（WGK）

WGK 1

閃點（°F）

Not applicable

閃點（°C）

Not applicable

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Jan Perner et al.
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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
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
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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