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Merck
모든 사진(1)

Key Documents

525276

Sigma-Aldrich

Phosphoramidon, Disodium Salt

Inhibits some metalloendopeptidases.

동의어(들):

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

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About This Item

실험식(Hill 표기법):
C23H32N3O10P · 2Na
Molecular Weight:
587.47
UNSPSC 코드:
12352202
NACRES:
NA.77

Quality Level

형태

lyophilized solid

제조업체/상표

Calbiochem®

저장 조건

OK to freeze
desiccated (hygroscopic)
protect from light

색상

white

solubility

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

배송 상태

ambient

저장 온도

2-8°C

일반 설명

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).

생화학적/생리학적 작용

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

경고

Toxicity: Standard Handling (A)

분석 메모

Single spot by TLC

기타 정보

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

법적 정보

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

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable


시험 성적서(COA)

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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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