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Key Documents

525276

Sigma-Aldrich

Phosphoramidon, Disodium Salt

Inhibits some metalloendopeptidases.

Sinónimos:

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

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About This Item

Fórmula empírica (notación de Hill):
C23H32N3O10P · 2Na
Peso molecular:
587.47
UNSPSC Code:
12352202
NACRES:
NA.77

Quality Level

form

lyophilized solid

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze
desiccated (hygroscopic)
protect from light

color

white

solubility

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

shipped in

ambient

storage temp.

2-8°C

General description

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).

Biochem/physiol Actions

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

Warning

Toxicity: Standard Handling (A)

Analysis Note

Single spot by TLC

Other Notes

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

Legal Information

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

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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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
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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