525276
Phosphoramidon, Disodium Salt
Inhibits some metalloendopeptidases.
别名:
Phosphoramidon, Disodium Salt, N-(α-Rhamnopyranosyloxyhydroxyphosphinyl)-L-leucyl-L-tryptophan, 2Na
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
Quality Level
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
thermolysin
Product does not compete with ATP.
Reversible: no
Target IC50: 4.6 µM against the conversion of big endothelin-1 to endothelin
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.
Howell, S., et al. 1993. Biochem. J. 290, 159.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
Toxicity: Standard Handling (A)
存储类别
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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
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
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