Description
General description
A cell-permeable sulfanilide compound that acts as a potent, substrate-competitive, and highly specific inhibitor of neutrophil elastase (IC₅₀ = 19-49 nM in rat, rabbit, hamster, human, and mouse leukocyte elastase). Displays >100-fold greater selectivity over pancreas elastase (IC₅₀ = 5.6 µM). Does not inhibit trypsin, thrombin, plasmin, kallikrein, chymotrypsin, and cathepsin G even at concentrations as high as 100 µM. Effectively suppresses human neutrophil elastase-induced lung hemorrhage and skin capillary permeability in vivo. Also reported to inhibit mast cell Stat6-protease.
A cell-permeable, potent, substrate-competitive, and highly specific inhibitor of neutrophil elastase (IC₅₀ = 19-49 nM using rat, rabbit, hamster, human, and mouse leukocyte elastase). Displays about 100-fold greater selectivity over pancreatic elastase (IC₅₀ = 5.6 µM) and is inactive against trypsin, thrombin, plasmin, kallikrein, chymotrypsin, and cathepsin G even at concentrations as high as 100 µM. Effectively suppresses human neutrophil elastase-induced lung hemorrhage and skin capillary permeability in vivo. Also reported to inhibit mast cell Stat6-protease.
Biochem/physiol Actions
Cell permeable: yes
Primary Target
Neutrophil elastase
Product does not compete with ATP.
Reversible: no
Target IC₅₀: 19-49 nM in rat, rabbit, hamster, human, and mouse leukocyte elastase
Packaging
Packaged under inert gas
Preparation Note
Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.
Other Notes
Suzuki, K., et al. 2003. Biochem. Biophys. Res. Commun.309, 768.
Kawabata, K., et al. 1991. Biochem. Biophys. Res. Commun.177, 814.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
Toxicity: Standard Handling (A)
