|Related Categories||Biochemicals and Reagents, Broad Spectrum Inhibitors of Proteolytic Enzyme Classes, Cell Biology, Cell Signaling and Neuroscience, Core Bioreagents,|
|solubility||H2O: soluble10 mM (Solutions are stable for a week at 4 °C. Stock solutions are stable up to 6 months at −20 °C.)|
|H2O: soluble50 mg/mL|
Leupeptin gives multiple peaks on HPLC due to equilibria among three forms in solution. Purity determined using three main peaks. Majority of contaminating peptide is racemized leupeptin.
Inhibitor of serine and cysteine proteases. Inhibits plasmin, trypsin, papain, calpain, and cathepsin B. Does not inhibit pepsin, cathepsins A and D, thrombin, or α-chymotrypsin. Effective concentration 10-100 μM. There have been numerous studies using leupeptin to protect against hearing loss caused by acoustic overstimulation or the ototoxic antibiotic gentamicin.1 (Loss of cochlear hair cells is believed to be mediated by calpain.)
Certificate of Analysis
Certificate of Origin
Saino, T., et al. Chem. Pharm. Bull. 30, 2319, (1982)
Beynon, R.J. and Bond, ed. Proteolytic Enzymes: A Practical Approach, (1989), 244-245
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