Synonyms: Leupeptin hemisulfate salt; Acetyl-Leu-Leu-Arg-al; N-Acetyl-L-leucyl-L-leucyl-L-argininal hemisulfate salt
Empirical Formula (Hill Notation): C20H38N6O4 ¬? 0.5H2O4S
Formula Weight: 475.59
Linear Formula: C20H38N6O4 ¬? 1/2H2SO4
MDL Number: MFCD00037012
Purity: ‚≥96.5%
Storage: 2-8°C
UNSPSC Code: 12352200
RIDADR: NONH for all modes of transport
Analysis Note:
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.
Features and Benefits:
Contents
Synthetic, white powder
Application:
Leupeptin as well as other protease inhibitors like antipain, chymostatin, pepstatin, and phosphoramidon are useful for the protection of proteins during their isolation from tissues or membranes. Leupeptin can be removed from the reaction by dialysis.
Note: To check other protease inhibitors, try our Protease Inhibitor Set including Antipain Dihydrochloride, Aprotinin, Bestatin, Chymostatin, E-64, EDTA-Na2, Leupeptin, Pefabloc SC, Pepstatin, and Phosphoramidon.
Biochem/physiol Actions:
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. (Loss of cochlear hair cells is believed to be mediated by calpain.)
Other Notes:
For life science research only. Not for use in diagnostic procedures.
Quality:
Function test: Performance controlled with trypsin.
Preparation Note:
Working concentration: 0.5 to 5 μg/ml (1 to 20 μM)
Comparison of working concentrations of pefabloc with leupeptin and PMSF is in files.
Working solution: Solvent is recommended in distilled water.
Highly soluble in water (1 mg/ml), methanol, ethanol, acetic acid, dimethyl formamide and dimethyl sulfoxide.
Poorly soluble in acetone, chloroform, ethyl ether and n-hexane.
Storage conditions (working solution): -15 to -25 °C
In aqueous solution leupeptin is stable for 1 month at 2 to 8 °C or for at least 6 months at - 15 to -25 °C, stored under nitrogen. For best results, freeze the dissolved inhibitor in aliquots and avoid repeated thawing.
Reconstitution:
Highly soluble in water (1 mg/ml). Stable for at least one week at 2 to 8 °C and 6 months frozen in aliquots at -15 to -25 °C.
Specificity:
Leupeptin inhibits serine and thiol proteases such as trypsin, plasmin, proteinase K, kallikrein, papain, thrombin, and cathepsin A and B.
Not affected are α-, β-, γ- and δ- chymotrypsin, pepsin, cathepsin D, elastase, renin, and thermolysin.