Advantages at a glance
- Assay: min. 96.5% (HPLC)
- Peptide content: min. 85%
- Solubility (1%, H2O): clear solution
- Formula: C20H38N6O4 x 1/2 H2SO4
- MW: 475.60 g/mol
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Product information "Leupeptin hemisulfate"
Leupeptin works as peptide antibiotic that has been isolated from different Streptomyces species. It is a reversible inhibitor of serine and cysteine proteases, eg. Plasmin, Trypsin, Papain, Cathepsin B and Thrombin. It does not inhibit pepsin, cathepsin A and D. The working concentration is 10-100µM (5 - 50µg/mL).
Leupeptin is soluble in water. A 1mg/mL stock solution can be stored at -20°C for 6 months. Umezawa, H. (1976) Methods Enzymol. 45 (Part B), 678-695. Brass, L.F. & Smith, S.J. (1988) J. Biol. Chem. 263, 5210-5216.
You will find further protease inhibitors here: Inhibitors >: Pepstatin A >, AEBSF >, Leupeptin >, TLCK >, or Bestatine >.
Specifications:
Assay: min. 96.5% (HPLC)
Peptide content: min. 85%
Solubility (1%, H2O): clear solution
C20H38N6O4 x 1/2 H2SO4
MW: 475.60 g/mol
Source:
Streptomyces SpezcesSafety Information:
Classification:
Documents:
Safety Data SheetCertificate
General Data 1
Category List
Source: NCBI PubMed
Accessory Items
Papain is a member of the class of proteolytic enzymes that needs a free sulfhydryl group for activity (group of the cysteine proteases). The pH optimum of Papain is approx. pH 6 and the optimum temperature for activity is 65°C. At the isoelectric point of approx. pH 9.6, the best solubility is achieved. Please note that even at this point, Papain will be dissolved incompletely. The recommended solvent is water.