Name: Leupeptin, Microbial
Price: 260.00 USD

- Overview
  - Please contact us at for specific academic pricing.
    
    Background
    
    Leupeptin is a reversible inhibitor of protease with Ki values of 35 nM, 3.4 μM, 6 nM and 72 nM for bovine trypsin, human plasmin, bovine spleen cathepsin B and recombinant human calpain, respectively [1, 2].
    As a protease inhibitor, leupeptin was originally isolated from the Streptomyces species. It exerted poor membrane permeability due to its polar C-terminal. For calpain, leupeptin showed moderate potent activities with IC50 values of 0.211 μM, 1.8 μM and 0.938 μM against the enzymes isolated from porcine erythrocyte, porcine kidney and human platelet, respectively. In cultured MRC-C cells, leupeptin suppressed the growth of human coronavirus strain 229E through inhibited the activity of trypsin. The mean IC50 value was 0.8 μM [2, 3].
    
    1. Mehdi S. Cell-penetrating inhibitors of calpain. Trends in biochemical sciences, 1991, 16: 150-153.
    2. Krauser J A, Powers J C. 6.1 BIOLOGICAL ROLES. Proteinase and Peptidase Inhibition: Recent Potential Targets for Drug Development, 2003: 144.
    3. Appleyard G, Tisdale M. Inhibition of the growth of human coronavirus 229E by leupeptin. Journal of general virology, 1985, 66(2): 363-366.
- Properties
  - Alternative Name
    
    Leupeptin hemisulfate salt microbial,L-Leucinamide,Leupeptin, Microbial; 2-acetamido-N-(1-((5-((diaminomethylene)amino)-1-oxopentan-2-yl)amino)-4-methyl-1-oxopentan-2-yl)-4-methylpentanamide
    
    CAS Number
    
    103476-89-7
    
    Molecular Formula
    
    C20H38N6O4·1/2H2SO4
    
    Molecular Weight
    
    475.59
    
    Purity
    
    98.00%
    
    Solubility
    
    ≥24.7 mg/mL in DMSO; ≥53.5 mg/mL in EtOH; ≥54.4 mg/mL in H2O
    
    Storage
    
    Store at -20°C. The product is not stable in solution, please dissolve it immediately before use.
    
    * For Research Use Only
- Reference
  - 1. Vimala Bondada, Jozsef Gal, et al. "The C2 domain of calpain 5 contributes to enzyme activation and membrane localization." Biochim Biophys Acta Mol Cell Res. 2021 Jun;1868(7):119019. PMID:33811937
    2. HeLia, GuanghuiDanga, et al. "Characterization of a novel Mycobacterium tuberculosis serine protease (Rv3194c) activity and pathogenicity." Tuberculosis. Available online 4 November 2019, 101880.