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  Cathepsin L, Human Liver
Cat. No. 219402  
All Categories » Calbiochem » Proteins and Enzymes » Proteases » Cathepsins

Liquid. In 400 mM NaCl, 20 mM malonate buffer, 1 mM EDTA, pH 5.5. AVOID FREEZE/THAW CYCLES. Native cathepsin L from human liver. The most potent of the lysosomal proteinases, having a higher activity than cathepsins B and H in the degradation of a variety of physiological protein substrates. Cathepsin L is believed to be responsible for the generation of endostatin from NC1 domain in collagen XVII. One unit is defined as the amount of enzyme that will hydrolyze 1.0 µmol of Z-FR-AFC per min at 25°C, pH 5.5. Prepared from tissue of individuals that have been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV. EC 3.4.22.15. Note: 1 mU = 1 milliunit.

Merck Index: 14, 1905
Ref.: Kurata, M., et al. 2001. J. Biochem. (Tokyo) 130, 857. Ferreras, M., et al. 2000. FEBS Lett. 486, 247. Baricos, W.H., et al. 1988. Biochem. J. 252, 301. McDonald, J.K., et al. 1988. Biochem. Biophys. Res. Commun. 151, 827.

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SolubilityMolecular FormulaMol. Wt.
  29000 

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219402: Cathepsin L, Human Liver - English
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All Categories » Calbiochem » Proteins and Enzymes » Proteases » Cathepsins

Selected Citations:
  1. Moin U Fareed, et al. (2006) Treatment of rats with calpain inhibitors prevents sepsis-induced muscle proteolysis independent of atrogin-1/MAFbx and MuRF1 expression. American Journal of Physiology Regulatory, Integrative and Comparative Physiology 290, R1589-R1597.