Cathepsin L is a lysosomal cysteine protease expressed in most eukaryotic cells. Cathepsin L is known to hydrolyze a number of proteins, including the proform of urokinase-type plasminogen activator, which is activated by Cathepsin L cleavage. Cathepsin L has also been shown to proteolytically inactivate a1-antitrypsin and secretory leucoprotease inhibitor, two major protease inhibitors of the respiratory tract.
Cathepsin L has been implicated in several pathologic processes, including rheumatoid arthritis, muscular dystrophy, Alzheimers, cancer, myofibril necrosis in myopathies and in myocardial ischemia, and in the renal tubular response to proteinuria
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Name Catalog # Size CARD8 RA30062 50 ug CARD9 RA30063 50 ug Caspase-10/b-Flice 2 RA15047 100 ug Caspase-12 RA15048 100 ug Caspase-14 RA30061 50 ug Caspase-3 GT15044 100 ug Caspase-3 (C terminal region) RA21011 50 ug Caspase-3 (N terminal region) RA21012 100 ug Caspase-3, active RA15046 50 ug Caspase-7 MO25036 100 ul Caspase-9 GT15045 100 ul Caspase-9 GT15045 50 ul Cathepsin B (Human) GT15046 100 ug Cathepsin B (Mouse) GT15047 100 ug Cathepsin D GT15042 100 ug Cathepsin F MO15096 500 ug Cathepsin G MO20021 100 ul Cathepsin L (Mouse) GT15049 100 ug Cathepsin O GT15197 100 ug Cathepsin S GT15198 100 ug Cathepsin V GT15199 100 ug