Cathepsin L (Mouse)

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.

Image: Cathepsin L staining of perfusion fixed frozen sections of mouse ovary (15 µg/mL) overnight at 4 °C. Tissue was stained using the Anti-Goat HRP-DAB (brown) and counterstained with hematoxylin (blue).

Image: Image: Cathepsin L staining of perfusion fixed frozen sections of mouse thymus (15 µg/mL) overnight at 4 °C. Tissue was stained using the Anti-Goat HRP-DAB (brown) and counterstained with hematoxylin (blue).