|Cathepsin L in Human Kidney. Cathepsin L was detected in immersion fixed paraffin-embedded sections of human kidney using Goat Anti-Human Cathepsin L Antigen Affinity-purified Polyclonal Antibody (Catalog # AF952) at 15 µg/mL overnight at 4 °C. Tissue was stained using the Anti-Goat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS008) and counterstained with hematoxylin (blue). Specific staining was localized to convoluted tubules. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.|
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 (1). Cathepsin L has also been shown to proteolytically inactivate alpha 1-antitrypsin and secretory leucoprotease inhibitor, two major protease inhibitors of the respiratory tract (2). These observations, combined with the demonstration of increased Cathepsin L activity in the epithelial lining fluid of the lungs of emphysema patients, have led to the suggestion that the enzyme may be involved in the progression of this disease. Cathepsin L has also been identified as a major excreted protein of transformed fibroblasts, indicating the enzyme could be involved in malignant tumor growth (3). Human Cathepsin L activity is greatest under mildly acidic conditions, from pH 4.5‑6.5. The stability of the enzyme decreases at higher pH values.
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