Human Cathepsin L Antibody

Applications

Human Cathepsin L Sandwich Immunoassay

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Scientific Data

Western Blot View Larger

Detection of Recombinant Human Cathepsin L by Western Blot. Western blot shows 10 ng of Recombinant Human Cathepsin L (952-CY), Recombinant Mouse Cathepsin L (1515-CY), Recombinant Human Cathepsin V (1080-CY), Recombinant Human Cathepsin K, Recombinant Human Cathepsin S (1183-CY), Recombinant Human Cathepsin H (7516-CY), and Recombinant Human Cathepsin F. PVDF Membrane was probed with 0.1 µg/mL of Goat Anti-Human Cathepsin L Antigen Affinity-purified Polyclonal Antibody (Catalog # AF952) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (HAF109). A specific band was detected for Cathepsin L at approximately 35 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 3.

Immunohistochemistry View Larger

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; 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.

Preparation and Storage

Background: Cathepsin L

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.

Product Datasheets

Related Research Areas

• Cathepsins
• Cysteine Proteases and Regulators
• Lysosomal Enzymes