Research area: Cell Signaling
Cathepsin L, Human Liver, native, is the most potent of all the lysosomal proteinases. Cathepsin L (CTSL) belongs to the papain subfamily of cysteine proteases and is mainly located in endolysosomal vesicles.

Cathepsin L (CTSL) has higher activity than cathepsins B and H in the degradation of a variety of physiological protein substrates. It is believed to be responsible for the generation of endostatin from the NC1 domain in collagen XVII. It is responsible for regulating cell cycle, nucleotide-binding domain, leucine-rich–containing family, pyrin domain–containing-3 (NLRP3) inflammasome activation, proteolytic processing of Bid during apoptosis, and TGF-β signaling. It can degrade a wide range of proteins, encompassing enzymes, receptors, and transcription factors. Additionally, it produces active enzymes, receptors, and biologically active peptides through controlled proteolysis. Moreover, Cathepsin L has been observed to enhance tumor cell migration by lowering cell-cell adhesion and breaking down elements of the extracellular matrix. The expression of CTSL escalates in several types of cancers, including glioma, melanoma, pancreatic, prostate, and breast cancer. It plays a major role in the proteolysis of both cellular and endocytosed macromolecules.

Please refer to vial label for lot-specific concentration.

Toxicity: Standard Handling (A)

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.

In 400 mM NaCl, 20 mM malonate buffer, 1 mM EDTA, 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.

Following initial thaw, aliquot and freeze (-70°C).

Note: 1 mU = 1 milliunit

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany