CTSL Human

Cathepsin-L is synthesized as an inactive preproenzyme. The cleavage of its 96-residue proregion is necessary to generate the fully active 221-residue mature enzyme . The enzyme is potent in degrading collagen, laminin, elastin, and other structural proteins of basement membranes . It also hydrolyzes a number of proteins, including the proform of urokinase-type plasminogen activator, which is activated by Cathepsin-L cleavage .

Cathepsin-L is involved in numerous physiological processes and pathological conditions. It participates in apoptosis, antigen processing, and extracellular matrix remodeling. These functions are implicated in various diseases, including tumor invasion and metastasis, inflammatory conditions, atherosclerosis, renal disease, diabetes, bone diseases, and viral infections .

Recombinant human Cathepsin-L is produced using various expression systems, including mouse myeloma cell lines and HEK293 cells . The recombinant protein is typically purified to high levels of purity, often exceeding 90% as determined by SDS-PAGE and HPLC . It is available in different formulations, including carrier-free versions that do not contain bovine serum albumin (BSA), which can interfere with certain applications .

Recombinant human Cathepsin-L is used in various research applications, including studies on protein degradation, cell cycle regulation, and disease mechanisms. It is also used in assays to measure its activity, such as the ability to cleave fluorogenic peptide substrates .

Recombinant human Cathepsin-L is typically shipped with dry ice or equivalent and should be stored at -20 to -70°C to maintain its stability. It is recommended to avoid repeated freeze-thaw cycles to preserve its activity .