CTSL Mouse

Cathepsin-L is a member of the peptidase C1 family and is composed of disulfide-linked heavy and light chains, both derived from a single protein precursor . The enzyme is initially synthesized as an inactive proenzyme (procathepsin L) and is activated through proteolytic cleavage. The active form of Cathepsin-L has a molecular mass of approximately 37 kDa .

The enzyme’s primary function is to degrade proteins within the lysosome, a cellular organelle responsible for breaking down waste materials and cellular debris. Cathepsin-L is particularly potent in degrading structural proteins of basement membranes, such as collagen and laminin . It also plays a role in the activation of other proteases, such as the proform of urokinase-type plasminogen activator .

Recombinant Mouse Cathepsin-L is produced using a mouse myeloma cell line (NS0) and is often tagged with a C-terminal 10-His tag for purification purposes . The recombinant form is used in various research applications, including studies on protein degradation, enzyme kinetics, and the role of Cathepsin-L in pathological processes.

The recombinant protein is typically supplied as a carrier-free solution in Tris and NaCl and is stable for up to six months when stored at -20 to -70°C . It is important to avoid repeated freeze-thaw cycles to maintain the protein’s activity.

Cathepsin-L has been implicated in several pathological processes, including myofibril necrosis in myopathies, myocardial ischemia, and the renal tubular response to proteinuria . Its ability to degrade extracellular matrix components makes it a key player in tissue remodeling and repair.

In research, recombinant Mouse Cathepsin-L is used to study its role in various diseases and to develop potential therapeutic interventions. For example, inhibitors of Cathepsin-L are being explored as potential treatments for conditions such as cancer, osteoporosis, and cardiovascular diseases.