CTSB Mouse, Active

Cathepsin B is a lysosomal cysteine protease that belongs to the family of cysteine cathepsins. It plays a crucial role in intracellular proteolysis, which is the breakdown of proteins within cells. In mice, cathepsin B is encoded by the CTSB gene located on chromosome 14 .

Cathepsin B is synthesized as an inactive proenzyme and undergoes proteolytic processing to become an active enzyme. The active form of cathepsin B is a single, glycosylated polypeptide chain containing 330 amino acids, with a molecular mass of approximately 36.4 kDa . The enzyme is characterized by its ability to cleave peptide bonds, particularly at acidic pH levels found within lysosomes .

Cathepsin B is involved in various physiological processes, including protein degradation, antigen processing, and tissue remodeling. It is also implicated in pathological conditions such as cancer, inflammation, and neurodegenerative diseases. The enzyme’s activity is regulated by its localization within lysosomes and its interaction with specific substrates .

Recombinant cathepsin B (mouse) is produced using baculovirus expression systems in Sf9 insect cells. This method allows for the production of large quantities of the enzyme with high purity and activity. The recombinant enzyme retains the biochemical properties of the native enzyme, making it suitable for research and therapeutic applications .

Recombinant cathepsin B is widely used in biochemical and biomedical research. It serves as a valuable tool for studying the enzyme’s structure, function, and role in disease. Additionally, it is used in drug discovery and development, particularly in the design of inhibitors that target cathepsin B activity in pathological conditions .