CTSB Mouse

Cathepsin B is a papain-family cysteine protease that is normally located in lysosomes . It possesses both endopeptidase and exopeptidase activities, meaning it can act on peptide bonds within a protein as well as at the ends of peptide chains . This dual functionality allows Cathepsin B to process a variety of proteins, including pro and active caspases, prorenin, and secretory leucoprotease inhibitor (SLPI) .

Cathepsin B plays several critical roles in maintaining normal cellular metabolism. It is involved in the turnover of proteins within lysosomes, contributing to the degradation and recycling of cellular components . Additionally, Cathepsin B is implicated in several pathological conditions, such as tumor progression and arthritis .

Recombinant Mouse Cathepsin B is produced using various expression systems, such as HEK293 cells or mouse myeloma cell lines . The recombinant protein is typically tagged with a His-tag for purification purposes and is available in both carrier-free and carrier-containing formulations . The purity of these recombinant proteins is generally greater than 95%, as determined by SDS-PAGE .

Recombinant Mouse Cathepsin B is widely used in research to study its enzymatic activity and role in various biological processes. It is also used in assays to measure the cleavage of specific substrates, providing insights into its function and regulation .

Lyophilized recombinant Cathepsin B proteins are stable for up to 12 months when stored at -20 to -80°C . Once reconstituted, the protein solution can be stored at 4-8°C for 2-7 days or at < -20°C for up to 3 months .