Mouse Cathepsin B Alexa Fluor® 594-conjugated Antibody

Applications

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Preparation and Storage

Background: Cathepsin B

Cathepsin B is the first described member of the family of lysosomal cysteine proteases (1). Cathepsin B possesses both endopeptidase and exopeptidase activities, in the latter case acting as a peptidyl-dipeptidase. It is known to process a number of proteins, including pro and active caspases, prorenin and secretory leucoprotease inhibitor (SLPI) (2‑4). Therefore, Cathepsin B may play a role in activation and inactivation of caspases, activation of renin and inactivation of SLPI, the key steps in apoptosis, angiotensin production, and progression of emphysema, respectively. Because of its increased levels and redistribution in human and animal tumors, Cathepsin B may also have a role in invasion and metastasis (5). In addition to the lysosome, Cathepsin B can be secreted or associated with plasma membrane, cytoplasm, and nucleus. It is synthesized as a preproenzyme. Following removal of the signal peptide, the inactive proenzyme undergoes further modifications including removal of the pro region to result in the active enzyme (5).

Product Datasheets

Related Research Areas

• APP Processing and Amyloid Plaque Formation
• Cathepsins
• Chondrogenesis Markers
• Cysteine Proteases and Regulators
• Granzyme-mediated Cell Death
• Lysosomal Enzymes
• Proteolytic Degradation of Amyloid beta