Anti-Calpain, clone Calp3C/12A2 (monoclonal) [Mouse]

Muscle specific calcium activated neutral protease, or calpain-3, is a 94kD nonlysosomal intracellular cysteine protease. It belongs to the calpain family, which includes three ubiquitous enzymes and several tissue specific forms. Tissue specific enzymes, such as calpain-3, appear to lack the regulatory subunit. The large subunits of calpains can be divided into four domains. The N-terminal region of domain I is autocatalytically cleaved during activation by calcium ions and it has been suggested that domain I may be involved in the regulation of proteolytic activity. Domain II is thought to contain the cysteine proteases active site, no function has been assigned to domain III and domain IV contains structures involved in calcium binding. In addition calpain-3 has three unique regions, namely NS at the beginning of domain I, IS1 in the protease domain and IS2 in domain III. These regions show little homology to other proteins but IS2 contains a nuclear translocation signal. It is thought that these regions may be important for the muscle specific function of calpain-3. This antibody reacts with fullsize calpain 3 (94kD) plus an additional breakdown product at 60kD in human skeletal muscle. The 94kD band can be seen in muscle extracts from rabbit, mouse, dog, chicken, hamster, pig and rat. Protein function: Calcium-regulated non-lysosomal thiol-protease. Proteolytically cleaves CTBP1 at 'His-409'. [The UniProt Consortium] Protein function: Calcium-regulated non-lysosomal thiol-protease. Proteolytically cleaves CTBP1 at 'His-409'. [The UniProt Consortium]