Description
Product Characteristics:
Calpain, and m calpain, also known as Calpain 2, are intracellular, calcium dependent cysteine proteases. Mu calpain has a micromolar sensitivity (thus the mu) as compared to the millimolar calcium sensitivity of m calpain. Both Calpains 1 and 2 are composed of an 80 kD subunit and a 30 kD subunit. Whereas the 30 kDa subunit is shared by both enzymes, the larger catalytic subunits are different and exhibit the distinct Ca++ requirements that are suggested by their names. The calpains have papain like activity, thus the pain nomenclature. Both Calpain 1 and Calpain 2 are ubiquitously expressed, and are countered by the endogenous calpain inhibitor, calpastatin. Other calpain family members (calpain 94, ncl2, ncl3, etc) have more limited tissue distribution, and perhaps different functions. The calpain family members consist of a common small subunit (Calpain 4), and a large variable subunit. It is not clear that all calpains contain a small subunit. Domains in the large subunit include the amino terminal domain I, the proteinase domain II, domain III, and the EF hand domain IV. The calpains appear to serve multiple physiological roles, and ideas concerning the functions of these enzymes are in a state of rapid flux.
Subcellular location: Cytoplasm, Cell membrane
Synonyms: Calcium activated neutral proteinase 2, Calcium activated neutral proteinase, CALP80, Calpain 2 m/II large subunit, Calpain 2 catalytic subunit, Calpain 2 large catalytic subunit, Calpain 2 large subunit, Calpain large polypeptide L2, Calpain M type, Calcium-activated neutral proteinase 2, CALP80, Calpain 2, large [catalytic] subunit, Calpain M-type, Calpain-2 catalytic subunit, Calpain-2 large subunit, CAN2_MOUSE, M-calpain, Millimolar-calpain, Calpain2, CANP 2, CANP L2, CANP2, CANPL 2, CANPL2, CANPml, Capa2, CAPN 2, CAPN2, FLJ39928, M calpain, M calpin, M type, mCANP, Millimolar calpain.
Target Information: Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction (By similarity)