Calpain 7 Rabbit anti-Human, Mouse, Rat, Polyclonal, Proteintech

Calpain proteinases are defined currently as papain-like neutral proteases that are calcium activated. Calpains 1 and 2 are composed of a large subunit, which is proteolytically active, and a small subunit (also called calpain-4), or enhancer protein, that is not proteolytically active. The other calpain proteins identified to date (calpain 5, 6, 8, 9, 10, 11, 12, 13, 14, 15) are not known to require 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 (domain-T in calpains 5 & 6, domain-N for calpain-7). Calpain-7 domain-N does not have the standard calpain EF hand domain for binding calcium, making it unclear whether it is calcium regulated. In place of the EF hand calcium-binding domain IV, calpain-7 has a sequence most closely resembling domain-III, with unknown function. Calpain-7 is widely distributed, found in most tissues analyzed.