The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Use at an assay dependent dilution. Predicted molecular weight: 93 kDa.
Use at an assay dependent dilution.
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.