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. RP2Calpain-7 recognizes both latent and amino-processed Calpain-7; the latent large subunit is 93 Kd, and the amino terminal truncation at activation yields an approximately 58 Kd form. Cleavage of the carboxyterminal region generates smaller forms of Calpain-7, but it is not clear if these forms are proteolytically active. RP2Calpain-7 works well for Western Blotting applications, and when used against the reduced protein identifies bands at 93 Kd, 68 Kd, and a series of further cleaved forms. RP2Calpain-7 will also bind to the non-reduced protein, and thus has application for immunoprecipitation, immunohistochemistry, and ELISA. Rat, mouse and human Calpain-7 are detected with RP2Calpain-7. A recommended starting concentration for Western blots is 1:1000 when using colorimetric substrates such as BCIP/NBT, and 1:5000 for chemiluminescent substrates. Higher concentrations of antibody may be needed for samples from more distantly related species

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