Calpain-12 is an intracellular, calcium-dependent cysteine protease. Calpain-12 was first described in the mouse, most strongly in the skin, and maps to mouse chromosome 7. The 720 amino acid sequence predicts a protein of 80.588 kD, and the truncated 502, 462 and 449 amino acid sequences predict proteins of 55.874, 51.492 and 50.397 kD respectively. The different isoforms differ in the carboxyterminal ends, ending with aberrant domain-III and lacking domain IV. Domains in the large subunit include the amino terminal domain-I, the proteinase domain-II, domain-III, and the EF-hand domain-IV, making Calpain-12 most similar to the “classical” calpains 1 & 2. Sequence alignments place Calpain-12 closest to chicken calpain u/m, and it may be that Calpain-12 is the human orthologue of this protein. RP2Calpain-12 recognizes latent and the aminotruncated (active) Calpain-12, and recognizes all but the shortest (449 AA) form of calpain-12. The latent large subunit migrates at about 80 kD on reduced SDS PAGE gels, and truncation at the amino terminal end yields an approximately 58 kD form. A cascade of smaller forms can be seen with further activation. RP2Calpain-12 Anti Calpain-12 works well for Western Blotting applications, and when used against the reduced protein identifies bands at 80 kD, and a series of further cleaved forms. RP2Calpain-12 will also bind to the non-reduced protein, and thus has application for immunoprecipitation, immunohistochemistry, and ELISA. Not all cell types produce Calpain-12; since it is a cellular protein, cell lysate works well for Western blots. Rat, mouse and human Calpain-12 are detected with RP2Calpain-12. 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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