Calpain-94, also known as Calpain-3 or Muscle Calpain, is an intracellular, calcium-dependent cysteine protease. The calpains have papain-like activity, thus the -pain nomenclature. The calpain family members consist of a common small subunit, and a large variable subunit. Domains in the large subunit include the amino terminal domain-I, the proteinase domain-II, domain-III, and the EF-hand domain-IV. Unlike M-calpain and m-calpain, which are ubiquitously expressed, Calpain-94 is a member of the tissue-specific Calpains. Unlike the other calpains, the endogenous calpain inhibitor, calpastatin, does not seem to inhibit Calpian-94. The half-life of native Calpain-94 is also much shorter; about 10 minutes. Mutations in Calpain-94 have been linked to Limb-Girdle Muscular Distrophy, and native Calpain-94 is known to act as a meat tenderizer. RP1Calpain-3 recognizes latent and active Calpain-94. The latent large subunit is 94 kD, and the amino terminal truncation at activation yields an approximately 64- 62 Kd form. A cascade of smaller forms can be seen with further activation. RP1Calpain-3 works well for Western Blotting applications, and when used against the reduced protein identifies bands at 94 Kd, 82 Kd, 62 Kd, 60 Kd, and a series of further cleaved active forms. RP1Calpain-94 will also bind to the non-reduced protein, and thus has application for immunoprecipitation, immunohistochemistry, and ELISA. Calpain-94 is a cellular protein, thus cell lysates work well for Western blots. 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. EDTA/EGTA treatment of tissues or lysates is required to see latent zymogen.

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