Calpain-14 is an intracellular, calcium-dependent cysteine protease. Calpain-14 was first described in human EST databases, and maps to mouse chromosome 2. The 663 amino acid sequence predicts a protein of 76.749 kD, with an isoelectric point of 8.587, much more basic than the acidic isoelectric points of the "classical" calpains. Calpain-14 looks similar to the other calpain members in domains I and II, but domain-III lacks the polyglutamic acid stretch that aids in calcium binding, and domain-IV is very different. Sequence alignments place calpain-14 closest to calpain-13, also found on chromosome 2. RP2Calpain-14 recognizes latent and aminotruncated (active) calpain-14. The latent large subunit migrates at about 76 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-14 Anti calpain-14 works well for Western Blotting applications, and when used against the reduced protein identifies bands at 76 kD, and a series of further cleaved forms. RP2calpain-14 will also bind to the non-reduced protein, and thus has application for immunoprecipitation, immunohistochemistry, and ELISA. Not all cell types produce calpain-14; since it is a cellular protein, cell lysate works well for Western blots. Rat, mouse and human calpain-14 are detected with RP2calpain-14. 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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