Calpain-13 is an intracellular, calcium-dependent cysteine protease. Calpain-13 was first described in human EST databases, and maps to mouse chromosome 2. Three sequences have been reported thus far; the 669 amino acid sequence predicts a protein of 76.726 kD, and the truncated 561, 423 amino acid sequences predict proteins of 63.94 and 48.032 kD respectively. The different isoforms differ in the carboxyterminal ends, ending with aberrant domain-III and lacking domain IV. Calpain-13 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-13 closest to calpain-14, also found on chromosome 2. RP1Calpain-13 recognizes latent but not the aminotruncated (active) Calpain-13. All three forms of calpain-13 are recognized by RP1Calpain-13. 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. RP1Calpain-13 Anti Calpain-13 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. RP1Calpain-13 will also bind to the non-reduced protein, and thus has application for immunoprecipitation, immunohistochemistry, and ELISA. Not all cell types produce Calpain-13; since it is a cellular protein, cell lysate works well for Western blots. Rat, mouse and human Calpain-13 are detected with RP1Calpain-13. 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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