Calpain-15 is an intracellular, calcium-dependent cysteine protease. Calpain-15 was first described as the human homologue of SOL, the small optic lobe protein, a drosophila protein. The calpain-15 sequence is very different from the classical calpains, and has a much longer aminoterminal end. In fact, about the only similarity between SOLH and the classical calpains is the catalytic residues, CHN, which are all conserved in calpain-15. Sequence alignments place Calpain-15 closest to calpain-7. The calpain-15 sequence is a whopping 1086 amino acids long, predicting a protein of 117.313 kD, much larger that other calpain family members (almost all of the difference is in the amino end). RP1Calpain-15 recognizes latent but not the aminotruncated (active) Calpain-15. RP1Calpain-15 Anti Calpain-15 works well for Western Blotting applications, and when used against the reduced protein identifies bands at 115 kD (minor band), and a series of further cleaved forms. RP1Calpain-15 will also bind to the non-reduced protein, and thus has application for immunoprecipitation, immunohistochemistry, and ELISA. Not all cell types produce Calpain-15; since it is a cellular protein, cell lysate works well for Western blots. Rat, mouse and human Calpain-15 are detected with RP1Calpain-15. 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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