Clone: 28F3.
Background: The calpains are calcium-dependent cysteine proteases that are widely expressed in mammalian systems. Both m-calpain (calpain II) and µ-calpain (calpain I) are composed of an 80 kD subunit and a 30 kD subunit. Whereas the 30 kDa subunit is shared by both enzymes, the larger catalytic subunits are different and exhibit the distinct Ca ++ requirements that are suggested by their names. Whereas m-calpain requires millimolar (mM) levels of calcium, µ-calpain is active at micromolar (µM) concentrations of Ca ++. In addition to the ubiquitously expressed m- and µcalpains, some tissue-specific calpains have been identified. The calpains appear to serve multiple physiological roles, and ideas concerning the functions of these enzymes are in a state of rapid flux.
Purification Method: Protein A/G Chromatography.
Source: Hybridoma produced by the fusion of splenocytes from mice immunized with human calpain with mouse myeloma.
References: 1. Adamec, E., et al. 'Calpain I activation in rat hippocampal neurons in culture is NMDA receptor selective and not essential for excitotoxic cell death.' Brain Res. Mol. Brain Res. 1998, 54, 35-48
2. Guttmann, R.P. et al. 'Oxidation inhibits substrate proteolysis by calpain I but not autolysis.' J. Biol. Chem. 1997, 272, 2005-2012.
UniProt: P17655.
Caution: This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals.
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