Human calpain 1 has been used in a study to assess how the crystal structures of human calpains 1 and 9 imply diverse mechanisms of action and auto-inhibition. Human calpain 1 has also been used in a study to investigate the synthesis, biological evaluation and molecular modelling of N-heterocyclic dipeptide aldehydes as selective calpain inhibitors.
Biochem/physiol Actions
Caplain 1 is a neutral calcium-dependent cysteine protease containing the EF-hand motif. The protease consists of two subunits; the larger subunit has four domains that are homologous with papain and calmodulin. The smaller subunit has one domain that shares homology with calmodulin. It is activated by micromolar levels of calcium and hence, it is also called as micro-calpain. Its activation leads to cellular protein degradation, neuronal cell degeneration, and autoimmune demyelinating diseases such as multiple sclerosis.
Cytosolic protease with involvement in cytoskeletal remodeling, autophagy, and apoptosis as an upstream regulator.
Physical properties
Calpain 1 is a heterodimeric calcium-activated thiol-protease.
Unit Definition
One unit will hydrolyze 1 picomole Suc-LLVY-AMC per minute at 25 deg C.
Physical form
Solution in 20 mM Imidazole-HCl, 5 mM β-Mercaptoethanol, 1 mM EDTA, 1 mM EGTA, and 30% glycerol.
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