Not available outside of the UK & Ireland.

Application

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

Cytosolic protease with involvement in cytoskeletal remodeling, autophagy, and apoptosis as an upstream regulator.

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.

Physical form

Solution in 20 mM Imidazole-HCl, 5 mM β-Mercaptoethanol, 1 mM EDTA, 1 mM EGTA, and 30% glycerol.

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.