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Calpain, an intracellular calcium-dependent protease that cleaves cytoskeletal and submembranous proteins, plays a role in cytoskeletal reorganization and muscle protein degradation. Calpain is a heterodimer composed of a small regulatory subunit and one of three large catalytic subunits, designated calpain 1, calpain 2 and calpain 3. Calpain 3 (calpain p94) is a muscle-preferred calcium activated neutral protease that localizes to the nucleus. Mutations involving the calpain 3 gene are associated with limb-girdle muscle dystrophy type 2A, a form of autosomal recessive and progressive neuromuscular diso4. Calpastatin regulates calpain by inhibiting both the proteolytic activity of calpain and its binding to membranes. Calpastatin exists in two types, tissue type and erythrocyte type, resulting from both alternative splicing and proteolytic processing.
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Protein Aliases: Calcium-activated neutral proteinase 3; calpain 3, (p94); Calpain L3; Calpain p94; calpain p94, large [catalytic] subunit; calpain, large polypeptide L3; Calpain-3; CANP 3; CAPN 3; LGMD 2A; MGC10767; MGC11121; MGC14344; MGC4403; Muscle-specific calcium-activated neutral protease 3; muscle-specific calcium-activated neutral protease 3 large subunit; nCL-1; New calpain 1; skeletal muscle specific calpain p94
Gene Aliases: AI323605; CANP3; CANPL3; Capa-3; Capa3; CAPN3; LGMD2; LGMD2A; Lp82; Lp84; Lp85; nCL-1; NCL1; p94
Molecular Function: cysteine protease