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Protease Assays

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Calpain Assays
 
Calpains belong to a family of calcium-dependent thiol-proteases that proteolyze a wide variety of cytoskeletal, membrane-associated, and regulatory proteins. Fifteen gene products of the calpain family are reported in mammals, which are classified as nine typical and six atypical calpains. Typical calpains are characterized by a C-terminal Ca2+-binding domain that includes EF-hand motifs, while atypical calpains lack this region, but often contain additional domains. Calpains do not generally function as destructive proteases, but act as calcium-dependent modulators that remove limited portions of protein substrates. Calpains respond to Ca2+ signals by cleaving specific proteins, frequently components of signaling cascades, thereby irreversibly modifying their function. Two major isoforms of calpain are reported in mammals, calpain 1 (m-form) and calpain 2 (m-form). They are constitutively expressed in all tissues and differ in their calcium requirement for activation (~50 mM for calpain 1 and ~500 mM for calpain 2) and contain several calcium-binding sites, which allosterically affect the enzyme activity.
 
 
Related Resource
Calpain Overview and Products