|Calculated MW||79995 Da|
|Other Names||Calpain-2 catalytic subunit, Calcium-activated neutral proteinase 2, CANP 2, Calpain M-type, Calpain large polypeptide L2, Calpain-2 large subunit, Millimolar-calpain, M-calpain, CAPN2, CANPL2|
|Target/Specificity||A synthetic peptide corresponding to residues within human calpain 2 was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Calpain-2 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves MYOC at 'Arg-226' (PubMed:17650508).|
|Cellular Location||Cytoplasm. Cell membrane. Note=Translocates to the plasma membrane upon Ca(2+) binding|
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Provided below are standard protocols that you may find useful for product applications.
The calcium-activated protease calpain cleaves a variety of biologically important proteins and serves, therefore, as a key regulator of many cellular functions. Activation of both main isoforms, calpain 1 and calpain 2, was demonstrated previously in Alzheimer's disease. Calpain 2 could be directly involved in tau hyperphosphorylation by modulating protein kinase activities. Results provide evidence of the important role of the calpain proteolytic system in the pathogenesis of neurodegenerative diseases with tau neurofibrillary pathology (1). Calpain is intimately involved in modulating cell adhesion and migration. The two ubiquitous isoforms of this protease, calpain I and II, are considered to be cytosolic proteins that can translocate to both focal complexes/adhesions or the plasma membrane. results reveal an increased association of calpain I, II, calpastatin, and the 30kDa regulatory subunit with the endoplasmic reticulum and Golgi apparatus as evidenced by their position in the gradient relative to calnexin, Rab6, caveolin, and beta1 integrin after laminin stimulation. Further experiments established that calpain II colocalizes with phosphatidylinositol 4,5-bisphosphate. (2)
1. Adamec E et al. Acta Neuropathol 104(1):92-104, 202
2. Hood JL, et al. Biohem Biophys Res Commun 310(4):1200-12, 2003
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