This Antibody was verified by KnockDown to ensure that the antibody binds to the antigen stated. View Details
MA3-940 detects mu-calpain from human platelets and erythrocytes, bovine platelets, heart and skeletal muscle, rat myoblasts, kidney, liver and spleen, mouse lung, pig cultured cells and hamster and rabbit samples. This antibody does not cross-react with m-calpain, n-calpain, calmodulin or calpastatin.
MA3-940 has been successfully used in Western blot, immunofluorescence, immunohistochemistry, and immunocytochemistry procedures. By Western blot, this antibody detects an 80 kDa protein representing mu-calpain from human platelets and erythrocytes and HeLa and A431 cell lysates. Immunocytochemical staining of mu-calpain in LLC-PK1 cells with MA3-940 results in diffuse cytoplasmic staining. This product has not been shown to be effective in immunoprecipitation experiments.
The MA3-940 antigen is purified bovine skeletal muscle 80 kDa mu-calpain subunit. This antibody recognizes an epitope between amino acids 465-520 (domain III) of human mu-calpain.
The calpain (calcium-dependent protease or calcium-activated neutral protease) system consists of two ubiquitous forms of calpain (mu-calpain and m-calpain), a tissue specific calpain (n-calpain), and a calpain inhibitory protein (calpastatin). The calpain system has been detected in every vertebrate tissue examined, and has been suggested to play a regulatory role in cellular protein metabolism. This regulatory role may have important implications in platelet aggregation and pathologies associated with altered calcium homeostasis and protein metabolism such as ischemic cell injury and degenerative diseases. Inhibitors of calpain have been shown to block dexamethasone and low-level irradiation induced apoptosis in thymocytes suggesting that calpain has a regulatory or mechanistic role in apoptotic cell death.
Mu-Calpain, also known as Calpain-I, and m-calpain, also known as Calpain-II, are intracellular, calcium-dependent cysteine proteases.
Mu- and m-calpains are heterodimers consisting of 28 kDa and 80 kDa subunits. The 28 kDa subunit is identical in the two isoforms, but the 80 kDa subunits differ with ~50% sequence similarity. 28 kDa/80 kDa complexes are thought to be inactive proenzymes which, upon binding of calcium, undergo conformational changes that promotes cleavage of the 28 kDa subunit and results in enzyme activation.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: Calcium-activated neutral proteinase 1; calpain 1, (mu/I) large subunit; calpain 1, large subunit; Calpain mu-type; calpain, large polypeptide L1; Calpain-1 catalytic subunit; Calpain-1 large subunit; Calpain-I; CaNP; CANP 1; Cell proliferation-inducing gene 30 protein; cell proliferation-inducing protein 30; micromolar calcium activated neutral protease 1; micromolar calcium-activated neutral protease 1; Micromolar-calpain; mu-calpain; muCANP
Gene Aliases: BOS_24946; CANP; CANP1; CANPL1; Capa-1; Capa1; CAPN1; Cls1; I79_024883; mu-calpin; muCANP; muCL; PIG30; SPG76