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  • C267 - Monoclonal Anti-μ-Calpain (Domain II) antibody produced in mouse

C267 Sigma

Monoclonal Anti-μ-Calpain (Domain II) antibody produced in mouse

clone 2H2A7C2, ascites fluid



Related Categories Alphabetical Index, Antibodies, Antibodies for Cell Biology, Antibodies for Intracellular Calcium Signaling, Antibodies to Calcium-Associated Proteins,
species reactivity   pig, bovine, human, rat
application(s)   indirect immunofluorescence: 1:25
  western blot: 1:1,000
clone   2H2A7C2, monoclonal
antibody form   ascites fluid
isotype   IgG1
mol wt   antigen mol wt 80 kDa
shipped in   dry ice
storage temp.   −20°C
Gene Information   human ... CAPN1(823)
rat ... Capn1(29153)
biological source   mouse
conjugate   unconjugated



μ-calpain from bovine skeletal muscle.

General description

Calpain-1 catalytic subunit is a protein encoded by the CAPN1 gene in humans. Calpains are calcium dependent proteases constituting a family of proteins. They share a homologous cysteine-protease domain and an E-F hand Ca2+-binding domain. The calpain system consists of two ubiquitous forms of calpain (m-calpain and μ-calpain), a tissue specific calpain (n-calpain) and a calpain inhibitory protein (calpastatin).

Physical form

Solution containing 0.05% sodium azide


Epitope mapping studies indicate the epitope is between amino acids 245-265 (domain II) of human μ-calpain. The antibody reacts specifically with μ-calpain. It does not cross-react with m-calpain, n-calpain, calmodulin or calpastatin. It is not recommended for immunoprecipitation. By immunoblotting, reactivity is observed with human platelets and erythrocytes, bovine platelets, heart and skeletal muscle and with rat myoblasts, kidney, liver and spleen. By immunofluorescence on pig LLC-PK1 cells, diffuse cytoplasmic staining is observed.


Monoclonal Anti-μ-Calpain (Domain II) antibody produced in mouse is suitable for indirect immunofluorescence at a dilution of 1:25 and western blotting at a dilution of 1:1000.

Biochem/physiol Actions

Calpain is involved in calmodulin-independent pathway for the activation of calcineurin. Endogenous calpain I forms active calcineurin in the human heart by proteolysis of calcineurin A, which may lead to pathogenesis of myocardial disease. μ-calpain, on overexpression, may have relationship with intractable epilepsy as well as the clinicopathological characteristics in such patients. Its activity may increase in skeletal muscle of gastric cancer patients.

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