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

μ-calpain from bovine skeletal muscle.

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.

Solution in phosphate buffered saline and contains 0.05% sodium azide

ascites fluid

2H2A7C2

buffered aqueous solution

antigen mol wt 80 kDa

human, bovine, rat, pig

immunoblotting: 1:1,000

indirect immunofluorescence: 1:25

IgG1

human ... CAPN1(823)

rat ... Capn1(29153)

dry ice

−20°C

Neumar, R.W., et al., Brain μ-calpain autolysis during global cerebral ischemia. J. Neurochem. 66, 421-424, (1996) abstract

Ravid, A., et al., 1,25-Dihydroxyvitamin D₃ increases the cellular content of the calcium-activated neutral protease mu-calpain in renal cell carcinoma. Endocrinology 135, 2822-2825, (1994) abstract

Lane, R.D., et al., A comparison of the intracellular distribution of μ-calpain m-calpain and calpastatin in proliferating human A431 cells. Exp. Cell Res. 203, 5-16, (1992) abstract

Glaser, T., et al., Calpain (Ca²⁺-dependent thiol protease) in erythrocytes of young and old individuals. Proc. Natl. Acad. Sci. USA 91, 7879-7883, (1994) abstract

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