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Gene Review

CAPN2  -  calpain 2, (m/II) large subunit

Bos taurus

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Disease relevance of CAPN2

  • Autolysis removes the N-terminal 19 (m-calpain) or 27 (mu-calpain) amino acids from the large subunit and approximately 90 amino acids from the N-terminus of the small subunit [1].

High impact information on CAPN2

  • CANP1 was maximally active at 700 microM while CANP2 exhibited highest activity at 2 microM CaCl2 [2].
  • For example, little cleavage of the 68 kDa protein by CANP2 and CANP3 was noted whereas 210 kDa and 150 kDa proteins remained largely intact [3].
  • Two forms ( CANP1 and CANP2 ) of a calcium activated neutral protease (CANP) have been purified to near homogeneity from calf brain synaptosomes and spinal cord [4].


  1. Effects of autolysis on properties of mu- and m-calpain. Li, H., Thompson, V.F., Goll, D.E. Biochim. Biophys. Acta (2004) [Pubmed]
  2. Purification and characterization of two forms of Ca2+-activated neutral protease from calf brain. Malik, M.N., Fenko, M.D., Iqbal, K., Wisniewski, H.M. J. Biol. Chem. (1983) [Pubmed]
  3. Purification and degradation of purified neurofilament proteins by the brain calcium-activated neutral proteases. Malik, M.N., Sheikh, A.M., Fenko, M.D., Wisniewski, H.M. Life Sci. (1986) [Pubmed]
  4. Purification and partial characterization of two forms of Ca2+-activated neutral protease from calf brain synaptosomes and spinal cord. Malik, M.N., Fenko, M.D., Wisniewski, H.M. Neurochem. Res. (1984) [Pubmed]
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