Calpastatin is an endogenous protease inhibitor that acts specifically on calpain (a calcium-dependent cysteine protease). It consists of four repetitive sequences comprising of 120 to 140 amino acid residues, and an N-terminal non-homologous sequence(L). This product is obtained from highly purified domain I of human calpastatin, comprising of 135 amino acids (MW 14,000), which is produced by genetic recombination technique.
Homogeneous on SDS-polyacrylamide gel electrophoresis. Greater than 90% pure as determined by amino acid composition analysis.
Storage
–20°C
Properties
Molecular weight: 14 kDa
Peptide length: 137 aa
Typical activity: 50 nM of calpastatin domain I completely inhibits the activity of 7.5 µg/ml calpain I. 15 nM of calpastatin domain I inhibits 50% of the activity of 7.5 µg/ml calpain I.
Asada, K. et al. cDNA cloning of human calpastatin: sequence homology among human, pig, and rabbit calpastatins. J. Enz. Inhib.3:49 (1989).
Kanaki, R. and Murachi, T. Physiological significance of the calpain-calpastatin system. Protein, Nucleic Acid and Enzyme32:116 (Japanese Journal) (1987).
Uemori, T. et al. Characterization of a functional domain of human calpastatin. Biochem. Biophys. Res. Comm. 166:1485 (1990).
Calpastatin is an endogenous protease inhibitor that acts specifically on calpain (a calcium-dependent cysteine protease). It consists of four repetitive sequences comprising of 120 to 140 amino acid residues, and an N-terminal non-homologous sequence(L). This product is obtained from highly purified domain I of human calpastatin, comprising of 135 amino acids (MW 14,000), which is produced by genetic recombination technique.
Homogeneous on SDS-polyacrylamide gel electrophoresis. Greater than 90% pure as determined by amino acid composition analysis.
Storage
–20°C
Properties
Molecular weight: 14 kDa
Peptide length: 137 aa
Typical activity: 50 nM of calpastatin domain I completely inhibits the activity of 7.5 µg/ml calpain I. 15 nM of calpastatin domain I inhibits 50% of the activity of 7.5 µg/ml calpain I.
Asada, K. et al. cDNA cloning of human calpastatin: sequence homology among human, pig, and rabbit calpastatins. J. Enz. Inhib.3:49 (1989).
Kanaki, R. and Murachi, T. Physiological significance of the calpain-calpastatin system. Protein, Nucleic Acid and Enzyme32:116 (Japanese Journal) (1987).
Uemori, T. et al. Characterization of a functional domain of human calpastatin. Biochem. Biophys. Res. Comm. 166:1485 (1990).
