P1431

Calmodulin exists as a long dumbbell shaped molecule. Each globular end contains two calcium binding domains. Upon binding calcium, calmodulin undergoes a conformational change in which the hydrophobic regions become exposed. These hydrophobic regions are believed to be involved with enzyme binding.

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P1431

Sigma

 

Calmodulin from bovine testes

BioUltra, ≥98% (SDS-PAGE), lyophilized powder, ≥40,000 units/mg protein (Lowry)

Synonym:CaM, Phosphodiesterase 3′:5′-cyclic nucleotide activator
CAS Number:77107-46-1
MDL number:MFCD00131869

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Description

Biochem/physiol ActionsCa2+ binding protein that is required for activation of cyclic nucleotide-dependent phosphodiesterase. It is also a cofactor/activator of nitric oxide synthase, calcineurin, and many kinases including ATPase, myosin light chain kinase, and CAM kinase I, II, and III. It mediates ryanodine receptor activation by cyclic ADP ribose and is involved in intracellular Ca2+ homeostasis.
Unit DefinitionOne unit will stimulate 0.008 activated unit of phosphodiesterase, 3′:5′-cyclic nucleotide in a 3 mL reaction volume at pH 7.5 and 30 °C, to 50% of the maximum activity of the enzyme when saturated with activator, in the presence of 0.01 mM Ca2+.

Properties

gradeBioUltra
assay≥98% (SDS-PAGE)
formlyophilized powder
total impurities salt, essentially free
storage temp.−20°C

Safety

Personal Protective EquipmentEyeshields, Gloves, type N95 (US), type P1 (EN143) respirator filter
WGK Germany3

References

referenceWatterson, D.M., The complete amino acid sequence of the Ca2+-dependent modulator protein (calmodulin) of bovine brain. J. Biol. Chem. 255, 962, (1980)
 Beavo, J.A., Cyclic nucleotide phosphodiesterases: functional implications of multiple isoforms. Physiol. Rev. 75, 725-748, (1995)
 Cheung, W.Y., Calmodulin plays a pivotal role in cellular regulation. Science 207, 19-27, (1980)
 Bredt, D., and Snyder, S.H., Isolation of nitric oxide synthetase, a calmodulin-requiring enzyme. Proc. Natl. Acad. Sci. U. S. A. 87, 682, (1990)
 Klee, C.B., Isolation and characterization of bovine brain calcineurin: a calmodulin-stimulated protein phosphatase. Meth. Enzymol. 102, 227, (1983)
 Carafoli, E., Biogenesis: plasma membrane calcium ATPase: 15 years of work on the purified enzyme. FASEB J. 8, 993, (1994)
 Stull, J.T., Ca2+/calmodulin-dependent myosin light-chain kinases. Adv. Second Messenger Phosphoprotein Res. 31, 141, (1997)
 Nairn, A.C., and Picciotto, M.R., Calcium/calmodulin-dependent protein kinases. Semin. Cancer Biol. 5, 295, (1994)
 Lee, H.C., Sensitization of calcium-induced calcium release by cyclic ADP-ribose and calmodulin. J. Biol. Chem. 270, 9060, (1995)