Calmodulin (CaM) is a ubiquitous, calcium-binding protein. CaM is expressed in many cell types and can have different subcellular locations, including the cytoplasm, within organelles, or associated with the plasma or organelle membranes. Many of the proteins that CaM binds are unable to bind calcium themselves, and as such use CaM as a calcium sensor and signal transducer. CaM can also make use of the calcium stores in the endoplasmic reticulum, and the sarcoplasmic reticulum. CaM undergoes a conformational change upon binding to calcium, which enables it to bind to specific proteins for a specific response.
Synonyms: CALM; CAM
Purity: >=95% (SDS-PAGE)
Application: Calmodulin from bovine brain has been used to study calmodulin-associated endothelium-derived relaxing factor/nitric oxide synthase activity in the particulate and cytosolic fractions of bovine aortic endothelial cells. It has also been used as a standard in size-exclusion chromatography.
Biochem Physiol Actions: Calmodulin (CaM) can bind to and regulate a multitude of different protein targets, thereby affecting many different cellular functions. It is involved in inflammation, metabolism, apoptosis, muscle contraction, intracellular movement, short-term and long-term memory, nerve growth and the immune response. CaM can bind up to four calcium ions, and can undergo post-translational modifications, such as phosphorylation, acetylation, methylation and proteolytic cleavage, each of which can potentially modulate its actions.