Calmodulin from bovine testes

Research area: Cell Signaling

Calmodulin (CaM) is a Ca²⁺-sensor protein containing four EF-hand motifs that bind to four Ca²⁺ ions. It is found ubiquitously in all eukaryotes.

Calmodulin from bovine testes has been used:

• as a component of the reaction mixture in PhosphoSens assay to measure Ca²⁺/calmodulin-dependent protein kinase II α (CaMKIIα) substrate phosphorylation
• to generate standard curve for the determination of in situ calmodulin concentration in tissues
• as a ligand in radio-ligand binding for studying calmodulin affinity

Calmodulin (CaM) aids in the Ca²⁺ signal transduction pathway in higher plants and animals. Ca²⁺ binding is required for CaM activation. Upon activation, CaM binds and activates numerous target proteins involved in a variety of cellular processes including regulation of plant metabolism, phytohormone signaling, ion transport, protein folding, protein phosphorylation and dephosphorylation, cell motility, exocytosis, and cytoskeletal assembly. In neurons, calcium-activated CaM helps in the regulation of glutamate receptors, modulation of proteins in signaling pathways, and regulation of voltage-gated calcium channels (VGCCs) activity.

Ca²⁺ 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.