p-CaM I Anticuerpo(Thr 79): sc-17018

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The level of intracellular calcium is tightly regulated in all eukaryotic cells. A modest increase in the calcium level can results in a myriad of physiological response, most of which are mediated by calmodulin. Calmodulin (CaM), a 148-amino acid universal calcium sensor, directly modulates the activity of protein kinases and phosphatases, ion channels and nitric oxide synthetases (1–5). Approximately 15% of CaM in the cell is phosphorylated and this phosphorylation is mediated by casein kinase II on Thr-79, Ser-81, Ser-101 and Thr-117. Although CaM is constitutively phosphorylated, insulin increases phosphate incorporation into serine, threonine and tyrosine residues in intact cells (6–8). Phosphocalmodulin (p-CaM) exhibits altered biological activity. For example, p-CaM reduces activation of the erythrocyte plasma membrane Ca2+ pump (6). This strongly suggests that phospho-rylation of CaM is an important component of intracellular signaling (8).