recommended for detection of Ser 101 phosphorylated CaM I of mouse, rat and human origin by WB, IF and ELISA; also reactive with additional species, including equine, canine, bovine, porcine and avian
CaM I Background Information The level of intracellular calcium is tightly regulated in all eukaryotic cells.
A modest increase in the calcium level can result in a myriad of physiological responses, 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. Approximately 15% of CaM in the cell is phosphorylated and this phospho-rylation 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. Phosphocalmodulin (p-CaM) exhibits altered biological activity. For example, p-CaM reduces activation of the erythrocyte plasma membrane Ca2+ pump. This strongly suggests that phosphorylation of CaM is an important component of intracellular signaling.
