goat polyclonal IgG, 200 µg/ml; also available as rabbit IgG, 200 µg/ml, sc-17018-R
epitope corresponding to a short amino acid sequence containing phosphorylated Thr 79 of calmodulin (Cam I) of human origin
recommended for detection of Thr 79 phosphorylated calmodulin of mouse, rat and human origin by WB and IF; 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 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).
