Enos (Ps633) Mouse Anti-Human, Unlabeled, Clone: 37, Bd, Mouse Monoclonal Antibody, Each

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Nitirc oxide synthase (nos), a cell type specific enzyme, catalyzes the synthesis of nitric oxide (no). No is a short-lived radical that transmits signals involved in vasorelaxation, neurotransmission, and cytoxicity. In neurons and endothelial cells, constitutive nos (cnos) is activated by agonists that increase intracellular ca2+; levels and enhance calmodulin binding. Neuronal nos (nnos) and endothelial nos (enos) have recognition sites for nadph, fad, fmn, and calmodulin. Enos has a unique n-myristylation consensus sequence that may explain its membrane localization. Various protein kinases have been implicated in regulation of enos activity, including ampk, pka, pkb/akt, pkc, and cam kinase ii. During vegf stimulation, enos is transiently phosphorylated at ser-1177 by pkb/akt and dephosphorylated at thr-495. At later time points, vegf stimulation leads to an increase in thr-495 phosphorylation mediated by pkc and a decrease in ser-1177 phosphorylation. In addition, ser-633 amd ser-1177 are phosphorylated by pka and pkg in vitro. Thus, enos activity may be regulated through complex phosphorylation events mediated by multiple kinases at various phosphorylation sites.Western blotting