eNOS (pS1177), Phospho-Specific Mouse anti-Human, Unlabeled, Clone: 19, BD

Nitric 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 cytotoxity. 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 and Ser-1177 are phosphorylated by PKA and PKG in vitro. Thus, eNOS activity may be regulated through complex phosphorylated events mediated by multiple kinases at various phosphorylation sites. Human endothelial cells are routinely tested as a positive control for eNOS (pS1177) mAb. 100% homology is detected for immunogen sequence in human, mouse, rat, dog and bovine. Cross-reactivity with other species is expected but not confirmed.

Flow Cytometry, Western Blotting