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

Description

• 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 Ca 2+ ; 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