eNOS (49G3) Rabbit mAb

Endothelial nitric-oxide synthase (eNOS) is an important enzyme in the cardiovascular system. It catalyzes the production of nitric oxide (NO), a key regulator of blood pressure, vascular remodeling, and angiogenesis (1,2). The activity of eNOS is regulated by phosphorylation at multiple sites. The two most thoroughly studied sites are the activation site Ser1177 and the inhibitory site Thr495 (3). Several protein kinases including Akt/PKB, PKA, and AMPK activate eNOS by phosphorylating Ser1177 in response to various stimuli (4,5). In contrast, bradykinin and H2O2 activate eNOS activity by promoting both Ser1177 phosphorylation and Thr495 dephosphorylation (6,7). 1.Fulton, D. et al. (2001) J Pharmacol Exp Ther 299, 818-24. 2.Shaul, P.W. (2002) Annu Rev Physiol 64, 749-74. 3.Chen, Z.P. et al. (1999) FEBS Lett 443, 285-9. 4.Dimmeler, S. et al. (1999) Nature 399, 601-5. 5.Fulton, D. et al. (1999) Nature 399, 597-601. 6.Harris, M.B. et al. (2001) J Biol Chem 276, 16587-91. 7.Thomas, S.R. et al. (2002) J Biol Chem 277, 6017-24.