p-NOS3 (T494) pAb

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h3 class=list6_t1Product/h3
p class=list6_text1 mg/ml in Phosphate buffered saline (PBS) with 15 mM sodium azide, approx. pH 7.2./p
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h3 class=list6_t1Purification amp; Purity/h3
p class=list6_textThe antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is gt; 95% (by SDS-PAGE)./p
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h3 class=list6_t1Specificity/h3
p class=list6_textp-NOS3 (T494) antibody detects endogenous levels of p-NOS3 protein./p
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h3 class=list6_t1Applications (Recommended Dilutions)/h3
p class=list6_textWB: 1:500~1:1000/p
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h3Western Blot(WB)/h3
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div style=width: 250pxWestern blot (WB) analyzes of p-NOS3 (T494) antibody in extracts from HepG2 cells./div
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h3 class=list6_t1Storageamp;Stability/h3
p class=list6_textStore at 4/p
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h3 class=list6_t1Background/h3
p class=list6_textNitric oxide (NO), produced by the endothelial NO synthase (NOS3), is a fundamental determinant of cardiovascular homeostasis that maintains system blood pressure, vascular remodeling and angiogenesis. NOS3 is stimulated, in a phosphatidylinositol 3-kinase (PI 3-kinase)-dependent fashion, by treatment of endothelial cells with insulin-like growth factor-1 and vascular endothelial growth factor (VEGF). The serine/threonine protein kinase Akt/PKB is an important downstream target of PI 3-kinase, regulating VEGF-stimulated endothelial cell survival. NOS3 activation via phosphorylation of Serine 1177 by Akt/PKB is necessary and sufficient for VEGF-mediated endothelial cell migration. Therfore, Akt/PKB can directly phosphorylate NOS3 on Serine 1177, activating the enzyme and leading to NO production./p
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