Nitric Oxide Synthase 3 (Endothelial Cell) (NOS3) (pSer633) antibody

Antigen: Nitric Oxide Synthase 3 (Endothelial Cell) (NOS3)

Synonyms: NOS, INOS, NOS2A, HEP-NOS, iNOS, Nos-2, Nos2a, i-NOS, NOS-II, eNOS, Nos-3, ecNOS, 2310065A03Rik, iNos, cNOS, EC-NOS, NOSIII, NOS3, NOS2, nos2, ECNOS

Binding Site: pSer633

Clonality: Monoclonal (37)

Host: Mouse

Reactivity: Human

Conjugate: Un-conjugated

Application: Western Blotting (WB)

Catalog no.: ABIN968905

Additional Information

Alternative name: eNOS

Immunogen: Phosphorylated Human eNOS (pS633) Peptide

Format: Liquid

Isotype: IgG1

Clone: 37

Description: 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.
Synonyms: Nitric Oxide Synthase

Characteristics: 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.

Molecular Weight: 140 kDa

Comments:

Related Products: ABIN968536, ABIN967389, ABIN967886

Application Details

Concentration: 250 µg/ml

Purity: Purified

Purification: Purified from tissue culture supernatant or ascites by affinity chromatography.

Buffer: Aqueous buffered solution containing BSA, glycerol.

Preservative: 0.09% Sodium azide.

Storage: Store undiluted at -20° C.

Research Area: Cancer, Enzymes, Metabolism, Inflammation

Restrictions: For Research Use only

Images

Western blot analysis for eNOS (pS633). Human endothelial cells were either left untreated (lane 1) or were treated with 200 U/mL of lambda phosphatase for 1 hour at 37°C (lane 2). The top panel was probed with a mouse anti-eNOS antibody (ABIN967886) and the bottom panel was probed with the mouse anti-eNOS (pS633) antibody at a 1:500 dilution with a band observable at ~ 140 kDa.

Publications

Product: Dimmeler, Fleming, Fisslthaler et al.: "Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation." in: Nature, Vol. 399, Issue 6736, pp. 601-5, 1999 (PubMed).

Gallis, Corthals, Goodlett et al.: "Identification of flow-dependent endothelial nitric-oxide synthase phosphorylation sites by mass spectrometry and regulation of phosphorylation and nitric oxide production by the phosphatidylinositol 3-kinase inhibitor LY294002." in: The Journal of biological chemistry, Vol. 274, Issue 42, pp. 30101-8, 1999 (PubMed).

Butt, Bernhardt, Smolenski et al.: "Endothelial nitric-oxide synthase (type III) is activated and becomes calcium independent upon phosphorylation by cyclic nucleotide-dependent protein kinases." in: The Journal of biological chemistry, Vol. 275, Issue 7, pp. 5179-87, 2000 (PubMed).

Michell, Chen Zp, Tiganis et al.: "Coordinated control of endothelial nitric-oxide synthase phosphorylation by protein kinase C and the cAMP-dependent protein kinase." in: The Journal of biological chemistry, Vol. 276, Issue 21, pp. 17625-8, 2001 (PubMed).