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

Details for Product anti-NOS3 Antibody No. ABIN968905, Supplier: Log in to see
Antigen
  • NOS3
  • ECNOS
  • eNOS
  • NOS
  • EC-NOS
  • NOSIII
  • cNOS
  • 2310065A03Rik
  • Nos-3
  • ecNOS
  • eNos
  • ENOS
Alternatives
anti-Human ENOS antibody for Enzyme Immunoassay
Epitope
pSer633
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24
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9
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2
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Reactivity
Human
375
208
194
31
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2
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Host
Mouse
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Clonality (Clone)
Monoclonal ()
Conjugate
This ENOS antibody is un-conjugated
28
25
17
8
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Application
Western Blotting (WB)
282
167
68
68
57
54
24
23
23
19
11
7
5
2
2
1
1
Supplier
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Immunogen Phosphorylated Human eNOS (pS633) Peptide
Clone 37-eNOS
Isotype IgG1
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.
Purification The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography.
Alternative Name eNOS (NOS3 Antibody Abstract)
Background 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
Molecular Weight 140 kDa
Research Area Cancer, Enzymes, Metabolism, Inflammation
Pathways ACE Inhibitor Pathway
Comment

Related Products: ABIN968536, ABIN967389, ABIN967886

Restrictions For Research Use only
Format Liquid
Concentration 250 μg/mL
Buffer Aqueous buffered solution containing BSA, glycerol, and ≤0.09 % sodium azide.
Preservative Sodium azide
Precaution of Use This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Storage Comment Store undiluted at -20°C.
Supplier Images
Western Blotting (WB) image for anti-ENOS antibody (Nitric Oxide Synthase 3 (Endothelial Cell)) (pSer633) (ABIN968905) Western blot analysis for eNOS (pS633). Human endothelial cells were either left untr...
Product cited in: 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).

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).

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).

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).