Invitrogen

Phospho-eNOS/nNOS (Tyr657, Tyr895) Polyclonal Antibody

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Datasheet
Protocols
Questions & Answers
Datasheet
Protocols
Questions & Answers

Product Details

PA5-143729

Applications
Tested Dilution
Publications

Western Blot (WB)

1:1,000
-

Immunocytochemistry (ICC/IF)

1:1,000
-
Product Specifications

Species Reactivity

Human, Mouse, Rat

Host/Isotype

Rabbit / IgG

Class

Polyclonal

Type

Antibody

Immunogen

Phospho-eNOS (Tyr-657) synthetic peptide (coupled to carrier protein) corresponding to amino acids surrounding tyrosine 657 in human eNOS. This sequence is conserved in mouse (Tyr-656) and rat (Tyr-656) eNOS, and is identical to the conserved site in nNOS (Tyr-895). The site is also well conserved in iNOS (Tyr-631).

Conjugate

Unconjugated Unconjugated Unconjugated

Form

Liquid

Concentration

~1.0 mg/mL

Purification

Antigen affinity chromatography

Storage buffer

PBS with 1mg/mL BSA, 50% glycerol

Contains

0.05% sodium azide

Storage conditions

-20°C, Avoid Freeze/Thaw Cycles

Shipping conditions

Ambient (domestic); Wet ice (international)

RRID

AB_2942957

Product Specific Information

The antibody detects a 140 kDa* band on SDS-PAGE immunoblots of human umbilical vein endothelial cells treated with pervanadate, and this reactivity is not observed after akaline phosphatase treatment.

Target Information

Nitric oxide (NO) has a broad range of biological activities and is implicated in signaling pathways in phylogenetically diverse species. Nitric oxide synthases (NOS), the enzymes responsible for synthesis of NO, are homodimers whose monomers are themselves two fused enzymes: a cytochrome reductase and a cytochrome that requires three cosubstrates (L-arginine, NADPH, and oxygen) and five cofactors or prosthetic groups (FAD, FMN, calmodulin, tetrahydrobiopterin, and heme). Several distinct NOS isoforms are produced from three distinct genes. The inducible form of NOS, iNOS (NOS-II), is Ca2+ independent and is expressed in a broad range of cell types, and two constitutive Ca2+/CaM-dependent forms of NOS: nNOS (bNOS, NOS-I) identified in neurons and eNOS (ecNOS, NOS-III) identified in endothelial cells. Regulation of eNOS activity occurs through phosphorylation at multiple sites. Phosphorylation of Ser-633 (mouse Ser-632) in the FMN binding domain increases eNOS activity and may be important for the maintenance of NO synthesis after initial activation by Ca2+ flux and Ser-1177 phosphorylation.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.

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Bioinformatics

Protein Aliases: cNOS; Constitutive NOS; EC-NOS; endothelial Nitric Oxide Synthase; endothelial nitric oxide synthase 3; Endothelial NOS; eNOS; Nitric oxide synthase 3; nitric oxide synthase 3 (endothelial cell); nitric oxide synthase 3 transcript variant eNOS-delta20; nitric oxide synthase 3 transcript variant eNOS-delta20-21; nitric oxide synthase 3 transcript variant eNOS-delta21; Nitric oxide synthase, endothelial; NOS type III; NOS-III; NOSIII

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Gene Aliases: 2310065A03Rik; ECNOS; eNOS; Nos-3; NOS3

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UniProt ID: (Human) P29474, (Mouse) P70313, (Rat) Q62600

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Entrez Gene ID: (Human) 4846, (Mouse) 18127, (Rat) 24600

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Function(s)
actin monomer binding nitric-oxide synthase activity iron ion binding protein binding calmodulin binding FMN binding heme binding tetrahydrobiopterin binding arginine binding cadmium ion binding flavin adenine dinucleotide binding NADP binding scaffold protein binding actin binding NADPH-hemoprotein reductase activity beta-catenin binding oxidoreductase activity cadherin binding metal ion binding nitric-oxide synthase binding Hsp90 protein binding
Process(es)
angiogenesis ovulation from ovarian follicle in utero embryonic development blood vessel remodeling regulation of sodium ion transport regulation of the force of heart contraction by chemical signal regulation of systemic arterial blood pressure by endothelin arginine catabolic process nitric oxide biosynthetic process mitochondrion organization nitric oxide mediated signal transduction regulation of blood pressure negative regulation of cell proliferation response to heat negative regulation of platelet activation negative regulation of muscle hyperplasia smooth muscle hyperplasia removal of superoxide radicals lung development positive regulation of guanylate cyclase activity lipopolysaccharide-mediated signaling pathway response to fluid shear stress negative regulation of potassium ion transport endothelial cell migration cell redox homeostasis positive regulation of angiogenesis negative regulation of blood pressure positive regulation of vasodilation regulation of blood vessel size regulation of nitric-oxide synthase activity negative regulation of hydrolase activity negative regulation of calcium ion transport oxidation-reduction process negative regulation of extrinsic apoptotic signaling pathway via death domain receptors signal transduction response to estradiol positive regulation of apoptotic process negative regulation of smooth muscle cell proliferation cellular response to mechanical stimulus cellular response to transforming growth factor beta stimulus response to hypoxia female pregnancy aging response to mechanical stimulus response to fructose response to metal ion response to lead ion response to organic cyclic compound response to activity response to lipopolysaccharide response to cytokine cellular response to heat response to statin response to drug response to amino acid response to peptide hormone response to ethanol response to axon injury response to corticosterone response to hyperoxia response to lipoprotein particle retina development in camera-type eye bone development cellular response to magnesium ion cellular response to cAMP cellular response to tumor necrosis factor cellular response to growth factor stimulus cellular response to organic cyclic compound response to candesartan response to peptide response to ketone response to salt
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