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

Applications

Tested Dilution

Publications

Western Blot (WB)

1:1,000

-

Immunocytochemistry (ICC/IF)

1:400

-

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

Wet ice

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.