Anti-eNOS (Tyr-657) /nNOS (Tyr-895), Phosphospecific Antibody

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.

Our eNOS (Tyr-657) /nNOS (Tyr-895) rabbit polyclonal phosphospecific primary antibody from PhosphoSolutions is produced in-house. It detects human, mouse, and rat eNOS (Tyr-657) /nNOS (Tyr-895) and is antigen affinity purified. It is great for use in WB, ICC.

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) .

For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.

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.