eNOS (phospho-Tyr-657) Blocking Peptide
€155.00
In stock
SKU
ECM-NX4035
Background:
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, inducible NOS (iNOS, NOS-II), neuronal NOS (bNOS, NOS-I), and endothelial NOS (eNOS, ecNOS, NOS-III). 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. Tyr-657 is phosphorylated by PYK2 in response to fluid shear stress and this phosphorylation leads to attenuation of enzyme activity.
Sequence: Phospho-eNOS (Tyr-657) synthetic peptide 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).
Specificity: The peptide is specifically recognized by anti-eNOS (Tyr-657) phospho-specific antibody (NP4031) in ELISA, and has been shown to block the reactivity of NP4031 during Western blot. In addition, the peptide is recommended for use in blocking NP4031 reactivity in immunocytochemistry.
Buffer/Storage:
Blocking Peptide is supplied in 50µl phosphate-buffered saline and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
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, inducible NOS (iNOS, NOS-II), neuronal NOS (bNOS, NOS-I), and endothelial NOS (eNOS, ecNOS, NOS-III). 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. Tyr-657 is phosphorylated by PYK2 in response to fluid shear stress and this phosphorylation leads to attenuation of enzyme activity.
Sequence: Phospho-eNOS (Tyr-657) synthetic peptide 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).
Specificity: The peptide is specifically recognized by anti-eNOS (Tyr-657) phospho-specific antibody (NP4031) in ELISA, and has been shown to block the reactivity of NP4031 during Western blot. In addition, the peptide is recommended for use in blocking NP4031 reactivity in immunocytochemistry.
Buffer/Storage:
Blocking Peptide is supplied in 50µl phosphate-buffered saline and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
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