Phospho-NOS3 (pSer632) Mouse Antibody [Clone ID: M232]

CAT#: TA389170

Anti-eNOS (Ser-632), Phosphospecific Antibody


USD 385.00

5 Days*

Size
    • 100 ul

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Specifications

Product Data
Clone Name M232
Applications WB
Recommended Dilution WB: 1:500
Reactivities Human, Mouse, Rat
Host Mouse
Isotype IgG1
Immunogen Clone M232 was generated from a Phospho-eNOS (Ser-632) synthetic peptide (coupled to carrier protein) corresponding to amino acids surrounding Ser-632 in mouse eNOS. This sequence is conserved in human (Ser-633) and rat (Ser-632) eNOS, and has low homology to other NOS family members.
Specificity The antibody detects a 140 and 120 kDa* bands on SDS-PAGE immunoblots of human umbilical vein endothelial cells, but these bands are not observed after lambda phosphatase treatment. The 120 kDa band may be a truncated form of eNOS.
Formulation PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol
Concentration lot specific
Purification Protein A Purified
Conjugation Unconjugated
Storage Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.
Stability After date of receipt, stable for at least 1 year at -20°C.
Predicted Protein Size 140
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. 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.
Note Protein G purified tissue culture supernatant.
Reference Data

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