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

Specifications

Product Data
Clone Name	M232
Applications	WB
Recommend Dilution	WB: 1:500
Reactivity	Human, Rat, Mouse
Host	Mouse
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 Condition	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.
Predicted Protein Size	140
Database Link	UniProt ID P29474
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

*Delivery time may vary from web posted schedule. Occasional delays may occur due to unforeseen complexities in the preparation of your product. International customers may expect an additional 1-2 weeks in shipping.