eNOS (Ser-632), Phosphospecific Antibody

Applications

Reactivity

Human
Mouse
Rat

Overview
Catalog #	bsm-70571m
Product Name	eNOS (Ser-632), Phosphospecific Antibody
Applications	WB
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. This sequence is conserved in human (Ser-633) and rat (Ser-632) eNOS, and has low homology to other NOS family members.
Reactivity	Human, Mouse, Rat
Specifications
Conjugation	Unconjugated
Host	Mouse
Source	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.
Modification Site	Ser-632
Clonality	Monoclonal
Clone #	M232
Isotype	IgG1
Purification	Purified by Protein A.
Storage Buffer	PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol
Storage Condition	Storage at -20C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20C.
Target
Swiss Prot	P70313
Synonyms	endothelial Nitric Oxide Synthase, eNOS, ecNOS, NOS-III, NOS3, NOSIII
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.
Application Dilution
WB