eNOS (bovine, recombinant, E. coli expressed)

Endothelial nitric oxide synthase (eNOS), also known as NOS3, converts arginine to citrulline and nitric oxide (NO) to regulate endothelial homeostasis and vascular tone. It is composed of an N-terminal oxygenase domain that contains binding sites for heme, its substrate L-arginine (Cay-23703), and the cofactor tetrahydrobiopterin (BH4) and a reductase domain with binding sites for NADPH, flavin mononucleotide, flavin-adenine dinucleotide, and calmodulin. eNOS is expressed in endothelial cells, as well as blood cells and circulating microparticles, with expression levels changing in response to growth factors, cytokines, and mechanical stimulation. Localization of eNOS is mediated by protein fatty acid acylation, with myristoylated and palmitoylated eNOS targeted to plasma membrane caveolae and the Golgi complex. eNOS functions as a homodimer and is activated by the binding of calcium-bound calmodulin. eNOS uncoupling and dysfunction, primarily induced by the loss of BH4 due to oxidation or decreased expression of dihydrofolate reductase (DHFR), induces the production of superoxide in place of NO and is a hallmark of most cardiovascular diseases, including atherosclerosis. Cayman's eNOS (bovine, recombinant, E. coli expressed) can be used for enzyme assay applications.Synonyms: Constitutive NOS, cNOS, Endothelial Nitric Oxide Synthase, Endothelial NOS, Nitric Oxide Synthase 3. Purity: Partially pure. Protein Identity Confirmed by Mass Spec: Yes. Source: Active recombinant bovine N-terminal His-tagged eNOS expressed in E. coli. Amino Acids: 2-1,205 (full length). MW: 134 kDa. Formulation: (Request formulation change), 50 mM HEPES, pH 7.8, with 0.5 mM DTT, 0.5 mM EDTA, 300 mM sodium chloride, 2 mM calcium chloride, 10 µM tetrahydro-L-biopterin (hydrochloride), and 20% glycerol. UniProt Accession #: P29473.