Active • Host: E. coli • AA: 2-1,205 (full length) • Tag: N-terminal His • MW: 134 kDa
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eNOS (bovine, recombinant; E. coli expressed)

Item No. 11868

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • Constitutive NOS
  • cNOS
  • Endothelial Nitric Oxide Synthase
  • Endothelial NOS
  • Nitric Oxide Synthase 3
Purity
Partially pure
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
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    10 units

    $469

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    Product Description

    Endothelial nitric oxide synthase (eNOS), also known as NOS3, converts arginine to citrulline and nitric oxide (NO) to regulate endothelial homeostasis and vascular tone.1,2,3 It is composed of an N-terminal oxygenase domain that contains binding sites for its substrate L-arginine (Item No. 23703), heme, and the cofactor tetrahydrobiopterin (BH4) and a reductase domain with binding sites for NADPH, flavin mononucleotide, flavin-adenine dinucleotide, and calmodulin.3 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.1,2 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.4,5 Cayman's eNOS (bovine, recombinant; E. coli expressed) can be used for enzyme assay applications.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Qian, J., and Fulton, D. Post-translational regulation of endothelial nitric oxide synthase in vascular endothelium. Front. Physiol. 4, 347 (2013).

    2. Heiss, C., Rodriguez-Mateos, A., and Kelm, M. Central role of eNOS in the maintenance of endothelial homeostasis. Antioxid. Redox Signal. 22(14), 1230-1242 (2015).

    3. Siragusa, M., and Fleming, I. The eNOS signalosome and its link to endothelial dysfunction. Pflugers Arch. 468(7), 1125-1137 (2016).

    4. Daiber, A., Xia, N., Steven, S., et al. New therapeutic implications of endothelial nitric oxide synthase (eNOS) function/dysfunction in cardiovascular disease. Int. J. Mol. Sci. 20(1), 187 (2019).

    5. Roe, N.D., and Ren, J. Nitric oxide synthase uncoupling: A therapeutic target in cardiovascular diseases. Vascul. Pharmacol. 57(5-6), 168-172 (2012).

    Product Citations

    Palumbo, A., d'Ischia, M., and Cioffi, F.A. 2-thiouracil is a selective inhibitor of neuronal nitric oxide synthase antagonising tetrahydrobiopterin-dependent enzyme activation and dimerisation. FEBS Lett. 485(2-3), 109-112 (2000).