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Key Documents

N3893

Sigma-Aldrich

Anti-Nitric Oxide Synthase, Endothelial (1185-1205) antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Synonyme(s) :

Anti-eNOS

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

IgG fraction of antiserum

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen 135 kDa

Espèces réactives

bovine, mouse, rat, human

Technique(s)

immunohistochemistry (frozen sections): 1:100 using acetone-fixed, frozen tissue sections of mouse heart
microarray: suitable
western blot: 1:10,000 using bovine lung endothelial cell extract

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... NOS3(4846)
mouse ... Nos3(18127)
rat ... Nos3(24600)

Description générale

Endothelial nitric oxide synthase (eNOS) is a 135 kDa protein and is an isoform of NOS. eNOS expression is not limited to the endothelium of blood vessels, it is also expressed in the epithelium of several tissues, including the bronchial tree. It is also localized in neurons in the brain, especially the pyramidal cells of the hippocampus.
The gene encoding endothelial nitric oxide synthase (eNOS) is localized on chromosome 7q35-36 and has 26 exons.

Immunogène

synthetic peptide corresponding to nitric oxide synthase (NOS) of bovine endothelial origin (eNOS, amino acids 1185-1205 with an N-terminally added lysine) conjugated to KLH. The immunogen sequence is highly conserved in human eNOS.

Application

Anti-Nitric Oxide Synthase, Endothelial (1185-1205) antibody produced in rabbit has been used in immunoblotting and immunohistochemistry.

Actions biochimiques/physiologiques

Endothelial nitric oxide synthase (eNOS) has been studied as a modulator of vascular function and it is involved in the production of nitric oxide. Defects in the enzyme expression have been shown to be associated with coronary artery disease.

Forme physique

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Clause de non-responsabilité

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Mónica Martínez-Moreno et al.
FEBS letters, 579(14), 3159-3163 (2005-06-01)
We have performed the recombinant expression and purification of the reductase domain of endothelial nitric oxide synthase (eNOS) and used it as a bait in search for interacting proteins present in endothelial cells. Using mass spectrometry of the bound proteins
Contribution of oxidative stress and prostanoids in endothelial dysfunction induced by chronic fluoxetine treatment
Simplicio JA, et al.
Vascular Pharmacology, 73(2), 124-137 (2015)
Katia Colombo Marchi et al.
Alcohol and alcoholism (Oxford, Oxfordshire), 51(5), 522-534 (2016-07-07)
Investigate the role of NADPH oxidase on ethanol-induced hypertension and vascular oxidative stress. Male Wistar rats were treated with ethanol (20% v/v). Apocynin (10 mg/kg/day, i.p.) prevented ethanol-induced hypertension. The increased contractility of endothelium-intact and endothelium-denuded aortic rings from ethanol-treated
Acute restraint stress induces endothelial dysfunction: role of vasoconstrictor prostanoids and oxidative stress
Carda APP, et al.
Stress: The International Journal on the Biology of Stress, 18(2), 233-243 (2015)
L G Fryer et al.
Diabetes, 49(12), 1978-1985 (2000-12-16)
Glucose transport in skeletal muscle is stimulated by two distinct stimuli, insulin and exercise. The mechanism by which exercise stimulates glucose transport is not known, although it is distinct from the insulin-mediated pathway. Recently, it has been shown that AMP-activated

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