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Merck

N3893

Sigma-Aldrich

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

IgG fraction of antiserum, buffered aqueous solution

Synonym(e):

Anti-eNOS

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About This Item

MDL-Nummer:
UNSPSC-Code:
12352203
NACRES:
NA.41

Biologische Quelle

rabbit

Konjugat

unconjugated

Antikörperform

IgG fraction of antiserum

Antikörper-Produkttyp

primary antibodies

Klon

polyclonal

Form

buffered aqueous solution

Mol-Gew.

antigen 135 kDa

Speziesreaktivität

bovine, mouse, rat, human

Methode(n)

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

UniProt-Hinterlegungsnummer

Versandbedingung

dry ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

Angaben zum Gen

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

Allgemeine Beschreibung

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.

Immunogen

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.

Anwendung

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

Biochem./physiol. Wirkung

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.

Physikalische Form

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

Haftungsausschluss

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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Lagerklassenschlüssel

10 - Combustible liquids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


Analysenzertifikate (COA)

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Die Dokumentenbibliothek aufrufen

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)
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)
María Teresa Soto-Navarrete et al.
Frontiers in cardiovascular medicine, 9, 928362-928362 (2022-08-26)
Bicuspid aortopathy occurs in approximately 50% of patients with bicuspid aortic valve (BAV), the most prevalent congenital cardiac malformation. Although different molecular players and etiological factors (genetic and hemodynamic) have been suggested to be involved in aortopathy predisposition and progression
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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