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N3893

Sigma-Aldrich

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

IgG fraction of antiserum, buffered aqueous solution

Sinónimos:

Anti-eNOS

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About This Item

MDL number:
MFCD01092428
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 135 kDa

species reactivity

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

UniProt accession no.

P29474

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

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

General description

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.

Application

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

Biochem/physiol Actions

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.

Physical form

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

Disclaimer

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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Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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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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