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Key Documents

SAB4200227

Sigma-Aldrich

Anti-NOX1 (N-terminal) antibody produced in rabbit

~1.5 mg/mL, affinity isolated antibody

Synonyme(s) :

Anti-GP91-2, Anti-MOX1, Anti-NADPH oxidase 1, Anti-NOH-1, Anti-NOH1

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen ~72 kDa

Espèces réactives

human

Concentration

~1.5 mg/mL

Technique(s)

immunohistochemistry (formalin-fixed, paraffin-embedded sections): 5-10 μg/mL using using human colon
western blot: 1.5-3.0 μg/mL using using HT29 cell extracts

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 ... NOX1(27035)

Description générale

Nicotinamide adenine dinucleotide phosphate (NADPH) oxidase 1 (NOX1) belongs to the family of NADPH oxidases. It is abundantly expressed in colon, primarily in differentiated epithelial cells. NOX1 has two cytosolic regulators, NOXA1 and NOXO1 as well as Ras-related protein Rac1.

Immunogène

synthetic peptide corresponding to the N-terminal of human NOX1 isoform long (NOX1L). The corresponding sequence is identical in human NOX1 isoform long variant (NOX1LV) and highly conserved in mouse and rat NOX1 (76% sequence identity).

Application

Anti-NOX1 (N-terminal) antibody produced in rabbit has been used in immunoblotting and immunohistochemistry.

Actions biochimiques/physiologiques

Nicotinamide adenine dinucleotide phosphate (NADPH) oxidase 1 (NOX1) catalyzes the generation of superoxide ion. It is mitogenic and a potent trigger of the angiogenic switch, increasing the vascularity of tumors and inducing molecular markers of angiogenesis.. NOX1 promotes neurotoxic activation of microglia suggesting, that they play a central role during neuroinflammatory states and in amyotrophic lateral sclerosis (ALS).

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

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

Jack L Arbiser et al.
Proceedings of the National Academy of Sciences of the United States of America, 99(2), 715-720 (2002-01-24)
The reactive oxygen-generating enzyme Nox1 transforms NIH 3T3 cells, rendering them highly tumorigenic and, as shown herein, also increases tumorigenicity of DU-145 prostate epithelial cells. Although Nox1 modestly stimulates cell division in both fibroblasts and epithelial cells, an increased mitogenic
Biological roles for the NOX family NADPH oxidases.
William M Nauseef
The Journal of biological chemistry, 283(25), 16961-16965 (2008-04-19)
Miklós Geiszt et al.
Journal of immunology (Baltimore, Md. : 1950), 171(1), 299-306 (2003-06-21)
Reactive oxygen species (ROS) serve several physiological functions; in some settings they act in host defense, while in others they function in cellular signaling or in biosynthetic reactions. We studied the expression and function of a recently described source of
Cyril Chéret et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 28(46), 12039-12051 (2008-11-14)
Reactive oxygen species (ROS) modulate intracellular signaling but are also responsible for neuronal damage in pathological states. Microglia, the resident CNS macrophages, are prominent sources of ROS through expression of the phagocyte oxidase which catalytic subunit Nox2 generates superoxide ion

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