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SAB4200097

Sigma-Aldrich

Anti-NOX1 antibody produced in rabbit

~1.5 mg/mL, affinity isolated antibody

Synonym(s):

Anti-GP91-2, Anti-MOX1 (mitogenic oxidase 1), Anti-NADPH oxidase 1, Anti-NOH1 (NADPH oxidase homolog 1)

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~72 kDa

species reactivity

human

concentration

~1.5 mg/mL

technique(s)

immunohistochemistry: 10-20 μg/mL using formalin-fixed, paraffin-embedded human colon
western blot: 0.5-1.0 μg/mL using HS68 cell extracts

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... NOX1(27035)
mouse ... Nox1(237038)
rat ... Nox1(114243)

General description

NADPH oxidase 1 (NOX1) is encoded by the gene mapped to human chromosome Xq22.1. The protein belongs to the family of NADPH oxidases and is co-localized with caveolin in punctate patches on the surface and laterally on the cellular margins. NOX1 is mainly expressed in colon epithelium.

Application

Anti-NOX1 antibody produced in rabbit has been used in:
  • Immunocytochemistry.
  • Immunoprecipitation
  • Immunoblotting.
Anti-NOX1 antibody produced in rabbit may be used in immunofluorescence and immunohistochemistry.

Biochem/physiol Actions

NADPH oxidase 1 (NOX1) requires two cytosolic regulators NADPH oxidase activator 1(NOXA1) and NADPH oxidase organizer 1 (NOXO1) as well as Ras-related C3 botulinum toxin substrate 1 (Rac1) for its activity. NOX1 and NOX2 promote neurotoxic activation of microglia suggesting that they play a central role during neuroinflammatory states and in amyotrophic lateral sclerosis (ALS). In ALS mice deletion of either NOX1 and NOX2 gene have been shown to significantly slowed disease progression and improved survival.
NOX1 catalyzes the production of hydrogen peroxide (H2O2). Overexpression of the protein leads to the production of both superoxide and H2O2 and triggers angiogenic switch, mediating vascularization and rapid expansion of the tumor. Elevated expression of NOX1 has been observed in the brain of Parkinson′s disease (PD) patients.

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 Code

10 - Combustible liquids

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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ROS production as a common mechanism of ENaC regulation by EGF, insulin, and IGF-1
Ilatovskaya DV
American Journal of Physiology. Cell Physiology, 304, C102-C111 (2013)
Involvement of Rac1 in activation of multicomponent Nox1-and Nox3-based NADPH oxidases
Ueyama T, et al.
Molecular and cellular biology, 26(6), 2160-2174 (2006)
Reactive oxygen generated by Nox1 triggers the angiogenic switch
Arbiser JL
Proceedings of the National Academy of Sciences of the USA, 99, 715-720 (2002)
Anthony J Valente et al.
Cellular signalling, 25(6), 1447-1456 (2013-04-02)
We investigated the role of TRAF3 interacting protein 2 (TRAF3IP2), a redox-sensitive adapter protein and an upstream regulator of IKK and JNK in interleukin (IL)-18 induced smooth muscle cell migration, and the mechanism of its inhibition by simvastatin. The pleiotropic
Augusto C Montezano et al.
Journal of the American Heart Association, 7(12) (2018-06-17)
NADPH Oxidase 5 (Nox5) is a calcium-sensitive superoxide-generating Nox. It is present in lower forms and higher mammals, but not in rodents. Nox5 is expressed in vascular cells, but the functional significance remains elusive. Given that contraction is controlled by

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