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SAB2701393

Sigma-Aldrich

Anti-DUOX1 antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Sinónimos:

DUOX1, LNOX1, MGC138840, MGC138841

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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

species reactivity

human

technique(s)

immunohistochemistry: suitable
western blot: 500-3000

NCBI accession no.

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... DUOX1(53905)

General description

The gene DUOX1 (dual oxidase 1) encodes a protein belonging to the family of NADPH oxidase/heme peroxidase proteins, Duox, and shares upto 85% amino acid similarity with another Duox isoform, Duox2. It contains an NAD(P)H oxidase domain and a heme peroxidase domain. The NAD(P)H oxidase domain of this protein is involved in H2O2 production and the heme peroxidase domain is similar to several peroxidases, but its function is yet to be characterized. The expression of Duox1 is stimulated by Th2 (T helper) cytokines, IL-4 (interleukin-4) and IL-13 (interleukin-13). The gene is mapped to human chromosome 15q15.3.

Immunogen

Recombinant fragment corresponding to a region within amino acids 257 and 566 of DUOX1 according to AAI14939

Application

Suggested starting dilutions are as follows: IHC-P: 1:100-1:1000, WB: 1:500-1:3000. Not yet tested in other applications. Optimal working dilutions should be determined experimentally by the end user.

Biochem/physiol Actions

The gene DUOX1 (dual oxidase 1) encodes a dual function NAD(P)H oxidase/peroxidase that serves as an important source for the production of hydrogen peroxide in respiratory tract epithelium. H2O2, thus produced, is involved in the regulation of cellular signaling pathways that participate in the production of inflammatory effectors. ATP-mediated activation of duox1 causes activation of ERK1/2 (extracellular signal-regulated kinase ½) and NFκ-B (nuclear factor κ-light-chain-enhancer of activated B cells) pathways. Duox1 is also involved in the regulation of pathways associated with production of various mucins, matrix metalloproteinase-9, and other inflammatory mediators, in response to environmental or bacterial stimuli.

Features and Benefits

Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.

Physical form

0.1M Tris, 0.1M Glycine, 20% Glycerol (pH7). 0.01% Thimerosal was added as a preservative.

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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pictograms

Exclamation mark

signalword

Warning

hcodes

Hazard Classifications

Aquatic Chronic 3 - Skin Sens. 1

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 2

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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Visite la Librería de documentos

Effect of iodide on nicotinamide adenine dinucleotide phosphate oxidase activity and Duox2 protein expression in isolated porcine thyroid follicles.
Morand S
Endocrinology, 144, 1241-1248 (2003)
ATP-mediated activation of the NADPH oxidase DUOX1 mediates airway epithelial responses to bacterial stimuli.
Boots AW
The Journal of Biological Chemistry, 284, 17858-17867 (2009)
Differential regulation of dual NADPH oxidases/peroxidases, Duox1 and Duox2, by Th1 and Th2 cytokines in respiratory tract epithelium.
Harper RW
Febs Letters, 579, 4911-4917 (2005)

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