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Key Documents

R8656

Sigma-Aldrich

Anti-Peroxiredoxin 2 (C-terminal) antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody, buffered aqueous solution

Synonyme(s) :

Anti-NKEFB, Anti-Natural killer-enhancing factor B, Anti-PRDX2, Anti-TDPX1, Anti-Thiol-specific antioxidant 1, Anti-Thioredon peroxidase 1, Anti-Torin

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen ~22 kDa

Espèces réactives

rat, human, mouse

Concentration

~1.0 mg/mL

Technique(s)

immunoprecipitation (IP): 2.0-5.0 μg using lysate of mouse 3T3 cells
western blot: 0.5-1.0 using whole extract of human HeLa cells
western blot: 1-2 μg/mL using whole extract of rat NRK cells

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 ... PRDX2(7001)
mouse ... Prdx2(21672)
rat ... PRDX2(29338)

Description générale

Peroxiredoxin 2 is a cytosolic member of the peroxiredoxin family of antioxidant enzymes. All peroxiredoxin enzymes exist as homodimers, they contain a conserved Cys residue corresponding to Cys51 in mammalian peroxiredoxin 1 and 2 and are distributed differentially within cells.

Immunogène

synthetic peptide corresponding to amino acid residues 184-198 of human peroxiredoxin 2 conjugated to KLH. The corresponding sequence is identical in rat and mouse peroxiredoxin 2.

Application

Anti-Peroxiredoxin 2 (C-terminal) antibody produced in rabbit has been used in immunoblottingand immunoprecipitation.

Actions biochimiques/physiologiques

Peroxiredoxin 2 has dual roles as a peroxireductase in moderately oxidative conditions and as a molecular chaperone that binds and protects denatured proteins in hyper-oxidative conditions. Peroxiredoxin 2 is involved in platelet-derived growth factor (PDGF) and tumor necrosis factor (TNF) signaling regulation and is elevated in several human cancers and neurodegenerative disorders.

Forme physique

Solution in 0.01 M phophate 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

Équipement de protection individuelle

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

2-cys peroxiredoxins: emerging hubs determining redox dependency of Mammalian signaling networks
Park J, et al.
International Journal of Cell Biology (2014)
Alexander V Peskin et al.
The Journal of biological chemistry, 291(6), 3053-3062 (2015-11-26)
Peroxiredoxin 2 (Prx2) is a thiol protein that functions as an antioxidant, regulator of cellular peroxide concentrations, and sensor of redox signals. Its redox cycle is widely accepted to involve oxidation by a peroxide and reduction by thioredoxin/thioredoxin reductase. Interactions
Regulation of PDGF signalling and vascular remodelling by peroxiredoxin II
Choi MH, et al.
Nature, 435(7040), 347-353 (2005)
Markus Dagnell et al.
The Journal of biological chemistry, 292(35), 14371-14380 (2017-07-08)
Regulation of growth factor signaling involves reversible inactivation of protein tyrosine phosphatases (PTPs) through the oxidation and reduction of their active site cysteine. However, there is limited mechanistic understanding of these redox events and their co-ordination in the presence of
Oxidative Stress-dependent Structural and Functional Switching of a Human 2-Cys Peroxiredoxin Isotype II That Enhances HeLa Cell Resistance to H2O2-induced Cell Death
Moon JC, et al.
Test, 280(31), 28775-28784 (2005)

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