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R8656

Sigma-Aldrich

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

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

Synonym(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

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 ~22 kDa

species reactivity

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

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

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

General description

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.

Immunogen

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.

Biochem/physiol Actions

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.

Physical form

Solution in 0.01 M phophate 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

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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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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)
Glutathionylation of the active site cysteines of peroxiredoxin 2 and recycling by glutaredoxin
Peskin AV, et al.
The Journal of Biological Chemistry, 291(6), 3053-3062 (2016)
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
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

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