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HPA006983

Sigma-Aldrich

Anti-PRDX6 antibody produced in rabbit

enhanced validation

Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution

Synonym(s):

Anti-1-Cys PRX antibody produced in rabbit, Anti-1-Cys peroxiredoxin antibody produced in rabbit, Anti-24 kDa protein antibody produced in rabbit, Anti-Acidic calcium-independent phospholipase A2 antibody produced in rabbit, Anti-Antioxidant protein 2 antibody produced in rabbit, Anti-NSGPx antibody produced in rabbit, Anti-Non-selenium glutathione peroxidase antibody produced in rabbit, Anti-Peroxiredoxin-6 antibody produced in rabbit, Anti-aiPLA2 antibody produced in rabbit

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About This Item

UNSPSC Code:
12352203
Human Protein Atlas Number:
HPA006983
NACRES:
NA.43

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

product line

Prestige Antibodies® Powered by Atlas Antibodies

form

buffered aqueous glycerol solution

species reactivity

human

enhanced validation

orthogonal RNAseq
Learn more about Antibody Enhanced Validation

technique(s)

immunoblotting: 0.04-0.4 μg/mL
immunohistochemistry: 1:50-1:200

immunogen sequence

GGLLLGDVAPNFEANTTVGRIRFHDFLGDSWGILFSHPRDFTPVCTTELGRAAKLAPEFAKRNVKLIALSIDSVEDHLAWSKDINAYNCEEPTEKLPFPIIDDRNRELAILLGMLDPAEKDEKGMPVTARVVFVFGPDKKLKLSILYPA

UniProt accession no.

P30041

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... PRDX6(9588)

Related Categories

General description

PRDX6 (Peroxiredoxin 6) is a thiol-specific antioxidant protein belonging to the thiol-specific antioxidant peroxiredoxin family. It contains one redox-active cysteine molecule, thus, also named as 1-Cys peroxiredoxin. In mammals, six types of peroxiredoxins have been identified. It is highly expressed in the lungs along with other tissues.

Immunogen

Peroxiredoxin-6 recombinant protein epitope signature tag (PrEST)

Application

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)

Biochem/physiol Actions

PRDX6 (Peroxiredoxin 6) possesses two types of activities, peroxidase and phospholipase A2 activities. It acts as a bifunctional enzyme in the β cell controlling during oxidative stress. PRDX6 converts hydrogen peroxide (H2O2) and alkyl hydroperoxides to water and alcohol through redox reactions. It also functions as an antioxidant enzyme in the antioxidant defense mechanism and lung phospholipid metabolism. It has been reported that overexpressed PRDX6 reduces the chances of oxidative damage, whereas knockdown expression leads to the oxidative stress and apoptosis. Deficiency in PRDX6 causes impaired homeostasis and cell death/apoptosis.

Features and Benefits

Prestige Antibodies® are highly characterized and extensively validated antibodies with the added benefit of all available characterization data for each target being accessible via the Human Protein Atlas portal linked just below the product name at the top of this page. The uniqueness and low cross-reactivity of the Prestige Antibodies® to other proteins are due to a thorough selection of antigen regions, affinity purification, and stringent selection. Prestige antigen controls are available for every corresponding Prestige Antibody and can be found in the linkage section.

Every Prestige Antibody is tested in the following ways:
  • IHC tissue array of 44 normal human tissues and 20 of the most common cancer type tissues.
  • Protein array of 364 human recombinant protein fragments.

Linkage

Corresponding Antigen APREST70729

Physical form

Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide

Legal Information

Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany

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

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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

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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Bruno Schremmer et al.
Sub-cellular biochemistry, 44, 317-344 (2007-12-19)
All six mammalian peroxiredoxins are expressed in the lung. Peroxiredoxin (Prx) VI is the isoform expressed at the highest level and its lung expression exceeds that for other organs. The predominant location of Prx VI is the cytosol and acidic
Flavia M M Paula et al.
Molecular and cellular endocrinology, 374(1-2), 56-64 (2013-04-30)
Peroxiredoxins are a family of six antioxidant enzymes (PRDX1-6), and may be an alternative system for the pancreatic beta cells to cope with oxidative stress. This study investigated whether the main diabetogenic pro-inflammatory cytokines or the anti-inflammatory cytokine IL-4 modulate
J W Chen et al.
The Journal of biological chemistry, 275(37), 28421-28427 (2000-07-14)
This report provides definitive evidence that the protein 1-Cys peroxiredoxin is a bifunctional ("moonlighting") enzyme with two distinct active sites. We have previously shown that human, rat, and bovine lungs contain an acidic Ca(2+)-independent phospholipase A(2) (aiPLA(2)). The cDNA encoding
S W Kang et al.
The Journal of biological chemistry, 273(11), 6303-6311 (1998-04-16)
A new type of peroxidase enzyme, named thioredoxin peroxidase (TPx), that reduces H2O2 with the use of electrons from thioredoxin and contains two essential cysteines was recently identified. TPx homologs, termed peroxiredoxin (Prx), have also been identified and include several
Hyun Ae Woo et al.
The Journal of biological chemistry, 278(48), 47361-47364 (2003-10-16)
We previously suggested that oxidation of the active site cysteine of peroxiredoxin (Prx) I or Prx II to cysteine sulfinic acid in H2O2-treated cells is reversible (Woo, H. A., Chae, H. Z., Hwang, S. C., Yang, K.-S., Kang, S. W.
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