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Key Documents

P0058

Sigma-Aldrich

Anti-Peroxiredoxin 6 (C-terminal) antibody produced in rabbit

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

Synonyme(s) :

Anti-1-Cys peroxiredoxin, Anti-Acidic calcium-independent phospholipase A2, Anti-Antioxidant protein 2, Anti-Non-selenium glutathione peroxidase, AOP2, Anti-PRDX6

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen ~25 kDa

Espèces réactives

human, rat, mouse

Concentration

~1.0 mg/mL

Technique(s)

immunoprecipitation (IP): 2-5 μg using whole extract of mouse brain
western blot: 0.5-1.0 μg/mL using whole extract of human HeLa cells.
western blot: 1-2 μg/mL using whole extract of rat brain

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 ... PRDX6(9588)
mouse ... Prdx6(11758)
rat ... Prdx6(94167)

Description générale

PRDX6 (peroxiredoxin 6) is a mammalian peroxidase belonging to the 1-Cys Prdx family, meaning it has 1-Cys at position 47 (Cys47). This protein is localized to cytoplasm, lysosomes, mitochondria, endoplasmic reticulum (ER) and plasma membrane. It is a homodimeric protein which is especially observed in mammalian lungs.†

Application

Anti-Peroxiredoxin 6 (C-terminal) antibody produced in rabbit has been used for Western Blotting.

Actions biochimiques/physiologiques

PRDX6 (peroxiredoxin 6) has both peroxidase and phospholipase A2 (PLA2) activities and thus, is a bifunctional protein. In liver, as a peroxidase it confers protection against damage from ROS (reactive oxygen species) during ischemia-reperfusion injury. As a PLA2 it is involved in lung surfactant metabolism. It is also essential for normal nicotinamide adenine dinucleotide phosphate-oxidase activity. In the livers of donors after brain death (DBD), this protein suppresses ischemia- and hypoxia-induced liver damage, and its expression is controlled by NF-κB (nuclear factor). In human and mouse neuronal cells, the delivery of PRDX6 protein leads to delay or suppression in oxidative stress-induced neuronal cell death.
Peroxiredoxin 6 contains a single redox-active cysteine and uses glutathione to catalyze the reduction of H2O2 and other organic peroxides. Overexpression of peroxiredoxin 6 in cells protects them against oxidative damage, whereas knockdown of this enzyme results in oxidative stress and apoptosis. The phospholipase A2 activity plays an important role in surfactant homeostasis. Peroxiredoxin 6 is a major antioxidant enzyme which functions in antioxidant defense and lung phospholipid metabolism.

Forme physique

Solution in 0.01 M phosphate 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)

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Consulter la Bibliothèque de documents

Peroxiredoxin 6 is a potent cytoprotective enzyme in the epidermis
Kumin A, et al.
The American Journal of Pathology, 169(4), 1194-1205 (2006)
Peroxiredoxin 6 attenuates ischemia- and hypoxia-induced liver damage of brain-dead donors.
Tu Q et al
Molecular Medicine Reports, 13(1), 753-761 (2016)
Gaetano Calabrese et al.
The EMBO journal, 38(18), e101552-e101552 (2019-08-08)
Hydrogen peroxide (H2 O2 ) plays important roles in cellular signaling, yet nonetheless is toxic at higher concentrations. Surprisingly, the mechanism(s) of cellular H2 O2 toxicity remain poorly understood. Here, we reveal an important role for mitochondrial 1-Cys peroxiredoxin from
Yuichiro J Suzuki et al.
F1000Research, 6, 455-455 (2017-06-06)
Reactive oxygen species (ROS) have been recognized as second messengers, however, targeting mechanisms for ROS in cell signaling have not been defined. While ROS oxidizing protein cysteine thiols has been the most popular proposed mechanism, our laboratory proposed that ligand/receptor-mediated
Delivery of a protein transduction domain-mediated Prdx6 protein ameliorates oxidative stress-induced injury in human and mouse neuronal cells.
Singh SP et al
American Journal of Physiology. Cell Physiology, 310(1), :C1-:16 (2016)

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