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P0058

Sigma-Aldrich

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

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

Synonym(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

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~25 kDa

species reactivity

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

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

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

General description

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.

Biochem/physiol Actions

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.

Physical form

Solution in 0.01 M phosphate 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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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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