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P0050

Sigma-Aldrich

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

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

Synonym(s):

Anti-1-Cys peroxiredoxin; acidic calcium-independent phospholipase A2, Anti-Antioxidant protein 2, Anti-NSGPx, Anti-Non-selenium glutathione peroxidase, AOP2, Anti-P29, Anti-PRDX6, Anti-PRX, Anti-aiPLA2

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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 ~25 kDa

species reactivity

human, mouse, rat

packaging

antibody small pack of 25 μL

concentration

~1.0 mg/mL

technique(s)

immunoprecipitation (IP): 5-10 μg using lysate of mouse brain
western blot: 2-5 μg/mL using whole extract of human HeLa cells
western blot: 5-10 μg/mL using whole extract of rat liver

UniProt accession no.

P30041

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

Peroxiredoxin 6 (1-Cys peroxiredoxin), is a member of the thiol-specific antioxidant peroxiredoxin family. Six mammalian peroxiredoxins have been identified. Peroxiredoxin 6 is the only one that contains a single redox-active cysteine and uses glutathione to catalyze the reduction of H2O2 and other organic peroxides. It is expressed in all tissues with the highest levels in the lung.

Application

The antibody has been used in several immunochemical techniques including immunoblotting and immunoprecipitation.

Biochem/physiol Actions

Peroxiredoxins are peroxidases, with the use of reducing equivalents provided by thiol-containing proteins that reduce hydrogen peroxide (H2O2) to water and alkyl hydroperoxides to alcohol. Peroxiredoxin 6 is a bifunctional enzyme with peroxidase and phospholipase A2 activities. 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

12 - Non Combustible Liquids

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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1-Cys Peroxiredoxin, a Bifunctional Enzyme with Glutathione Peroxidase and Phospholipase A2 Activities
Chen JW, et al.
The Journal of biological chemistry, 275(37), 28421-28427 (2000)
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.
Yefim Manevich et al.
Free radical biology & medicine, 38(11), 1422-1432 (2005-05-14)
Peroxiredoxin 6 (Prdx6), a bifunctional 25-kDa protein with both GSH peroxidase and phospholipase A2 activities, is the only mammalian 1-Cys member of the peroxiredoxin superfamily and is expressed in all major organs, with a particularly high level in lung. Prdx6
C McDonald et al.
International journal of oncology, 45(1), 219-226 (2014-05-03)
Peroxiredoxin (Prdx) proteins are thiol-specific antioxidants that protect cells from oxidative stress in many normal and disease states. There are six Prdx proteins expressed in mammals, each with a characteristic tissue expression, subcellular distribution and substrate specificity. Recent studies have
Ran Liu et al.
Molecular neurobiology, 50(3), 1035-1048 (2014-05-06)
Following spinal cord injury (SCI), limit spontaneous functional recovery often emerged. However, the neuronal mechanisms associated with this phenomenon still remains obscure. By using proteomics analysis, endoplasmic reticulum protein 29 (ERp29) was discovered to increase in the motor cortexes of

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