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AB195174

Recombinant Mouse Peroxiredoxin 6 protein

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(2 Publications)

Recombinant Mouse Peroxiredoxin 6 protein is a Mouse Full Length protein, in the 2 to 224 aa range, expressed in Escherichia coli, with >99%, suitable for SDS-PAGE, sELISA.

View Alternative Names

Aop2, Ltw4, Prdx5, Prdx6, Peroxiredoxin-6, 1-Cys peroxiredoxin, Acidic calcium-independent phospholipase A2, Antioxidant protein 2, Glutathione-dependent peroxiredoxin, Lysophosphatidylcholine acyltransferase 5, Non-selenium glutathione peroxidase, 1-Cys PRX, aiPLA2, LPC acyltransferase 5, LPCAT-5, Lyso-PC acyltransferase 5, NSGPx

3 Images
Sandwich ELISA - Recombinant Mouse Peroxiredoxin 6 protein (AB195174)
  • sELISA

Supplier Data

Sandwich ELISA - Recombinant Mouse Peroxiredoxin 6 protein (AB195174)

Example of data generated using ab195174 in a sandwich ELISA.

ELISA - Recombinant Mouse Peroxiredoxin 6 protein (AB195174)
  • ELISA

Supplier Data

ELISA - Recombinant Mouse Peroxiredoxin 6 protein (AB195174)

Example of data generated using ab195174 in a direct ELISA.

SDS-PAGE - Recombinant Mouse Peroxiredoxin 6 protein (AB195174)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Mouse Peroxiredoxin 6 protein (AB195174)

SDS PAGE gel stained with colloidal coomassie blue

Lane 1 : Ladder
Lane 2 : ab195174, 500ng

Key facts

Purity

>99% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

sELISA, SDS-PAGE

applications

Biologically active

No

Accession

O08709

Animal free

No

Carrier free

No

Species

Mouse

Storage buffer

pH: 7.5 Constituents: 10% Trehalose, 8.06% Sodium chloride, 2.16% Sodium phosphate dibasic heptahydrate, 0.2% Potassium chloride, 0.2% Potassium phosphate monobasic

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "sELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Product details

Product was previously marketed under the MitoSciences sub-brand.

Sequence info

[{"sequence":"HHHHHHGSGGSGPGGLLLGDEAPNFEANTTIGRIRFHDFLGDSWGILFSHPRDFTPVCTTELGRAAKLAPEFAKRNVKLIALSIDSVEDHLAWSKDINAYNGETPTEKLPFPIIDDKGRDLAILLGMLDPVEKDDNNMPVTARVVFIFGPDKKLKLSILYPATTGRNFDEILRVVDSLQLTGTKPVATPVDWKKGESVMVVPTLSEEEAKQCFPKGVFTKELPSGKKYLRYTPQP","proteinLength":"Full Length","predictedMolecularWeight":"25.96 kDa","actualMolecularWeight":null,"aminoAcidEnd":224,"aminoAcidStart":2,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"O08709","tags":[{"tag":"His","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Peroxiredoxin 6 also known as Prdx6 or peroxiredoxin-6 is a unique member of the peroxiredoxin family. It distinguishes itself by possessing both peroxidase and phospholipase A2 activities. This protein weighs approximately 25 kDa and is ubiquitously expressed in various tissues showing a high concentration in the lung. The expression pattern suggests its importance across different physiological contexts.
Biological function summary

We can understand peroxiredoxin 6 as a versatile enzyme that reduces hydrogen peroxide and organic hydroperoxides. It does not form a complex like some other peroxiredoxins. Instead it acts independently in cellular protection against oxidative stress. This role is mainly due to its peroxidase activity which helps in maintaining cellular redox balance and mitigating oxidative damage.

Pathways

Multiple cellular processes incorporate the enzymatic functions of peroxiredoxin 6. It plays an important role in the antioxidant defense pathway by collaborating with glutathione peroxidase to detoxify hydrogen peroxide. Another major pathway that involves Prdx6 is the phospholipid metabolism where it participates in the repair of oxidatively damaged cell membranes. This protein interacts with cytoplasmic thioredoxin proteins forming a network for managing intracellular reactive oxygen species.

Peroxiredoxin 6 has significant implications. Researchers have linked it to lung cancer where its expression levels correlate with disease progression possibly interacting with oncogenic proteins like NF-kB. In addition peroxiredoxin 6 is associated with neurodegenerative diseases such as Alzheimer’s disease. Its function in oxidative stress regulation might influence the aggregation of proteins like Tau which is a hallmark of Alzheimer's pathology.

Specifications

Form

Liquid

General info

Function

Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (By similarity). Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides (By similarity). Has phospholipase activity (PubMed : 26830860). Can either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or hydrolyze the sn-2 ester bond of phospholipids (phospholipase activity) (By similarity). These activities are dependent on binding to phospholipids at acidic pH and to oxidized phospholipds at cytosolic pH (By similarity). Plays a role in cell protection against oxidative stress by detoxifying peroxides and in phospholipid homeostasis (By similarity). Exhibits acyl-CoA-dependent lysophospholipid acyltransferase which mediates the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (PubMed : 26830860). Shows a clear preference for LPC as the lysophospholipid and for palmitoyl CoA as the fatty acyl substrate (By similarity).

Sequence similarities

Belongs to the peroxiredoxin family. Prx6 subfamily.

Post-translational modifications

Irreversibly inactivated by overoxidation of Cys-47 to sulfinic acid (Cys-SO(2)H) and sulfonic acid (Cys-SO(3)H) forms upon oxidative stress.. Phosphorylation at Thr-177 by MAP kinases increases the phospholipase activity of the enzyme (By similarity). The phosphorylated form exhibits a greater lysophosphatidylcholine acyltransferase activity compared to the non-phosphorylated form (By similarity).

Subcellular localisation

Lysosome

Product protocols

Target data

Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (By similarity). Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides (By similarity). Has phospholipase activity (PubMed : 26830860). Can either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or hydrolyze the sn-2 ester bond of phospholipids (phospholipase activity) (By similarity). These activities are dependent on binding to phospholipids at acidic pH and to oxidized phospholipds at cytosolic pH (By similarity). Plays a role in cell protection against oxidative stress by detoxifying peroxides and in phospholipid homeostasis (By similarity). Exhibits acyl-CoA-dependent lysophospholipid acyltransferase which mediates the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (PubMed : 26830860). Shows a clear preference for LPC as the lysophospholipid and for palmitoyl CoA as the fatty acyl substrate (By similarity).
See full target information Prdx6

Publications (2)

Recent publications for all applications. Explore the full list and refine your search

Nature communications 15:2716 PubMed38548759

2024

Condensin-mediated restriction of retrotransposable elements facilitates brain development in Drosophila melanogaster.

Applications

Unspecified application

Species

Unspecified reactive species

Bert I Crawford,Mary Jo Talley,Joshua Russman,James Riddle,Sabrina Torres,Troy Williams,Michelle S Longworth

Bioengineered 12:2676-2687 PubMed34115550

2021

Overexpression of PLK1 relieved the myocardial ischemia-reperfusion injury of rats through inducing the mitophagy and regulating the p-AMPK/FUNDC1 axis.

Applications

Unspecified application

Species

Unspecified reactive species

Shan Mao,Shuning Tian,Xianghong Luo,Ming Zhou,Zheng Cao,Ji Li
View all publications

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