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AB93947

Recombinant human Peroxiredoxin 4 protein (His tag N-Terminus)

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(5 Publications)

Recombinant human Peroxiredoxin 4 protein (His tag N-Terminus) is a Human Full Length protein, in the 38 to 271 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, FuncS.

View Alternative Names

Peroxiredoxin-4, Antioxidant enzyme AOE372, Peroxiredoxin IV, Thioredoxin peroxidase AO372, Thioredoxin-dependent peroxide reductase A0372, Thioredoxin-dependent peroxiredoxin 4, AOE37-2, Prx-IV, PRDX4

1 Images
SDS-PAGE - Recombinant human Peroxiredoxin 4 protein (AB93947)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant human Peroxiredoxin 4 protein (AB93947)

15% SDS-PAGE analysis of ab93947 (3μg)

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

FuncS, SDS-PAGE

applications

Biologically active

Yes

Biological activity

Specific activity: approximately 230-310 pmole/min/μg. Enzymatic activity was confirmed by measuring the remaining peroxide after incubation of PRDX4 and peroxide for 20 min at room temperature. Specific activity is defined as the amount of hydroperoxide that 1ug of enzyme can reduce at 25 C for 1 minute. Specific activity: approximately 230-310 pmole/min/μg. Enzymatic activity was confirmed by measuring the remaining peroxide after incubation of PRDX4 and peroxide for 20 min at room temperature. Specific activity is defined as the amount of hydroperoxide that 1ug of enzyme can reduce at 25 C for 1 minute.

Accession

Q13162

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 0.316% Tris HCl

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p>Specific activity: approximately 230-310 pmole/min/µg.</p>" } } }
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Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMWETEERPRTREEECHFYAGGQVYPGEASRVSVADHSLHLSKAKISKPAPYWEGTAVIDGEFKELKLTDYRGKYLVFFFYPLDFTFVCPTEIIAFGDRLEEFRSINTEVVACSVDSQFTHLAWINTPRRQGGLGPIRIPLLSDLTHQISKDYGVYLEDSGHTLRGLFIIDDKGILRQITLNDLPVGRSVDETLRLVQAFQYTDKHGEVCPAGWKPGSETIIPDPAGKLKYFDKLN","proteinLength":"Full Length","predictedMolecularWeight":"28.8 kDa","actualMolecularWeight":null,"aminoAcidEnd":271,"aminoAcidStart":38,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q13162","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
True
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Supplementary information

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

Peroxiredoxin 4 also known as Prdx4 is a protein that acts as an antioxidant enzyme and belongs to the peroxiredoxin family. It influences the reduction of hydrogen peroxide and organic hydroperoxides. The molecular mass of Prdx4 is approximately 31 kDa. It is expressed mainly in the endoplasmic reticulum but you can find some expression in the cytosol as well.
Biological function summary

Prdx4 plays a list of roles in cellular defense against oxidative stress. It not only reduces peroxides but also contributes to the maintenance of protein folding by modifying disulfide bonds in the endoplasmic reticulum. Prdx4 does not function as part of a larger complex but acts independently within its compartments. The protective functions of Prdx4 are important for cell survival and proper cellular function.

Pathways

Prdx4 interacts with oxidative stress response pathways. Specifically it participates in the redox signaling pathways that regulate cellular reactive oxygen species levels. Peroxiredoxin 4 is closely associated with proteins such as thioredoxin in these pathways. Together they regulate the cellular redox environment which is important for maintaining cellular homeostasis.

Oxidative stress imbalance implicates Prdx4 in conditions like diabetes and cancer. For example in diabetes altered Prdx4 levels disturb normal cell function due to increased oxidative stress. In cancer Prdx4 can influence tumor progression by modulating the antioxidant capacity within cells. Prdx4 also shows a functional connection to proteins like glutathione peroxidase in regulating oxidative stress-related pathologies.
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Specifications

Form

Liquid

Additional notes

ab93947 was purified using conventional chromatography techniques.

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General info

Function

Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation.

Sequence similarities

Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.

Post-translational modifications

The enzyme can be inactivated by further oxidation of the cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) and sulphonic acid (C(P)-SO3H) instead of its condensation to a disulfide bond.

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Product protocols

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Target data

Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation.
See full target information PRDX4
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Publications (5)

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

The Journal of biological chemistry 296:100665 PubMed33895140

2021

Oxidation of peroxiredoxin-4 induces oligomerization and promotes interaction with proteins governing protein folding and endoplasmic reticulum stress.

Applications

Unspecified application

Species

Unspecified reactive species

Evan A Elko,Allison M Manuel,Sheryl White,Ester Zito,Albert van der Vliet,Vikas Anathy,Yvonne M W Janssen-Heininger

The EMBO journal 38:e101266 PubMed31544965

2019

Prdx4 limits caspase-1 activation and restricts inflammasome-mediated signaling by extracellular vesicles.

Applications

Unspecified application

Species

Unspecified reactive species

Simone Lipinski,Steffen Pfeuffer,Philipp Arnold,Christian Treitz,Konrad Aden,Henriette Ebsen,Maren Falk-Paulsen,Nicolas Gisch,Antonella Fazio,Jan Kuiper,Anne Luzius,Susanne Billmann-Born,Stefan Schreiber,Gabriel Nuñez,Hans-Dietmar Beer,Till Strowig,Mohamed Lamkanfi,Andreas Tholey,Philip Rosenstiel

Journal of applied physiology (Bethesda, Md. : 198 127:858-866 PubMed31246554

2019

Characterization of extracellular redox enzyme concentrations in response to exercise in humans.

Applications

Unspecified application

Species

Unspecified reactive species

Alex J Wadley,Gary Keane,Tom Cullen,Lynsey James,Jordan Vautrinot,Matthew Davies,Bethan Hussey,David J Hunter,Sarabjit Mastana,Adrian Holliday,Steen V Petersen,Nicolette C Bishop,Martin R Lindley,Steven J Coles

Methods in molecular biology (Clifton, N.J.) 1208:299-311 PubMed25323516

2014

Preoxiredoxin family members (Prx3 and Prx4) and pregnancy disorder (recurrent pregnancy loss).

Applications

Unspecified application

Species

Unspecified reactive species

Behrouz Gharesi-Fard

American journal of reproductive immunology (New York, N.Y. : 1989) 69:248-55 PubMed23190175

2012

Presence of autoantibody against two placental proteins, peroxiredoxin 3 and peroxiredoxin 4, in sera of recurrent pregnancy loss patients.

Applications

Unspecified application

Species

Unspecified reactive species

Behrouz Gharesi-Fard,Leila Jafarzadeh,Farzaneh Ghaderi-shabankareh,Jaleh Zolghadri,Eskandar Kamali-Sarvestani
View all publications
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