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AB74172

Recombinant human Peroxiredoxin 1/PAG protein (His tag N-Terminus)

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(2 Publications)

Recombinant human Peroxiredoxin 1/PAG protein (His tag N-Terminus) is a Human Full Length protein, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, FuncS.

View Alternative Names

PAGA, PAGB, TDPX2, PRDX1, Peroxiredoxin-1, Natural killer cell-enhancing factor A, Proliferation-associated gene protein, Thioredoxin peroxidase 2, Thioredoxin-dependent peroxide reductase 2, Thioredoxin-dependent peroxiredoxin 1, NKEF-A, PAG

1 Images
SDS-PAGE - Recombinant human Peroxiredoxin 1/PAG protein (His tag N-Terminus) (AB74172)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant human Peroxiredoxin 1/PAG protein (His tag N-Terminus) (AB74172)

ab74172, detecting Peroxiredoxin 1/PAG protein (His tag) at 24 kDa by SDS-PAGE. 3ug by SDS-PAGE under reducing condition and visualized by coomassie blue stain.

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 600-670 pmole/min/μg. Enzymatic activity is defined as the amount of hydroperoxide that 1μg of enzyme can reduce at 25C for 1 minute. Conditions - Reaction buffer : 1mM DTT, 0.03X PBS, 0.5% glycerol. - Initial amount of substrate : 0.85μg - Total reaction volume: 100 μl. - Reaction temperature: Room temperature Specific activity: approximately 600-670 pmole/min/μg. Enzymatic activity was confirmed by measuring the remaining peroxide after incubation of PRDX1 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

Q06830

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.5 Constituents: 20% Glycerol (glycerin, glycerine), 0.242% Tris

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 600-670 pmole/min/µg.</p>" } } }
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Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMSSGNAKIGHPAPNFKATAVMPDGQFKDISLSDYKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHLAWVNTPKKQGGLGPMNIPLVSDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQITVNDLPVGRSVDETLRLVQAFQFTDKHGEVCPAGWKPGSDTIKPDVQKSKEYFSKQK","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q06830","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 1 also known as PAG plays an important role as an antioxidant enzyme. It is part of the peroxiredoxin family with a molecular mass of around 22 kDa. This protein helps reduce hydrogen peroxide and organic hydroperoxides to water and corresponding alcohols using reducing equivalents provided by thiol-containing donor molecules. Peroxiredoxin 1/PAG expresses widely in human tissues and cells including liver and erythrocytes reflecting its involvement in cellular redox regulation.
Biological function summary

Peroxiredoxin 1 helps maintain cellular homeostasis by protecting cells from oxidative stress. It forms homodimers or interacts with other proteins to propagate cellular responses to changes in redox state. As an important member of the antioxidant defense mechanism it contributes to cellular signaling through modulation of hydrogen peroxide signaling pathways. The protein also plays a role in cell proliferation and apoptosis making it significant for cellular health and disease prevention.

Pathways

Peroxiredoxin 1 participates in critical processes such as the MAPK signaling and TGF-beta pathways. It interacts with MAPK-related proteins influencing cell survival and growth. Peroxiredoxin 1 indirectly modulates downstream signaling molecules that contribute to cellular responses. In these pathways the protein's antioxidant properties allow regulation of reactive oxygen species levels which directly affect cellular signaling cascades.

Peroxiredoxin 1 is relevant to cancer and neurodegenerative disorders. Overexpression or misregulation of this protein has been linked to various cancers where it potentially interacts with oncogenic proteins like c-Myc to promote tumor progression. Additionally abnormal levels of Peroxiredoxin 1 associate with neurodegenerative diseases as oxidative stress is a common factor in their pathology. These connections suggest the protein as a promising target in therapeutic interventions for these diseases.
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Specifications

Form

Liquid

Additional notes

ab74172 is purified by 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. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2) (PubMed : 9497357). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity).

Sequence similarities

Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.

Post-translational modifications

Phosphorylated on Thr-90 during the M-phase, which leads to a more than 80% decrease in enzymatic activity.. The enzyme can be inactivated by further oxidation of the cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) instead of its condensation to a disulfide bond. It can be reactivated by forming a transient disulfide bond with sulfiredoxin SRXN1, which reduces the cysteine sulfinic acid in an ATP- and Mg-dependent manner.

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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. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2) (PubMed : 9497357). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity).
See full target information PRDX1
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Publications (2)

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

EMBO molecular medicine 14:e14511 PubMed34779136

2021

LIF, a mitogen for choroidal endothelial cells, protects the choriocapillaris: implications for prevention of geographic atrophy.

Applications

Unspecified application

Species

Unspecified reactive species

Pin Li,Qin Li,Nilima Biswas,Hong Xin,Tanja Diemer,Lixian Liu,Lorena Perez Gutierrez,Giovanni Paternostro,Carlo Piermarocchi,Sergii Domanskyi,Ruikang K Wang,Napoleone Ferrara

Biochimica et biophysica acta. General subjects 1861:3019-3029 PubMed27612662

2016

S-nitrosylation of peroxiredoxin 1 contributes to viability of lung epithelial cells during Bacillus anthracis infection.

Applications

Unspecified application

Species

Unspecified reactive species

Myung-Chul Chung,Farhang Alem,Sarah G Hamer,Aarthi Narayanan,Konstantin Shatalin,Charles Bailey,Evgeny Nudler,Ramin M Hakami
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