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AB79945

Recombinant human Peroxiredoxin 1/PAG protein

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(1 Publication)

Recombinant human Peroxiredoxin 1/PAG protein is a Human Full Length protein, expressed in Baculovirus, with >90%, suitable for SDS-PAGE, WB, 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

3 Images
Functional Studies - Recombinant human Peroxiredoxin 1/PAG protein (AB79945)
  • FuncS

Unknown

Functional Studies - Recombinant human Peroxiredoxin 1/PAG protein (AB79945)
Western blot - Recombinant human Peroxiredoxin 1/PAG protein (AB79945)
  • WB

Unknown

Western blot - Recombinant human Peroxiredoxin 1/PAG protein (AB79945)

This protein is a homodimer consisting of two subunits with an expected molecular weight of 23kDa.

All lanes:

Western blot - Anti-Peroxiredoxin 1/PAG antibody (<a href='/en-us/products/primary-antibodies/peroxiredoxin-1-pag-antibody-ab41906'>ab41906</a>) at 1 µg/mL

All lanes:

Western blot - Recombinant human Peroxiredoxin 1/PAG protein (ab79945) at 0.01 µg

Secondary

All lanes:

Western blot - Goat Anti-Rabbit IgG H&L (HRP) preadsorbed (<a href='/en-us/products/secondary-antibodies/goat-rabbit-igg-h-l-hrp-preadsorbed-ab97080'>ab97080</a>) at 1/5000 dilution

Predicted band size: 22 kDa

true

Exposure time: 30s

SDS-PAGE - Recombinant human Peroxiredoxin 1/PAG protein (AB79945)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant human Peroxiredoxin 1/PAG protein (AB79945)

Lane 1 : ab79945 on 14% SDS-PAGE, Coomassie staining, 20μg.
Lane 2 : Protein marker.

Key facts

Purity

>90% SDS-PAGE

Expression system

Baculovirus

Tags

Tag free

Applications

SDS-PAGE, FuncS, WB

applications

Biologically active

Yes

Biological activity

Specific Activity between 800 and 1000 pmol/min/μg. Please enquire as to activity of specific lots. 1.88 μg of Peroxiredoxin 1 was incubated in 50 mM Hepes (pH 7.0) containing 200 μM NADPH, 3 μM thioredoxin, and 1.5 μM thioredoxin reductase. The reaction mixture was incubated at 30C for 5 min, followed by the addition of 0.22 mM H2O2. NADPH oxidation was monitored (fluorescence decrease) for the next 10 min.

Accession

Q06830

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 50% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.395% Tris HCl, 0.05% Sorbitan monolaurate, ethoxylated, 0.0462% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

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>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p>ab79945 can be used as a WB positive control in conjunction with <a href='/en-us/products/primary-antibodies/peroxiredoxin-1-pag-antibody-ab41906'>ab41906</a>.</p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p>Useful for the study of biochemical function.</p>" } } }
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Sequence info

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"Q06830","tags":[]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°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

Affinity purified.

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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 (1)

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

Cell chemical biology 26:449-461.e8 PubMed30713096

2019

Selective Disruption of Mitochondrial Thiol Redox State in Cells and In Vivo.

Applications

Unspecified application

Species

Unspecified reactive species

Lee M Booty,Justyna M Gawel,Filip Cvetko,Stuart T Caldwell,Andrew R Hall,John F Mulvey,Andrew M James,Elizabeth C Hinchy,Tracy A Prime,Sabine Arndt,Cristiane Beninca,Thomas P Bright,Menna R Clatworthy,John R Ferdinand,Hiran A Prag,Angela Logan,Julien Prudent,Thomas Krieg,Richard C Hartley,Michael P Murphy
View all publications
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