Recombinant human Peroxiredoxin 6 protein (His tag N-Terminus)
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(2 Publications)
Recombinant human Peroxiredoxin 6 protein (His tag N-Terminus) is a Human Full Length protein, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, WB, FuncS.
View Alternative Names
AOP2, KIAA0106, PRDX6, Peroxiredoxin-6, 1-Cys peroxiredoxin, 24 kDa protein, Acidic calcium-independent phospholipase A2, Antioxidant protein 2, Glutathione-dependent peroxiredoxin, Liver 2D page spot 40, Lysophosphatidylcholine acyltransferase 5, Non-selenium glutathione peroxidase, Red blood cells page spot 12, 1-Cys PRX, aiPLA2, LPC acyltransferase 5, LPCAT-5, Lyso-PC acyltransferase 5, NSGPx
- WB
Unknown
Western blot - Recombinant human Peroxiredoxin 6 protein (His tag N-Terminus) (AB87631)
All lanes:
Western blot - Anti-Peroxiredoxin 6 antibody (<a href='/en-us/products/primary-antibodies/peroxiredoxin-6-antibody-ab73350'>ab73350</a>) at 1 µg/mL
All lanes:
Western blot - Recombinant human Peroxiredoxin 6 protein (His tag N-Terminus) (ab87631) 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: 25 kDa
true
Exposure time: 30s
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant human Peroxiredoxin 6 protein (His tag N-Terminus) (AB87631)
3ug by SDS-PAGE under reducing condition and visualized by coomassie blue stain.
false
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
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.
Specifications
Form
Liquid
Additional notes
Purified by using conventional chromatography.
General info
Function
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (PubMed : 10893423, PubMed : 9497358). Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides (PubMed : 10893423). Also has phospholipase activity, can therefore either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or hydrolyze the sn-2 ester bond of phospholipids (phospholipase activity) (PubMed : 10893423, PubMed : 26830860). These activities are dependent on binding to phospholipids at acidic pH and to oxidized phospholipds at cytosolic pH (PubMed : 10893423). Plays a role in cell protection against oxidative stress by detoxifying peroxides and in phospholipid homeostasis (PubMed : 10893423). 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 (PubMed : 26830860).
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 (PubMed:26830860).
Subcellular localisation
Lysosome
Target data
Publications (2)
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Cell communication and signaling : CCS 23:15 PubMed39780184
2025
Applications
Unspecified application
Species
Unspecified reactive species
BMC genomics 24:245 PubMed37147584
2023
Applications
Unspecified application
Species
Unspecified reactive species
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