Human Recombinant PRDX6 protein, His Tag (V2LY-0526-LY6115)

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Basic Information

Expressed Host
E. coli
Protein Species
Human
Tag
His Tag
Protein Construction
This product is Human Recombinant PRDX6 protein, His Tag consist of Amino Acid: 1-224 and predicts a molecular mass of 26.5 kDa.
Molecule Mass
26.5 kDa
Sequence
Amino Acid: 1-224
Species
Human

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity
>95% as determined by SDS-PAGE
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile PBS
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
peroxiredoxin 6
Function
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (PubMed:9497358, PubMed:10893423).
Can reduce H2O2 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).
Biological Process
Cell redox homeostasisManual Assertion Based On ExperimentIBA:GO_Central
Cellular oxidant detoxificationManual Assertion Based On ExperimentIMP:CAFA
Glycerophospholipid catabolic processManual Assertion Based On ExperimentIMP:CAFA
Positive regulation of mRNA splicing, via spliceosomeManual Assertion Based On ExperimentIGI:UniProtKB
Response to oxidative stressManual Assertion Based On ExperimentIMP:CAFA
Cellular Location
Cytoplasm
Lysosome
Also found in lung secretory organelles (lamellar bodies).
PTM
Irreversibly inactivated by overoxidation of Cys-47 to sulfinic acid (Cys-SO2H) and sulfonic acid (Cys-SO3H) 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).
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For research use only. Not intended for any clinical use.

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