Name :
PRDX4 Protein

Description :
Peroxiredoxin-4 (PRDX4) is a member of the AhpC/TSA family. PRDX4 is a cytoplasmic protein and contains one thioredoxin domain. PRDX4 exists in homodimer or heterodimer with PRDX1. PRDX4 reduces hydrogen peroxide and alkyl hydroperoxides to water and alcohol with the use of reducing equivalents derived from thiol-containing donor molecules. In addition, PRDX4 is probably involved in redox regulation of the cell, regulating the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation.

Species :
Human

Uniprotkb :
E. coli

Tag :
N-6His

Synonyms :
Prx-IV, Thioredoxin-Dependent Peroxide Reductase A0372, PRDX4, Thioredoxin Peroxidase AO372, Peroxiredoxin-4, Antioxidant Enzyme AOE372, Peroxiredoxin IV, AOE37-2

Construction :
Recombinant Human Peroxiredoxin-4 is produced by our E.coli expression system and the target gene encoding Trp38-Asn271 is expressed with a 6His tag at the N-terminus.

Protein Purity :
Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Molecular Weight :
30 KDa, reducing conditions

Endotoxin :
Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.

Formulatione :
Supplied as a 0.2 μm filtered solution of PBS, pH 7.4.

Reconstitution :

Stability & Storage :
Store at ≤-70°C, stable for 6 months after receipt.Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.

Shipping :
The product is shipped on dry ice/polar packs.Upon receipt, store it immediately at the temperature listed below.

Research Background :
Peroxiredoxin-4 (PRDX4) is a member of the AhpC/TSA family. PRDX4 is a cytoplasmic protein and contains one thioredoxin domain. PRDX4 exists in homodimer or heterodimer with PRDX1. PRDX4 reduces hydrogen peroxide and alkyl hydroperoxides to water and alcohol with the use of reducing equivalents derived from thiol-containing donor molecules. In addition, PRDX4 is probably involved in redox regulation of the cell, regulating the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation.

References and Literature :

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