Recombinant Human Peroxiredoxin-4/PRDX4 (N-6His)
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| Amount : | 50 µg |
| Content : | Supplied as a 0.2 µm filtered solution of 20mM PB, 150mM NaCl, 1mM DTT, pH 7.2. |
| Storage condition : | Store at -20°C, stable for 6 months after receipt. Please minimize freeze-thaw cycles. |
| AA sequence : | MGSSHHHHHHSSGLVPRGSHMWETEERPRTREEECHFYAGGQVYPGEASRVSVADHSLHLSKAKISKPAPYWEGTAVIDGEFKELKLTDYRGKYLVFFFYPLDFTFVCPTEIIAFGDRLEEFRSINTEVVACSVDSQFTHLAWINTPRRQGGLGPIRIPLLSDLTHQISKDYGVYLEDSGHTLRGLFIIDDKGILRQITLNDLPVGRSVDETLRLVQAFQYTDKHGEVCPAGWKPGSETIIPDPAGKLKYFDKLN |
Source: E.coli.
MW :33.8kD.
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. 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.
MW :33.8kD.
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. 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.
Endotoxin : Less than 0.1 ng/µg (1 IEU/µg) as determined by LAL test.
For Research Use Only. Not for use in diagnostic/therapeutics procedures.
| Subcellular location: | Cytoplasm, Endoplasmic reticulum |
| Post transnational modification: | The enzyme can be inactivated by further oxidation of the cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) and sulphonic acid (C(P)-SO3H) instead of its condensation to a disulfide bond. |
| BioGrid: | 115800. 58 interactions. |
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