Recombinant Human Peroxiredoxin-3/PRDX3
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| Amount : | 50 µg |
| Content : | Supplied as a 0.2 µm filtered solution of 20mM TrisHCl,pH8.0. |
| Storage condition : | Store at -20°C, stable for 6 months after receipt. Please minimize freeze-thaw cycles. |
| AA sequence : | MPAVTQHAPYFKGTAVVNGEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWINTPRKNGGLGHMNIALLSDLTKQISRDYGVLLEGSGLALRGLFIIDPNGVIKHLSVNDLPVGRSVEETLRLVKAFQYVETHGEVCPANWTPDSPTIKPSPAASKEYFQKVNQ |
Source: E. coli.
MW :21.6kD.
Recombinant Human Peroxiredoxin-3 is produced by our E.coli expression system and the target gene encoding Pro63-Gln256 is expressed. Thioredoxin-Dependent Peroxide Reductase Mitochondrial (PRDX3) is an enzyme that belongs to the AhpC/TSA family. Human and mouse PRDX3 genes are highly conserved, and they map to the regions syntenic between mouse and human chromosomes. Human PRDX3 protein has an antioxidant function and is localized in the mitochondrion. PRDX3 is involved in redox regulation of the cell. PRDX3 protects radical-sensitive enzymes from oxidative damage by a radical-generating system. It acts synergistically with MAP3K13 to regulate the activation of NF-kappa-B in the cytosol.
MW :21.6kD.
Recombinant Human Peroxiredoxin-3 is produced by our E.coli expression system and the target gene encoding Pro63-Gln256 is expressed. Thioredoxin-Dependent Peroxide Reductase Mitochondrial (PRDX3) is an enzyme that belongs to the AhpC/TSA family. Human and mouse PRDX3 genes are highly conserved, and they map to the regions syntenic between mouse and human chromosomes. Human PRDX3 protein has an antioxidant function and is localized in the mitochondrion. PRDX3 is involved in redox regulation of the cell. PRDX3 protects radical-sensitive enzymes from oxidative damage by a radical-generating system. It acts synergistically with MAP3K13 to regulate the activation of NF-kappa-B in the cytosol.
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: | Mitochondrion, Cytoplasm |
| 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: | 116136. 67 interactions. |
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