Recombinant Human Peroxiredoxin-4/PRDX4
Product name: | Recombinant Human Peroxiredoxin-4/PRDX4 |
Source: | E.coli |
Purity: | Greater than 95% as determined by reducing SDS-PAGE. |
Buffer Formulation: | Supplied as a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, 1mM DTT, pH 7.2. |
Applications: | Applications:SDS-PAGE; WB; ELISA; IP. |
Storage: | Avoid repeated freeze/thaw cycles. Store at 2-8 oC for one month. Aliquot and store at -80 oC for 12 months. |
UOM: | 100ug/50ug/200ug/1mg/1g |
Source | E.coli |
Description | 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. |
Names | Peroxiredoxin-4, Antioxidant Enzyme AOE372, AOE37-2, Peroxiredoxin IV, Prx-IV, Thioredoxin Peroxidase AO372, Thioredoxin-Dependent Peroxide Reductase A0372, PRDX4 |
Accession # | Q13162 |
Formulation | Supplied as a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, 1mM DTT, pH 7.2. |
Shipping |
The product is shipped on dry ice/ice packs. |
Storage |
Store at < -20°C, stable for 6 months after receipt. Please minimize freeze-thaw cycles. |
Purity |
Greater than 95% as determined by reducing SDS-PAGE. |
Endotoxin | Less than 0.1 ng/µg (1 IEU/µg) as determined by LAL test. |
Amino Acid Sequence |
MGSSHHHHHHSSGLVPRGSHMWETEERPRTREEECHFYAGGQVYPGEASRVSVADHSLHLSKAKI SKPAPYWEGTAVIDGEFKELKLTDYRGKYLVFFFYPLDFTFVCPTEIIAFGDRLEEFRSINTEVV ACSVDSQFTHLAWINTPRRQGGLGPIRIPLLSDLTHQISKDYGVYLEDSGHTLRGLFIIDDKGIL RQITLNDLPVGRSVDETLRLVQAFQYTDKHGEVCPAGWKPGSETIIPDPAGKLKYFDKLN
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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. |