GLRX2 Recombinant Protein
|Amount :||50 µg|
|Purification :||Purity of GRX2 is greater than 90% as determined by SDS-PAGE.|
|Content :||Glutaredoxin-2 solution contains 25mM Tris-HCl pH-7.5 & 0.01% Na Azide.|
|Storage condition :||1 week at 2-10°C. For long term store at -20 to -80°C.|
|Alternative Name :||Thioltransferase, Glutathione-dependent oxidoreductase 2, TTR, TTR1, GLRX2, GRX2, GRX-2, GLRX-2, Glutaredoxin 2.|
Source : Escherichia Coli. Glutaredoxin-2 Saccharamyces cerevisiae Recombinant containing 6x His tag at C-terminus produced in E.Coli is a single, non-glycosylated, Polypeptide chain having a molecular mass of 17 kDa. GLRX2 is a multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage. Glutaredoxins are a family of glutathione-dependent hydrogen donors that participate in a variety of cellular redox reactions.