Description
Data Sheet
| Amino acid sequence | MSAGWLDRAA GAAGAAAAAA SGMESNTSSS LENLATAPVN QIQETISDNC VVIFSKTSCS YCTMAKKLFH DMNVNYKVVE LDLLEYGNQF QDALYKMTGE RTVPRIFVNG TFIGGATDTH RLHKEGKLLP LVHQCYLKKS KRKEFQLEHH HHHH. |
| Description | Glutaredoxin-2 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 154 amino acids (20-164 a.a.) and having a molecular mass of 17 kDa. The GRX2 is fused to 8 amino acid His tag at C-Terminus. |
| Expression host | Escherichia Coli. |
| Formulation | Glutaredoxin-2 solution contains 20mM Tris-HCl pH-8 & 0.1mM PMSF and 10% glycerol. |
| Protein Background | 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. |
| Purity | Purity of GRX2 is greater than 90% as determined by SDS-PAGE. |
| Reagent Appearance | Sterile Filtered clear colorless solution. |
| Stability | 1 week at 2-10°C. For long term store at -20 to -80°C. |
| Synonyms | Thioltransferase, Glutathione-dependent oxidoreductase 2, TTR, TTR1, GLRX2, GRX2, GRX-2, GLRX-2, Glutaredoxin 2. |
