Synonyms Thioltransferase, Glutathione-dependent oxidoreductase 2, TTR, TTR1, GLRX2, GRX2, GRX-2, GLRX-2, Glutaredoxin 2.
Introduction 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.
Description 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.
Source Escherichia Coli.
Physical Appearance Sterile Filtered clear colorless solution.
Formulation Glutaredoxin-2 solution contains 25mM Tris-HCl pH-7.5 & 0.01% Na Azide.
Stability 1 week at 2-10°C. For long term store at -20 to -80°C.
Purity Purity of GRX2 is greater than 90% as determined by SDS-PAGE.
Applications ELISA, Western Blot, strongly binds to glutathione, reduced and oxidized.
Usage CHI's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.