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Thioltransferase, GRX, GLRX1, GRX1, GRX-1, GLRX-1, Glutathione-dependent oxidoreductase 1, Glutaredoxin 1.
GRX1 has a glutathione-disulfide oxidoreductase activity in the presence of nadph and glutathione reductase. Reduces low molecular weight disulfides and proteins. Glutaredoxin is a glutathione (GSH)-dependent hydrogen donor for ribonucleotide reductase and also catalyzes glutathione-disulfide oxidoreduction reactions in the presence of NADPH and glutathione reductase. GRX1 is 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.
Glutaredoxin Saccharamyces cerevisiae Recombinant conaining 6x His tag at C-Terminus produced in E.Coli is a single, non-glycosylated, Polypeptide chain having a molecular mass of 16 kDa.
Escherichia Coli.
Sterile Filtered clear colorless solution.
Glutaredoxin solution contains 25mM Tris-HCl pH-7.5 & 0.01% Na Azide.
1 week at 2-10°C. For long term store at -20 to -80°C.
Greater than 90% as determined by SDS-PAGE.
ELISA, Western Blot, strongly binds to glutathione, reduced and oxidized.
ProSpec'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.
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