GSR, 43-522aa, Human, His tag, E.coli (Bioactivity Validated)
Description
Purity: > 95% by SDS - PAGE Format: Liquid. In 20mM Tris-HCl buffer (pH 8.0) containing 1mM DTT, 10% glycerol, 0.1M NaCl. Glutathione reductase, also known as GSR, is a member of the class-I pyridine nucleotide-disulfide oxidoreductase family. This enzyme is a homodimeric flavoprotein and plays a role in maintaining glutathione (GSH) in its reduced form by catalyzing the reduction of glutathione disulfide (GSSG): GSSG + NADPH + H+ ->2GSH + NADP+. In most eukaryotic cells, GSR maintains the ratio of [GSH] / [GSSG], and participates in several vital functions such as the detoxification of reactive oxygen species as well as protein and DNA biosynthesis. Recombinant human GSR protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.