Glutaredoxin 2 (human, recombinant)

Glxr2|Grx2|Thioltransferease 2|TTF2

Glutaredoxin 2 (Grx2) is a thiol-disulfide oxidoreductase and member of the thioredoxin family encoded by GLRX2 with a role in the maintenance of cellular thiol redox homeostasis.{53968,53969} Alternative splicing of GLRX2 produces three ubiquitously expressed isoforms, Grx2a, Grx2b, and Grx2c, with Grx2a localized to the mitochondria and Grx2b and Grx2c in the cytoplasm and nucleus. It is a dithiol Grx that contains two active site cysteine residues and catalyzes the glutathione-dependent reduction of disulfides, acting as an electron donor for ribonucleotide or sulfate reduction, and regulating protein levels of glutathione mixed disulfides.{53969} In its inactive state, Grx2 is a homodimer linked by a single [2Fe-2S] cluster, which acts as a redox sensor that drives monomerization and activation of Grx2 under conditions of oxidative stress, such as free radical formation or oxidation of the glutathione (GSH) pool.{53969,53970,53971} The oxidized active site in Grx2 is reduced by GSH and, unlike other eukaryotic Grxs, is also a substrate for thioredoxin reductase (TrxR). Grx2 catalyzes the reversible glutathionylation of mitochondrial complex I to regulate superoxide production and facilitates the reduction of protein disulfides, glutathionylated proteins, and other low molecular weight substrates under conditions of oxidative stress.{57138} Knockdown or overexpression of GLRX2 enhances and reduces, respectively, oxidative stress-induced apoptosis in HeLa cells. Glrx2 knockdown increases high-fat diet-induced insulin resistance, hippocampal inflammation, increases in body weight, and cognitive dysfunction in mice.{53972} Cayman’s Glutaredoxin 2 (human, recombinant) protein can be used for enzyme activity assays.

-80

-80

50 mM Tris-HCl, pH 7.8, with 150 mM sodium chloride, 1 mM EDTA, 10% glycerol, and 0.1 mM DTT

365

≥95% estimated by SDS-PAGE