GLRX2 Human

GLRX2 is a 15 kDa mitochondrial thiol transferase that contains an N-terminal mitochondrial targeting signal and a CSYC (Cys-Ser-Tyr-Cys) motif . There are two isoforms of GLRX2: GRX2a and GRX2b. GRX2a is targeted to mitochondria, while GRX2b is predicted to be localized in the nucleus .

GLRX2 catalyzes the formation and glutathionylation of disulfide bonds in proteins, particularly complex I. This reversible process is essential for maintaining the equilibrium between the mitochondrial glutathione pool and protein thiols, thereby regulating the mitochondrial response to redox signals and oxidative stress . Unlike GRX1, GRX2 is not inhibited by the oxidation of structural cysteine residues and can receive electrons from both glutathione (GSH) and thioredoxin reductase, supporting both monothiol and dithiol reactions .

GLRX2 is involved in the cellular response to apoptotic stimuli and oxidative stress at the mitochondrial checkpoint . It has been used in various biochemical assays, including the 2-oxoglutarate dehydrogenase (Ogdh) activity reaction . The enzyme’s ability to catalyze reversible protein glutathionylation/deglutathionylation under varying GSH/GSSG ratios makes it a valuable tool in studying redox biology and mitochondrial function .

Human recombinant GLRX2 is typically produced in Escherichia coli (E. coli) and is available in various forms, including a non-glycosylated polypeptide chain containing 154 amino acids with a molecular mass of 17 kDa . The recombinant protein is often fused to a His tag at the C-terminus for purification purposes .

Recombinant GLRX2 is supplied as a solution in a buffer containing Tris-HCl, PMSF, and glycerol. It should be stored at 4°C for short-term use and at -20°C for long-term storage. To prevent degradation, it is recommended to add a carrier protein and avoid multiple freeze-thaw cycles .