GLRX5 Human

Glutaredoxin 5 is composed of approximately 100 amino acids and utilizes glutathione as a cofactor. The human recombinant form of GLRX5 is typically expressed in Escherichia coli and is purified to a high degree of purity, often exceeding 85% . The recombinant protein is usually non-glycosylated and has a molecular mass of around 18.8 kDa .

GLRX5 is involved in the biogenesis of iron-sulfur clusters, which are essential for various cellular processes, including mitochondrial respiration and DNA synthesis . The enzyme receives 2Fe/2S clusters from scaffold proteins and mediates their transfer to apoproteins or the 4Fe/4S cluster biosynthesis machinery . This transfer is crucial for maintaining normal iron homeostasis within the cell.

The enzyme operates by being oxidized by substrates and subsequently reduced non-enzymatically by glutathione . This redox activity is vital for its function in iron-sulfur cluster assembly and maintenance.

GLRX5 is essential for the regulation of hemoglobin synthesis by the iron-sulfur protein ACO1 . Defects in the GLRX5 gene can lead to anemia sideroblastic pyridoxine-refractory autosomal recessive (PRARSA), a condition characterized by defective hemoglobin synthesis .

Recombinant human GLRX5 is widely used in research to study its role in iron-sulfur cluster biogenesis and its implications in various diseases. It is also used in biochemical assays and structural studies to understand its mechanism of action and interaction with other proteins .

The recombinant protein is typically stored at 4°C for short-term use and at -20°C for long-term storage. It is recommended to add a carrier protein to prevent degradation during storage .