GLRX1 Human

Glutaredoxin 1 (GRX1), also known as GLRX, is a small redox enzyme that plays a crucial role in cellular redox homeostasis. It belongs to the glutaredoxin family and is involved in various cellular processes, including the reduction of disulfides and the regulation of protein thiol-disulfide balance.

Human Glutaredoxin 1 is a protein consisting of 106 amino acids. It is typically expressed in Escherichia coli for recombinant production. The recombinant form of Glutaredoxin 1 is often tagged with a polyhistidine tag at the N-terminus to facilitate purification . The protein has a molecular mass of approximately 12-13.6 kDa .

Glutaredoxin 1 functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase . It uses glutathione as a cofactor and is involved in the reduction of low molecular weight disulfides and protein disulfides . This activity is essential for maintaining the redox state of the cell and protecting against oxidative stress.

The biological activity of recombinant Glutaredoxin 1 is significant in various biochemical assays. It exhibits glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase . This activity is crucial for reducing disulfides in proteins and maintaining cellular redox balance.

Recombinant Human Glutaredoxin 1 is widely used in research for studying redox biology, oxidative stress, and related cellular processes. It is also utilized in high-throughput screening assays and as a positive control in Western blotting (WB) and SDS-PAGE .

Recombinant Glutaredoxin 1 is typically provided as a lyophilized powder and is stable for up to twelve months when stored at -20°C to -80°C . It is recommended to store the protein under sterile conditions and avoid repeated freeze-thaw cycles to maintain its stability and activity .