G6PD Human
Hi-5 cells.
Description
G6PD Human Recombinant produced in Hi-5 cells is a single polypeptide chain containing 535 amino acids (1-515) and having a molecular mass of 61.4kDa.
G6PD is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Hi-5 cells.
Product Science Overview
G6PD plays a significant role in various cellular processes:
- Biosynthesis: NADPH generated by G6PD is used in the synthesis of fatty acids, cholesterol, and nucleotides .
- Redox Homeostasis: NADPH is crucial for maintaining the reducing environment of the cell, which is necessary for detoxifying reactive oxygen species (ROS) .
- Protection Against Oxidative Stress: In erythrocytes, G6PD is the sole source of NADPH, which is essential for the regeneration of reduced glutathione, a critical antioxidant .
G6PD deficiency is the most common human enzymopathy, affecting approximately 400 million people worldwide . This X-linked genetic disorder results from mutations in the G6PD gene, leading to reduced enzyme activity. The deficiency can cause a range of clinical manifestations, from asymptomatic individuals to those with severe conditions such as neonatal jaundice, acute hemolysis, or chronic nonspherocytic hemolytic anemia .
Recombinant human G6PD is produced using genetic engineering techniques to study the enzyme’s structure, function, and the effects of various mutations. This approach allows for the detailed characterization of G6PD variants and their role in disease . For instance, studies have shown that mutations, regardless of their distance from the active site, can significantly affect the enzyme’s catalytic properties and stability .
The refolding of recombinant human G6PD is a complex process influenced by various chemical and physical factors. Key players in this process include L-arginine, NADP+, and dithiothreitol (DTT), which help prevent aggregation and promote proper folding . The refolding process is relatively slow, taking about seven days to complete at room temperature .
Understanding the folding and stability of G6PD is crucial for developing treatments for G6PD deficiency. The ability to produce recombinant G6PD with high recovery yield and unaltered properties paves the way for future studies on clinical mutants with folding defects . This knowledge can also provide insights into the folding process of other oligomeric proteins.
