PGK2 Human, Active

The human recombinant form of PGK2 is typically produced in Escherichia coli and is a single, non-glycosylated polypeptide chain containing 437 amino acids, with a molecular mass of approximately 46.9 kDa . The recombinant protein often includes a His tag at the N-terminus to facilitate purification .

PGK2 is essential for energy production in sperm cells, where it catalyzes a key step in glycolysis. The enzyme’s specific activity is measured by its ability to convert 1 micromole of 1,3-bisphosphoglycerate to 3-phosphoglycerate per minute at pH 8.0 and 37°C . This activity is crucial for maintaining the energy balance required for sperm motility and fertility.

Recombinant PGK2 is used in various biochemical and physiological studies to understand its role in energy metabolism and its potential implications in male fertility. It is also employed in research focused on glycolytic enzymes and their regulation.

The recombinant PGK2 protein is typically stored in a buffer containing 20 mM Tris-HCl (pH 8.0), 20% glycerol, 0.1 M sodium chloride, and 1 mM dithiothreitol (DTT). For long-term storage, it is recommended to aliquot and store the protein at -20°C to -80°C to avoid repeated freeze-thaw cycles .

The purity of recombinant PGK2 is usually greater than 95%, as determined by SDS-PAGE under reducing conditions and visualized by Coomassie blue staining . This high level of purity ensures the reliability and reproducibility of experimental results.