Active Recombinant Human Phosphoglucose Isomerase

PGI is a cytosolic enzyme that belongs to the isomerase class and catalyzes the reversible interconversion of glucose-6-phosphate and fructose-6-phosphate. It plays a central role in both glycolysis and gluconeogenesis. In addition to its intracellular metabolic function, PGI is also known to function extracellularly as a cytokine-like protein, including roles as autocrine motility factor (AMF) and neuroleukin, highlighting its multifunctional (“moonlighting”) properties.

Phosphoglucose isomerase has been used in:

• Glycolysis and metabolic pathway studies
• Enzyme kinetics and activity assays
• Cancer metabolism and cell migration studies
• Functional studies of metabolic enzymes

PGI catalyzes the isomerization of glucose-6-phosphate to fructose-6-phosphate, a critical step in glycolysis. In addition to its metabolic role, it has extracellular signaling functions associated with tumor cell motility and growth regulation.

Centrifuge the vial at 4ºC before opening to recover the entire contents. It is recommended that sterile water be added to the vial to prepare a stock solution.

Lyophilized from 10mM KPB (pH 8.0), 0.150M NaCl

Centrifuge the vial at 4ºC before opening to recover the entire contents. It is recommended that sterile water be added to the vial to prepare a stock solution.

Unit definition: One enzyme activity unit is defined as the amount of enzyme required to convert 1.0 μmol of D-fructose-6-phosphate to D-glucose-6-phosphate per minute at pH 7.4 and a temperature of 25 °C.