2‑Phosphoglycerate (2-PG) links glycolytic ATP generation to carbon flow and serine biosynthesis via 3‑phosphoglycerate. Its steady‑state level is set by phosphoglycerate mutase, which converts 3‑phosphoglycerate to 2‑PG, and enolase, which dehydrates 2‑PG to phosphoenolpyruvate (PEP). The steady-state concentration of 2-PG reflects the balance between glycolytic ATP production and demands of downstream pathways like the TCA cycle. Pathophysiology associated with 2-PG is reflected in enolase dysregulation. Enolase deficiency compromises conversion of 2‑PG to PEP, leading to impaired ATP production in tissues heavily reliant on glycolysis. In red blood cells this can cause hemolytic anemia and in skeletal muscle, glycogen storage disease type XIII, with exercise intolerance, myalgia, muscle weakness, elevated creatine kinase, and increased glycogen. Since enolase is present in most cell types, defects can exacerbate stress in hypoxic or highly glycolytic tissues such as brain, myocardium, and tumors. Conversely, high enolase activity/rapid 2‑PG turnover are indicative of Warburg‑type metabolic reprogramming seen in cancer, where increased glycolysis supports biosynthesis and redox balance. AkrivisBio’s 2-Phosphoglycerate Assay is a simple, sensitive way to measure 2-PG in a variety of sample types with a detection limit below 20 pmol.
