PFKM Antibody / Phosphofructokinase muscle type, 100 ug

PFKM antibody detects Phosphofructokinase, muscle type, a key glycolytic enzyme that catalyzes the phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate. The UniProt recommended name is ATP-dependent 6-phosphofructokinase, muscle type (PFKM). This enzyme controls a rate-limiting step in glycolysis and is a central regulator of glucose metabolism and energy production in muscle tissue.

Functionally, PFKM antibody identifies a 780-amino-acid cytosolic enzyme that forms homo- or heterotetramers with other phosphofructokinase isoforms (PFKL and PFKP). PFKM activity is allosterically regulated by ATP, citrate, AMP, and fructose-2,6-bisphosphate, allowing fine-tuned control of glycolytic flux according to cellular energy status. Its catalytic action commits glucose to the glycolytic pathway, linking energy demand with carbohydrate metabolism.

The PFKM gene is located on chromosome 12q13.11 and is predominantly expressed in skeletal and cardiac muscle. It plays a vital role in maintaining muscle energy supply during contraction. PFKM expression and activity adapt to metabolic cues, hypoxia, and hormonal regulation, integrating glycolysis with systemic energy homeostasis.

Pathologically, mutations in PFKM cause Glycogen storage disease type VII (Tarui disease), characterized by exercise intolerance, muscle cramps, and myoglobinuria. Deficiency leads to impaired glycolytic ATP production and accumulation of glycogen in muscle fibers. Aberrant PFKM regulation is also associated with metabolic disorders and tumor glycolysis (Warburg effect). Research with PFKM antibody supports studies in metabolism, enzymology, and inherited myopathies.

PFKM antibody is suitable for western blotting, immunohistochemistry, and enzyme assays to detect muscle phosphofructokinase expression. NSJ Bioreagents provides validated PFKM antibody reagents optimized for glycolysis, muscle physiology, and metabolic disease research.

Structurally, Phosphofructokinase, muscle type forms a tetrameric enzyme with alternating catalytic and regulatory domains. Allosteric binding sites modulate its conformational state and enzymatic efficiency. This antibody allows detailed analysis of PFKM's contribution to energy metabolism and metabolic control.