PGK1 Recombinant Rabbit mAb

PGK1 (phosphoglycerate kinase 1) is a key metabolic enzyme in the glycolytic pathway, encoded by the PGK1 gene. It catalyzes the reversible transfer of a phosphate group between 1,3-bisphosphoglycerate and ADP in the cytoplasm, generating 3-phosphoglycerate and ATP—this constitutes the first ATP-producing step in glycolysis, playing an indispensable role in maintaining the cellular supply of energy currency. This protein belongs to the phosphoglycerate kinase family and features a typical two-domain three-dimensional structure connected by a hinge region, undergoing conformational changes upon substrate binding to achieve catalytic function. It is also an evolutionarily highly conserved enzyme, with homologs found in virtually all organisms. Beyond its classical metabolic function, PGK1 also possesses non-enzymatic functions, such as acting as an angiogenic factor when secreted extracellularly or participating in the regulation of fibrinolysis by binding to cell surface receptors. In tumor biology, PGK1 expression is often upregulated by HIF-1α-mediated hypoxic responses, thereby enhancing the glycolytic capacity of tumor cells to adapt to the hypoxic microenvironment, and its overexpression is closely associated with poor prognosis in various cancers (including liver, gastric, and lung cancers). Furthermore, defects or mutations in the PGK1 gene can lead to phosphoglycerate kinase deficiency, a rare X-linked recessive disorder in which patients primarily present with hemolytic anemia, rhabdomyolysis, and neurological dysfunction (such as epilepsy and ataxia), reflecting the multiple important roles of this protein in erythrocyte energy metabolism, muscle contractile function, and neuronal activity maintenance.