Phosphoglycerate Kinase 1 (PGK1) is a crucial enzyme in the glycolytic pathway, playing a significant role in cellular metabolism. It catalyzes the reversible conversion of 1,3-bisphosphoglycerate (1,3-BPG) to 3-phosphoglycerate (3-PG), generating one molecule of ATP in the process . This enzyme is ubiquitously expressed in all cells and is essential for energy production.
PGK1 is a monomeric enzyme with a molecular weight of approximately 45 kDa . It belongs to the phosphoglycerate kinase family and is encoded by the PGK1 gene located on the X chromosome . The enzyme’s structure includes two domains that facilitate its catalytic activity. The N-terminal domain binds to 1,3-BPG, while the C-terminal domain binds to ADP, enabling the transfer of a phosphate group to form ATP .
PGK1 is not only pivotal in glycolysis but also plays roles in other cellular processes. It has been reported to exhibit thiol reductase activity on plasmin, leading to the formation of angiostatin, which inhibits angiogenesis and tumor growth . Additionally, PGK1 is involved in DNA replication and repair within mammalian cell nuclei . Its expression is upregulated in various cancers, making it a potential target for cancer therapy .
Mouse anti-human PGK1 antibodies are monoclonal antibodies designed to specifically bind to the human PGK1 protein. These antibodies are commonly used in various research applications, including Western blotting (WB), immunohistochemistry (IHC), and enzyme-linked immunosorbent assay (ELISA) . They are valuable tools for studying PGK1 expression, localization, and function in different biological contexts.