Anti-PGK1

0.5mg/ml if reconstituted with 0.2ml sterile DI water. Phosphoglycerate Kinase 1, also known as PGKA, is an enzyme that in humans is encoded by the PGK1 gene. Willard et al.(1985) used a cDNA for human PGK to map the functional PGK1 gene to Xq13. Disulfide bonds in secreted proteins are considered to be inert because of the oxidizing nature of the extracellular milieu. An exception to this rule is a reductase secreted by tumor cells that reduces disulfide bonds in the serine proteinase plasmin. Lay et al.(2000) showed that the plasmin reductase isolated from conditioned medium of fibrosarcoma cells is the glycolytic enzyme phosphoglycerate kinase. Recombinant phosphoglycerate kinase had the same specific activity as the fibrosarcoma-derived protein. Plasma of mice bearing fibrosarcoma tumors contained several-fold more phosphoglycerate kinase, as compared with mice without tumors. Protein function: In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein). [The UniProt Consortium]