Phosphoglycerate Kinase Activity Assay Kit (Colorimetric) ab252890 provides a quick and easy way for monitoring PGK activity in various samples.
Individual kit components also available for purchase with a minimum order of 20 units. Contact us to discuss your needs.
Application | Reactivity | Dilution info | Notes |
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Catalyzes one of the two ATP producing reactions in the glycolytic pathway via the reversible conversion of 1,3-diphosphoglycerate to 3-phosphoglycerate (PubMed:30323285, PubMed:7391028). In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein) (PubMed:2324090). May play a role in sperm motility (PubMed:26677959).
PGKA, MIG10, OK/SW-cl.110, PGK1, Phosphoglycerate kinase 1, Cell migration-inducing gene 10 protein, Primer recognition protein 2, PRP 2
Phosphoglycerate Kinase Activity Assay Kit (Colorimetric) ab252890 provides a quick and easy way for monitoring PGK activity in various samples.
Individual kit components also available for purchase with a minimum order of 20 units. Contact us to discuss your needs.
Phosphoglycerate Kinase Activity Assay Kit (Colorimetric) ab252890 provides a quick and easy way for monitoring PGK activity in various samples. In the first step of this enzymatic assay, PGK converts 3-Phosphoglycerate and ATP to 1,3-Bisphosphoglycerate and ADP. The nascent intermediate is detected via a series of enzymatic reactions that lead the oxidation of NADH to NAD , which can be easily detected (OD= 340 nm). The assay is simple, sensitive and can detect Phosphoglycerate Kinase Activity lower than 50 mU in variety of samples.
This product is manufactured by BioVision, an Abcam company and was previously called K194 Phosphoglycerate Kinase Activity Assay Kit (Colorimetric). K194-100 is the same size as the 100 test size of ab252890.
The Safety Datasheet for this product has been updated for certain countries. Please check the current version in the Support and downloads section.
PGK1 also known as phosphoglycerate kinase-1 is an enzyme involved in glycolysis with a mass of approximately 45 kDa. PGK1 catalyzes the reversible transfer of a phosphate group from 13-bisphosphoglycerate to ADP forming 3-phosphoglycerate and ATP. This enzyme is expressed ubiquitously across various tissues with significant roles in energy metabolism. In yeast it is referred to simply as phosphoglycerate kinase where its function in cellular respiration is widely studied.
The PGK1 protein plays an essential role in energy production by participating in the glycolytic pathway. This enzyme functions independently and is not part of any complex. By converting 13-bisphosphoglycerate to 3-phosphoglycerate it supports cellular processes that require ATP. Such activity facilitates the high energy needs of cells ensuring proper cellular function and homeostasis.
The enzyme PGK1 operates predominantly within the glycolytic and gluconeogenesis pathways. Throughout glycolysis it partners with enzymes like phosphofructokinase and pyruvate kinase facilitating the breakdown of glucose into pyruvate while generating ATP. In gluconeogenesis PGK1 aids in glucose formation which helps balance energy dynamics particularly in tissues like the liver and kidney.
PGK1 has associations with tumor growth and proliferation in various cancers. Its elevated expression is often found in tumors linking it to oncogenesis due to the increased demand for glycolytic activity. Additionally mutations in PGK1 can result in phosphoglycerate kinase deficiency a disorder affecting red blood cell metabolism. This links it to related proteins involved in managing metabolic pathways of energy production in affected tissues.
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Relative PGK Activity was calculated in lysates prepared from rat liver (2 μg), rat muscle (0.5 μg), HeLa (Human epithelial cell line from cervix adenocarcinoma) (1.5 μg) and Jurkat (Human T cell leukemia cell line from peripheral blood) (1.5 μg).
Kinetic measurement of Phosphoglycerate Kinase activity from various samples.
NADH standard curve.
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