Recombinant Human PGM2 protein is a Human Full Length protein, in the 1 to 612 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE.
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Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Catalyzes the conversion of the nucleoside breakdown products ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses (PubMed:17804405). Catalyzes the reversible isomerization of alpha-D-glucose 1-phosphate to alpha-D-glucose 6-phosphate but with a lower catalytic efficiency (PubMed:17804405). The mechanism proceeds via the intermediate compound alpha-D-glucose 1,6-bisphosphate (PubMed:17804405). In vitro, has also a low glucose 1,6-bisphosphate synthase activity which is most probably not physiologically relevant (PubMed:17804405, PubMed:18927083).
MSTP006, PGM2, Phosphopentomutase, Glucose phosphomutase 2, Phosphodeoxyribomutase, Phosphoglucomutase-2
Recombinant Human PGM2 protein is a Human Full Length protein, in the 1 to 612 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE.
pH: 7.4
Constituents: 90% PBS, 10% Glycerol (glycerin, glycerine)
purified by using conventional chromatography techniques
Catalyzes the conversion of the nucleoside breakdown products ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses (PubMed:17804405). Catalyzes the reversible isomerization of alpha-D-glucose 1-phosphate to alpha-D-glucose 6-phosphate but with a lower catalytic efficiency (PubMed:17804405). The mechanism proceeds via the intermediate compound alpha-D-glucose 1,6-bisphosphate (PubMed:17804405). In vitro, has also a low glucose 1,6-bisphosphate synthase activity which is most probably not physiologically relevant (PubMed:17804405, PubMed:18927083).
Belongs to the phosphohexose mutase family.
Phosphoglucomutase 2 also known as PGM2 is an enzyme involved in carbohydrate metabolism. It catalyzes the reversible conversion of glucose-1-phosphate to glucose-6-phosphate an essential step in glycogenesis and glycogenolysis. PGM2 has a mass of about 65 kDa and is expressed in various tissues including liver muscle and brain. It is often expressed in cells that require significant amounts of energy due to its role in glucose utilization.
PGM2 functions to maintain cellular energy balance by supporting glycogen storage and breakdown. It operates as an individual enzyme not being part of any multi-enzyme complex but it significantly impacts glucose flux within cells. The enzyme plays a role in both anabolic and catabolic processes highlighting its importance in energy homeostasis. Adequate functioning of PGM2 ensures that cells have access to glucose during fasting or between meals vital for processes like muscle contraction and brain function.
PGM2 is actively involved in the glycogen metabolism pathway and interacts with key enzymes like glycogen phosphorylase and glycogen synthase. Its enzymatic activity links it to pathways such as glycolysis where glucose-6-phosphate serves as a substrate. Through its role in glucose conversion PGM2 influences the availability of substrate for additional enzymes in glycolysis and glycogenesis impacting energy production and storage in cells.
Defects in PGM2 have been associated with glycogen storage disease which affects glucose and glycogen metabolism leading to energy production issues. It is also observed in metabolic myopathies where disordered energy metabolism leads to muscle weakness and fatigue. PGM2 interacts with glycogen phosphorylase in these disorders as both play parts in the conversion of glucose-1-phosphate to glucose-6-phosphate implicating their coordination in maintaining metabolic stability.
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15% SDS Page analysis of ab201877 (3μg).
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