Recombinant Human Glucokinase protein is a Human Full Length protein, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE.
| Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
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Catalyzes the phosphorylation of hexose, such as D-glucose, D-fructose and D-mannose, to hexose 6-phosphate (D-glucose 6-phosphate, D-fructose 6-phosphate and D-mannose 6-phosphate, respectively) (PubMed:11916951, PubMed:15277402, PubMed:17082186, PubMed:18322640, PubMed:19146401, PubMed:25015100, PubMed:7742312, PubMed:8325892). Compared to other hexokinases, has a weak affinity for D-glucose, and is effective only when glucose is abundant (By similarity). Mainly expressed in pancreatic beta cells and the liver and constitutes a rate-limiting step in glucose metabolism in these tissues (PubMed:11916951, PubMed:15277402, PubMed:18322640, PubMed:25015100, PubMed:8325892). Since insulin secretion parallels glucose metabolism and the low glucose affinity of GCK ensures that it can change its enzymatic activity within the physiological range of glucose concentrations, GCK acts as a glucose sensor in the pancreatic beta cell (By similarity). In pancreas, plays an important role in modulating insulin secretion (By similarity). In liver, helps to facilitate the uptake and conversion of glucose by acting as an insulin-sensitive determinant of hepatic glucose usage (By similarity). Required to provide D-glucose 6-phosphate for the synthesis of glycogen (PubMed:8878425). Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate (PubMed:7742312).
Hexokinase-4, HK4, Glucokinase, Hexokinase type IV, Hexokinase-D, HK IV, GCK
Recombinant Human Glucokinase protein is a Human Full Length protein, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE.
pH: 7.9
Constituents: 20% Glycerol (glycerin, glycerine), 0.75% Potassium chloride, 0.316% Tris HCl, 0.0154% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.00584% EDTA
ab82190 is greater than 95% homogeneous based on SDS-PAGE analysis, purified by affinity and FPLC chromatography.
Catalyzes the phosphorylation of hexose, such as D-glucose, D-fructose and D-mannose, to hexose 6-phosphate (D-glucose 6-phosphate, D-fructose 6-phosphate and D-mannose 6-phosphate, respectively) (PubMed:11916951, PubMed:15277402, PubMed:17082186, PubMed:18322640, PubMed:19146401, PubMed:25015100, PubMed:7742312, PubMed:8325892). Compared to other hexokinases, has a weak affinity for D-glucose, and is effective only when glucose is abundant (By similarity). Mainly expressed in pancreatic beta cells and the liver and constitutes a rate-limiting step in glucose metabolism in these tissues (PubMed:11916951, PubMed:15277402, PubMed:18322640, PubMed:25015100, PubMed:8325892). Since insulin secretion parallels glucose metabolism and the low glucose affinity of GCK ensures that it can change its enzymatic activity within the physiological range of glucose concentrations, GCK acts as a glucose sensor in the pancreatic beta cell (By similarity). In pancreas, plays an important role in modulating insulin secretion (By similarity). In liver, helps to facilitate the uptake and conversion of glucose by acting as an insulin-sensitive determinant of hepatic glucose usage (By similarity). Required to provide D-glucose 6-phosphate for the synthesis of glycogen (PubMed:8878425). Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate (PubMed:7742312).
Belongs to the hexokinase family.
Glucokinase also known as GCK is an enzyme with a mass around 50 kDa. It functions by catalyzing the phosphorylation of glucose to glucose-6-phosphate an important step in glycolysis. Glucokinase displays a higher affinity for glucose as compared to other hexokinases which is indicated by its specific kinetic property known as the Km value. This enzyme is mainly expressed in the liver and pancreatic beta-cells where it plays an important role in glucose metabolism. Additionally glucokinase can also be found in the hypothalamus indicating its broader reach in carbohydrate sensing.
Glucokinase acts as a glucose sensor regulating blood sugar levels and insulin secretion. This process does not involve the enzyme as part of a larger complex. Instead glucokinase functions independently to sense glucose concentrations and adjusts the rate of glucose phosphorylation accordingly. Its activity significantly affects the balance of glucose uptake and energy production especially during postprandial states when glucose levels rise. Glucokinase activity is therefore important to maintaining glucose homeostasis.
Glucokinase plays a central role in the glycolytic pathway and interacts with the insulin signaling pathway. Within these pathways it influences how the liver stores glucose as glycogen and controls insulin release from pancreatic beta-cells. Glucokinase activity is modulated by glucose levels and is closely related to insulin receptor substrates that affect downstream insulin signaling. Its function is important for the proper regulation of these pathways linking glucose sensing with metabolic control in varied tissues.
Glucokinase is pivotal in the context of diabetes mellitus and hyperglycemia. Mutations or dysregulation of glucokinase can lead to different forms of diabetes including maturity-onset diabetes of the young type 2 (MODY2). Glucokinase inhibitors and activators are being explored as potential therapeutic agents for modulating glucose levels in diabetics. Additionally its role interfaces with the functions of insulin tying glucokinase closely to conditions of insulin resistance and pancreatic dysfunction. Understanding these connections is instrumental for developing targeted treatment strategies.
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