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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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Glucokinase, also known as Hexokinase IV or GCK, is a key enzyme that catalyzes the phosphorylation of glucose to glucose-6-phosphate, the first step in the glycolytic pathway. Unlike other hexokinase isoforms, glucokinase displays a lower affinity for glucose and is not inhibited by its product, allowing it to function as an effective glucose sensor in specific tissues. It is predominantly expressed in the liver and pancreatic β-cells, where it plays a vital role in maintaining systemic glucose homeostasis.
In the liver, glucokinase regulates glycogen synthesis and glycolysis in response to elevated blood glucose levels. In pancreatic β-cells, it governs insulin secretion by controlling the rate of glucose metabolism. Mutations or altered regulation of glucokinase are associated with various metabolic disorders, including maturity-onset diabetes of the young (MODY) and persistent hyperinsulinemic hypoglycemia of infancy (PHHI). Given its tissue-specific function and clinical relevance, glucokinase is a valuable biomarker in both basic research and metabolic disease studies.
The Glucokinase antibody is an essential tool for researchers studying glucose metabolism, pancreatic function, and diabetes. With proven performance in immunohistochemistry, western blot, and immunofluorescence, the Glucokinase antibody allows for accurate detection of glucokinase expression in relevant tissues and models. Incorporating the Glucokinase antibody into your workflow provides critical insight into glucose regulation pathways and supports translational research into metabolic disorders.
Optimal dilution of the Glucokinase antibody should be determined by the researcher.
A recombinant human partial protein corresponding to amino acids Y234-T431 was used as the immunogen for the Glucokinase antibody.
After reconstitution, the Glucokinase antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing.
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