Glucokinase (GK), also known as hexokinase IV, is a critical enzyme in glucose homeostasis, primarily expressed in pancreatic β-cells and hepatocytes. It catalyzes the phosphorylation of glucose to glucose-6-phosphate, serving as a glucose sensor to regulate insulin secretion and hepatic glucose metabolism. Antibodies targeting glucokinase are essential tools for studying its expression, localization, and function in metabolic tissues. These antibodies are widely used in techniques such as Western blotting, immunohistochemistry (IHC), and immunofluorescence (IF) to investigate GK's role in diabetes, particularly in maturity-onset diabetes of the young type 2 (MODY2), linked to GK gene mutations.
Glucokinase antibodies are typically raised against specific epitopes of the enzyme, often derived from recombinant human or rodent GK proteins. They enable researchers to assess tissue-specific GK expression levels, which can vary under different metabolic conditions, such as fasting or hyperglycemia. Validation of these antibodies includes testing in knockout models or siRNA-treated cells to confirm specificity. Commercially available GK antibodies may differ in clonality (monoclonal or polyclonal), species reactivity, and applications, requiring careful selection based on experimental needs. Their use has advanced understanding of GK's regulatory mechanisms and potential therapeutic targets for diabetes and metabolic disorders.