Monoclonal Anti-GCK, (C-terminal) antibody produced in mouse

Glucose is phosphorylated to glucose-6-phosphate by glucokinases. The main function of glucokinase (GCK) is to regulate carbohydrate metabolism. The enzyme triggers the release of insulin in β-cells of pancreas. It can be useful for studies including enzyme kinetics, activator screening and kinase selectivity. Mutation in the gene encoding this protein is associated with a rare form of diabetes and the protein may also have a role in type 2 diabetes.

Hexokinases phosphorylate glucose to produce glucose-6-phosphate, the first step in most glucose metabolism pathways. Alternative splicing of this gene results in three tissue-specific forms of glucokinase, one found in pancreatic islet beta cells and two found in liver. The protein localizes to the outer membrane of mitochondria. In contrast to other forms of hexokinase, this enzyme is not inhibited by its product glucose-6-phosphate but remains active while glucose is abundant. Mutations in this gene have been associated with non-insulin dependent diabetes mellitus (NIDDM), maturity onset diabetes of the young, type 2 (MODY2) and persistent hyperinsulinemic hypoglycemia of infancy (PHHI). (provided by RefSeq)

GCK (AAH01890.1, 356 a.a. ~ 465 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.

Sequence
GLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFKERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACKKACMLGQ

Solution in phosphate buffered saline, pH 7.4