Human Hexokinase 1/2 Antibody

Applications

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Preparation and Storage

Background: Hexokinase 1/2

Hexokinases phosphorylate hexose to form hexose 6-phosphate, the first step in hexose metabolism (1). Phosphorylation of a hexose adds charge to molecule thereby making it difficult to transport out of a cell. The hexose is therefore retained for intracellular metabolic processes, such as glycolysis or glycogen synthesis. In most organisms, glucose is the most important substrate of hexokinases and glucose-6-phosphate is the most important product. There are four mammalian hexokinases (2). Hexokinase 1, 2 and 3 are referred to as high-affinity hexokinases because their Km for glucose is below 1 mM. Hexokinase 4 is specific for glucose and is also referred to as glucokinase (3). Hexokinase I localizes to the outer membrane of mitochondria and is found in all mammalian tissues. The amino acids involved in mitochondrion membrane localization (4) have been removed in the recombinant enzyme. Hexokinase 1 (HK1) contains two homologous halves that are believed to be evolved from a single ancestral hexokinase by gene duplication and fusion (5). While the regulatory function is associated with the N-terminal half, the catalytic site is associated with the C-terminal half. HK1 is insensitive to product inhibition (6). Mutation in the active site of human hexokinase is associated with hexokinase deficiency and severe nonspherocytic hemolytic anemia (7). The enzymatic activity of recombinant human HK1 is measured using a phosphatase-coupled method (8).

Product Datasheets

Product Specific Notices

Related Research Areas

• Bcl-2 Proteins and Regulators
• Glucose Homeostasis
• Glycobiology-related Enzymes
• HIF Transcription Factors
• Intracellular Kinases
• Mitochondrial Proteins