Human Hexokinase 1/2 Alexa Fluor® 488-conjugated 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 2 (HK2), also known as muscle form hexokinase, localizes to the outer membrane of mitochondria and is present in adipose tissue, skeletal muscle, and heart (4). The amino acids corresponding to the mitochondrial binding domain (5) have been removed in the recombinant enzyme. Like Hexokinase 1 (HK1), HK2 contains two homologous halves that may have evolved from an ancestral hexokinase through gene duplication and tandem ligation (6). Unlike HK1, in HK2 both the C-terminal and N-terminal portions are catalytically active with the N-terminal half having higher activity than the C-terminal half (7). In HK2 both the N-terminal and C-terminal halves exhibit product inhibition. HK2 overexpression is required for tumor growth making HK2 an attractive oncotarget (4). The enzymatic activity of recombinant human HK2 is measured using a phosphatase-coupled method (8).

Product Datasheets

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