Recombinant human Acetylcholinesterase/ACHE protein

ACHE, also known as Acetylcholinesterase, is a member of the type-B carboxylesterase/lipase family. It is an enzyme that catalyzes the breakdown of acetylcholine and of some other choline esters that function as neurotransmitters. During neurotransmission, ACH is released from the presynaptic neuron into the synaptic cleft and binds to ACH receptors on the post-synaptic membrane, relaying the signal from the nerve. ACHE, also located on the post-synaptic membrane, terminates the signal transmission by hydrolyzing ACH. This protein is thought to be involved in the pathology of Alzheimers disease (AD) by accelerating the assembly of A beta peptides into fibrillar species through forming complexes with A beta via the peripheral anionic site on ACHE. ACHE inhibitors have been used to delay symptoms of AD patients by virtue of their ability to enhance ACH availability, as well as reduce amyloidogenesis and subsequent neurotoxicity. Recombinant human ACHE, fused to His-tag at C-terminus, was expressed in HEK293 cell and purified by using conventional chromatography techniques.