Recombinant Mouse Acetylcholinesterase/ACHE Protein, CF

The classical role of ACHE is to terminate cholinergic neurotransmission by hydrolysis of acetylcholine (ACH) (1). ACHE is thought to be involved in the pathology of Alzheimer's 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 (2). Its involvement in the cholinergic anti-inflammatory pathway connects ACHE with a possible marker of low-grade systemic inflammation in obesity, hypertension, coronary heart disease, and AD (3). Alternative splicing produces three isoforms: an amphipathic form that exists as both monomeric and mutimeric forms, a soluble-monomeric form lacking the cysteine residue near the C-terminus, and a GPI-anchored dimeric form found in the membranes of erythrocytes (1). The recombinant mouse ACHE (rmACHE) was expressed as the amphipathic form that consists of soluble monomer and mutimeric forms.