Butyrylcholinesterase (human, recombinant)

Butyrylcholinesterase (BChE) is a serine hydrolase that preferentially hydrolyzes butyrylcholine (BCh) but can also hydrolyze acetylcholine (ACh). It is composed of a large catalytic domain and C-terminal tetramerization domain. BChE can exist as a monomer but primarily oligomerizes into soluble or membrane-anchored tetramers by combining with polyproline-rich peptides, such as lamellipodin. It is widely expressed with high levels in the plasma, liver, lungs, and brain. In addition to its hydrolysis of BCh and ACh, BChE also hydrolyzes certain ester-containing exogenous substances. Due to this, loss-of-function mutations in BCHE are associated with the accumulation of exogenous BChE substrates, including the muscle relaxant succinylcholine (Cay-32829), which can lead to adverse effects such as prolonged apnea. BChE is implicated in the regulation of the peptide hormone ghrelin, and dysregulation of BChE is found in various conditions, including Alzheimer's disease, where it is found in amyloid-beta plaques and neurofibrillary tangles, and sudden infant death syndrome (SIDS), where it is found at reduced levels in infant dried blood spots. Cayman's Butyrylcholinesterase (human, recombinant) protein can be used for enzyme activity assays.