Acetylcholinesterase (human, recombinant)

Acetylcholinesterase (AChE) is a highly conserved homotetrameric carboxylesterase that is composed of four ~70 kDa subunits with each subunit containing a single active site. It is a product of alternative splicing and can be membrane bound via a glycosyl-phosphatidylinositol anchor in the membrane or a proline-rich membrane anchor (PRIMA) peptide linker for erythrocyte and synaptic AChE, respectively, or soluble in water, with each form demonstrating identical catalytic activity. AChE is primarily found in red blood cells as well as at neuromuscular junctions and in the brain at cholinergic synapses where it hydrolyzes acetylcholine to acetate and choline to terminate synaptic transmission. It accelerates amyloid-beta (Abeta) fibrillogenesis in vitro and overexpression of AChE accelerates Abeta plaque formation and disease progression in the Tg2576 transgenic mouse model of Alzheimer's disease. AChE activity is also increased in islets of Langerhans in rats with diabetes induced by streptozotocin (Cay-13104). Cayman's Acetylcholinesterase (human, recombinant) protein can be used for ELISA, enzymatic activity assay, and Western blot (WB) applications.CAS Number: 9000-81-1. Synonyms: Acetylcholinesterase (YT Blood Group), Acetylcholinesterase (Cartwright Blood Group), AChE, AcChoEase, ARACHE, EC 3.1.1.7. Purity: >95% estimated by SDS-PAGE. Source: Active recombinant human C-terminal His-tagged AChE expressed in Expi293F(TM) cells. Amino Acids: 1-614 (full length). MW: 68.76 kDa. Formulation: (Request formulation change), 50 mM HEPES, pH 7.6, with 150 mM sodium chloride. UniProt Accession #: P22303.