Active • Host: Mammalian cells • AA: 1-614 (full length) • Tag: C-terminal His • MW: 68.76 kDa
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Alternative(s)
44687Acetylcholinesterase (eel)
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Acetylcholinesterase (human, recombinant)

Item No. 39956

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
CAS Number
9000-81-1
Synonyms
  • 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 mammalian 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
Host
Mammalian cells
UniProt Accession №
P22303
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    20 µg

    $418

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    Cayman Chemical
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    Product Description

    Acetylcholinesterase (AChE) is a highly conserved homotetrameric carboxylesterase that is composed of four ~70 kDa subunits with each subunit containing a single active site.1,2 It is primarily found at neuromuscular junctions and in the brain at cholinergic synapses, where it hydrolyzes acetylcholine to acetate and choline to terminate synaptic transmission.3,4 AChE can be bound to the extracellular side of the plasma membrane via a proline-rich membrane anchor (PRiMA) on neuronal synapses but can also be linked to the outer membrane of erythrocytes.3 It accelerates amyloid-β (Aβ) fibrillogenesis in vitro, and overexpression of AChE accelerates Aβ plaque formation and disease progression in the Tg2576 transgenic mouse model of Alzheimer's disease.5 AChE activity is also increased in islets of Langerhans in rats with diabetes induced by streptozotocin (Item No. 13104). Cayman's Acetylcholinesterase (human, recombinant) protein can be used for ELISA, enzyme activity assay, and Western blot (WB) applications.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Xu, Y., Colletier, J.P., Weik, M., et al. Flexibility of aromatic residues in the active-site gorge of acetylcholinesterase: X-ray molecular dynamics. Biophys. J. 95(5), 2500-2511 (2008).

    2. Cartaud, J., Rieger, F., Bon, S., et al. Fine structure of electric eel acetylcholinesterase. Brain Res. 88(1), 127-130 (1975).

    3. Stasiuk, M., Janiszewska, A., and Kozubek, A. Phenolic lipids affect the activity and conformation of acetylcholinesterase from Electrophorus electricus (Electric eel). Nutrients 6(5), 1823-1831 (2014).

    4. Pohanka, M., Hrabinova, M., Kuca, K., et al. Assessment of acetylcholinesterase activity using indoxylacetate and comparison with the standard Ellman’s method. Int. J. Mol. Sci. 12(4), 2631-2640 (2011).

    5. Mushtaq, G., Greig, N.H., Khan, J.A., et al. Status of acetylcholinesterase and butyrylcholinesterase in Alzheimer’s disease and type 2 diabetes mellitus. CNS Neurol. Disord. Drug Target 13(8), 1432-1439 (2014).