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Recombinant Human Acetylcholinesterase (ACHE)

ACP00390

Number
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Specifications


Cat.No ACP00390 Target Nameache
Target SynonymsAChEFormLiquid or Lyophilized powder
Expression SystemMammalian cellExpression Range32-614aa
Mol Weight66.0 kDaProtein LengthFull Length of Mature Protein
PurityGreater than 95% as determined by SDS-PAGE.Storage Buffer5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0.

Immunogen Information


Target SpeciesHumanUniprot IDP22303
Background Information
  • Uniprot Id

    P22303

  • Target Species

    Human

  • Target Name

    ACHE

  • Target Full Name

    Acetylcholinesterase

  • Target Function

    Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. Role in neuronal apoptosis.

  • Target Subcellular Location

    Cell junction, synapse. Secreted. Cell membrane; Peripheral membrane protein.; [Isoform T]: Nucleus. Note=Only observed in apoptotic nuclei.; [Isoform H]: Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side.

  • Target Protein Families

    Type-B carboxylesterase/lipase family

  • Target Tissue Specificity

    Isoform H is highly expressed in erythrocytes.

  • Target Research Area

    Others

  • Target Synonyms

    ACEE; ACES_HUMAN; Acetylcholinesterase; AChE; Apoptosis related acetylcholinesterase; ARACHE; N ACHE; N-ACHE; YT; YT blood group

  • Target Background

    Acetylcholinesterase hydrolyzes the neurotransmitter, acetylcholine at neuromuscular junctions and brain cholinergic synapses, and thus terminates signal transmission. It is also found on the red blood cell membranes, where it constitutes the Yt blood group antigen. Acetylcholinesterase exists in multiple molecular forms which possess similar catalytic properties, but differ in their oligomeric assembly and mode of cell attachment to the cell surface. It is encoded by the single ACHE gene, and the structural diversity in the gene products arises from alternative mRNA splicing, and post-translational associations of catalytic and structural subunits. The major form of acetylcholinesterase found in brain, muscle and other tissues is the hydrophilic species, which forms disulfide-linked oligomers with collagenous, or lipid-containing structural subunits. The other, alternatively spliced form, expressed primarily in the erythroid tissues, differs at the C-terminal end, and contains a cleavable hydrophobic peptide with a GPI-anchor site. It associates with the membranes through the phosphoinositide (PI) moieties added post-translationally. AChE activity may constitute a sensitive biomarker of RBC ageing in vivo, and thus, may be of aid in understanding the effects of transfusion

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