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| Cat.No | ACP23931 | Target Name | ache |
|---|---|---|---|
| Target Synonyms | ACEE; ACES_HUMAN; Acetylcholinesterase; AChE; Apoptosis related acetylcholinesterase; ARACHE; N ACHE; N-ACHE; YT; YT blood group | Form | Lyophilized powder |
| Expression System | Custom Production. Please inquire and provide the desire expression system. | Expression Range | 32-614 |
| Protein Length | Full Length of Mature Protein | Purity | >85% (SDS-PAGE) |
| Storage Buffer | 5%-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. |
| Target Species | Human | Uniprot ID | P22303 |
|---|
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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