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ACHE Antibody (C-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P22303 |
|---|---|
| Clone Names | 80305110 |
| Gene ID | 43 |
|---|---|
| Other Names | Acetylcholinesterase, AChE, ACHE |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP7853b was selected from the C-term region of human ACHE. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | ACHE (HGNC:108) |
|---|---|
| Function | Hydrolyzes rapidly the acetylcholine neurotransmitter released into the synaptic cleft allowing to terminate the signal transduction at the neuromuscular junction. Role in neuronal apoptosis. |
| Cellular Location | Synapse. Secreted. Cell membrane; Peripheral membrane protein [Isoform H]: Cell membrane; Lipid- anchor, GPI-anchor; Extracellular side |
| Tissue Location | Isoform H is highly expressed in erythrocytes. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Acetylcholinesterase hydrolyzes the neurotransmitter, acetylcholine at neuromuscular junctions and brain cholinergic synapses, and thus terminates signal transmission. The Protein 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. 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.
References
Liang,D., FEBS J. 276 (1), 94-108 (2009)Scacchi,R., Am. J. Med. Genet. B Neuropsychiatr. Genet. (2008)
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