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Goat Anti-ACHE Antibody
Peptide-affinity purified goat antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IF, FC, Pep-ELISA |
|---|---|
| Primary Accession | P22303 |
| Other Accession | NP_000656, 43 |
| Reactivity | Human |
| Predicted | Mouse, Rat |
| Host | Goat |
| Clonality | Polyclonal |
| Concentration | 0.5 mg/ml |
| Isotype | IgG |
| Calculated MW | 67796 Da |
| Gene ID | 43 |
|---|---|
| Other Names | Acetylcholinesterase, AChE, 3.1.1.7, ACHE |
| Format | 0.5 mg IgG/ml in Tris saline (20mM Tris pH7.3, 150mM NaCl), 0.02% sodium azide, with 0.5% bovine serum albumin |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | Goat Anti-ACHE Antibody is for research use only and 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. |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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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. 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.
References
Variation at the NFATC2 Locus Increases the Risk of Thiazolinedinedione-Induced Edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) Study. Bailey SD, et al. Diabetes Care, 2010 Jul 13. PMID 20628086.
Physiogenomic analysis of statin-treated patients: domain-specific counter effects within the ACACB gene on low-density lipoprotein cholesterol? Rua帽o G, et al. Pharmacogenomics, 2010 Jul. PMID 20602615.
Evaluation of Candidate Genes for Cholinesterase Activity in Farmworkers Exposed to Organophosphorous Pesticides - Association of SNPs in BCHE. Howard TD, et al. Environ Health Perspect, 2010 Jun 8. PMID 20529763.
Comparison of human and guinea pig acetylcholinesterase sequences and rates of oxime-assisted reactivation. Cadieux CL, et al. Chem Biol Interact, 2010 Sep 6. PMID 20433814.
Single PCR multiplex SNaPshot reaction for detection of eleven blood group nucleotide polymorphisms: optimization, validation, and one year of routine clinical use. Di Cristofaro J, et al. J Mol Diagn, 2010 Jul. PMID 20431033.
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