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Validated All-in-One™ qPCR Primer for ACHE(NM_000665.4) Search again
Product ID:
HQP102501
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
ACEE, ARACHE, N-ACHE, YT
Gene Description:
acetylcholinesterase (Cartwright blood group)
Target Gene Accession:
NM_000665.4(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
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.
Gene References into function
- serum and erythrocyte membrane enzyme inhibited by antidepressants, fluoxetine, sertraline and amitriptyline, in a dose related manner
- REVIEW: Simulations show how breathing motions in the enzyme facilitate the displacement of substrate from the surface of the enzyme to the buried active site; such motions suggest possible modes of regulation of the activity of the enzyme.
- The aromatic "trapping" of the catalytic histidine is essential for efficient catalysis
- regulation of ACHE expression in developing muscle cells
- complex regulation of its gene expression in brain tumors
- AChE activity in the CSF of Alzeimer's disease patients is affected differentially by different AChE inhibitors. (AChE)
- AChE was predominantly expressed in neurons of the anterodorsal, midline, ventral, intralaminar, and reticular nuclei.
- analysis of acetylcholinesterase active site
- muscle-induced neuronal AChE expression in co-culture is mediated by a cAMP-dependent signaling
- oxidation of AchE by hydrogen peroxide contributes significantly to the well-established oxidative stress in vitiligo
- analysis of acetylcholinesterase near the active center gorge
- Data suggest that alternative promoter usage combined with alternative splicing may lead to stress-dependent combinatorial complexity of acetylcholinesterase mRNA transcripts and their protein products.
- complexed with abeta protein, is toxic to rat brain beta-amyloid aggregation, laminin expression, reactive astrocytosis, and neuronal cell loss.
- AChE is involved in regulating cell-matrix interactions in bone
- A total of 13 ACHE SNPs were identified, 10 of which are newly described, and five that should produce amino acid substitutions
- This study found a layer 3 magnopyramidal AChERN left-right size asymmetry restricted to Brodmann's area 45, a component of Broca's language area.
- findings suggest that inherited interactive weakness of acetylcholinesterase and paraoxonase 1 expression increases the insecticide-induced occurrence of Parkinson's disease
- Variations were observed in expression of mRNA for presenilin-1, which was highest in singly transgenic hAChE mice, and the stress-inducible form of AChE, which was elevated when both transgenes were present.
- Human plasma contains four esterases: butyrylcholinesterase, paraoxonase, acetylcholinesterase, and albumin.
- basal lamina formation is the essential event in the transformation of immature neuromuscular contact into differentiated neuromuscular junction, with the accumulation of not only muscular but also neuronal AChE in the synaptic cleft
- functional and molecular design of the AChE active center
- demonstration of the existence of a membrane-bound acetylcholinesterase in human endothelial cells
- Increased membrane AChE activity may be due to high homocysteine levels
- expression level of acetylcholinesterase was increased in lung cancer
- Variant-specific causal involvement of AChE in the progression of both neurodegenerative diseases and neuromuscular syndromes raises the possibility that future therapeutic drugs might target specific AChE variant(s) or the corresponding RNA transcripts.
- These findings suggest that the Polyethyleneglycol conjugated (PEGylated) recombinant human acetylcholinesterase exhibits unaltered biodistribution and high bioavailability.
- Upregulation of acetylcholinesterase is associated with ovarian cancer
- Down-regulation of Acetylcholinesterase is associated with colorectal carcinoma
- These results indicate that cortical acetylcholineesterase activity is relatively well preserved in apolipoprotein E4 carriers, either by preservation of its cellular expression or as AChE activity in amyloid plaques.
- relationship between the expression of AChE and the aggressiveness in tumors.
- Levels of AChE, its molecular forms, and glycosylation in the cerebrospinal fluid (CSF) from Creutzfeldt-Jakob disease (CJD) patients differs from normal values.
- Asingle ACHE gene produces several types of catalytic subunits by alternative splicing, but a single splice variant, called type T (AChET), is expressed in adult mammalian muscle and brain
- Modified AChE gene expression and properties are causally involved in thymic function and development.
- These results indicate that calcineurin mediates acetylcholinesterase expression during apoptosis.
- calcium-activated butyrylcholinesterase as a major protective mechanism against suicide inhibition of AchE by organophosphates in this non-neuronal tissue
- Combination of obidoxime and HI6 reactivated AChE inhibited by a range of cholinesterase inhibitors.
- AChE's 3' alternative splicing, and the corresponding changes in AChE-S/CtBP interactions, thus emerge as being actively involved in controlling hematopoiesis
- AChE polymorphisms do not constitute a major genetic risk factor for susceptibility to Alzheimer's diseasein a Sardinian population.
- that the 55-kDa AChE may be involved in different biological processes such as neural development, tumor progression, and angiogenesis.
- Report concentration-dependent interactions of chlorpyrifos oxon with acetylcholinesterase.
- Computational and biochemical approaches have been combined to shed light on the atomic aspects of the role of Li(+), Na(+), and K(+) on human acetylcholinesterase (hAChE) ligand binding
- These findings suggest that cell surface AChE, possibly in a novel signalling complex containing APP and perlecan, contributes to a generalised mechanism for polarised membrane protrusion and migration in all adherent cells.
- Genotoxic biomarkers and AChE levels are important parameters for determining effects of pesticide exposure on health.
- Testing potency of acetylcholinesterase reactivators.
- ACHE increases spermatozoan apoptosis but enhances sperm motility.
- define sites for the interaction of AChE and laminin and suggest that the interaction plays a role in cell adhesion
- Interactions of AChE with caveolin-1 and subsequently with cytochrome c appear to be indispensable for apoptosome formation in a colon cancer cell line.
- PS1 can interact with AChE and influence its expression, supporting the notion of cholinergic-amyloid interrelationships.
- Determne in vitro oxime protection of human red blood cell acetylcholinesterase inhibited by diisopropyl-fluorophosphate.
- During a normal delivery process, the increased levels of catecholamines and the increased AChE activity, post-delivery, may be due to the increased stress of delivery.
- Results show that acetylcholinesterase (AChE) activity and RNA levels increase during differentiation, and that differentiation of intestinal cells involves AChE-induced cell cycle arrest.
- Acetylcholinesterase supports anchorage independence in colon cancer.
- N-acetylcholinesterase has a role in apoptosis in Alzheimer's disease
- Differences between the t peptides of Aacetylcholinesterase and butyrylcholinesterase are conserved among all vertebrates.