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Mouse (Murine) Acetylcholinesterase Protein expressed in Human Cells - ABIN2007952
Hillier, Fulton, Fulton, Graves, Pepin, Wagner-McPherson, Layman, Maas, Jaeger, Walker, Wylie, Sekhon, Becker, OLaughlin, Schaller, Fewell, Delehaunty, Miner, Nash, Cordes, Du, Sun, Edwards et al.: The DNA sequence of human chromosome 7. ... in Nature 2003
Show all 5 Pubmed References
these results suggest that the design and investigation of multifunctional agents containing along with the acetylcholinesterase inhibitory segment also an antioxidant moiety capable of alleviating metal (copper)-induced oxidative stress, may be of importance in the treatment of Alzheimer's disease.
Significance of AChE Genetic Variants to Risk of Toxicity from Cholinesterase (show BCHE Proteins) Inhibitors (review)
miR (show MLXIP Proteins)-124 could directly target the 3'-untranslated region of both signal transducer and activator of transcription 3 (STAT3 (show STAT3 Proteins)) and acetylcholinesterase (AChE) mRNAs, and suppress their protein expressions.
Data suggest membranes of erythrocytes of patients with chronic obstructive pulmonary disease exhibit the following changes: increase in acetylcholinesterase; decrease in total ATPases and Na+/K+-ATPases; increase in lipid peroxidation/oxidative stress.
toxicogenetics/genetic association study in population in Turkey: Data suggest SNP in PON1 (show PON1 Proteins) (192Q/R) is associated with susceptibility to organophosphate poisoning; plasma ACHE activities of exposed workers vary w/ PON1 (show PON1 Proteins) genotype: 192RR>192QR>192QQ.
Data suggest cholinesterase (show BCHE Proteins) inhibitors with high potency have proper conformation in active site of ACHE and interact with key residues (Trp84, Phe330 at catalytic anionic site; Trp279 at peripheral anionic site; Gly118, Gly119, Ala201 at oxyanion hole.
Phosphorylated p38 (show CRK Proteins), DNMT1 (show DNMT1 Proteins) and AChE were aberrantly expressed in a subset of hepatocellular carcinoma tumors.
Report acetylcholinesterase kinetics using fluorogenic probe for the investigation of free thiols.
Report reactivation kinetics of a large series of bispyridinium oximes with organophosphate-inhibited human acetylcholinesterase.
Case Report: repetitive obidoxime treatment induced increase of red blood cell acetylcholinesterase activity even in a late phase of a severe methamidophos poisoning.
To date, AChE and BChE (show BCHE Proteins) are the only proteins known that include polyproline tetramer organizing peptides in their tetrameric structure.
findings show that AChE induces a remarkable aggregation of PrP (show PRNP Proteins) 106-126 with a mechanism similar to that described for amyloid beta protein
In this work, the catalytic activity of acetylcholinesterase (AChE) immobilized on these materials was investigated, using neostigmina as AChE inhibitor.
Results strongly support the role of acetylcholinesterase in triggering amyloidogenesis and the potential therapeutic relevance of peripheral site blocker compounds.
Hydrolysis of acetylthiocoline, o-nitroacetanilide and o-nitrotrifluoroacetanilide by fetal bovine serum acetylcholinesterase
iNOS (show NOS2 Proteins) and AChE expression increases in spiral ganglia treated with streptomycin. Salvia miltiorrhiza injection reduces ototoxicity by reducing the levels of iNOS (show NOS2 Proteins) and AChE.
Data show that 1-month of oral treatment with beta-asarone reduces AChE, Abeta42, APP (show APP Proteins) and Beclin-1 (show BECN1 Proteins) levels and alleviates some behavioral impairments by inhibiting the autophagy via regulating the PI3K/Akt (show AKT1 Proteins)/mTOR (show FRAP1 Proteins) pathway in APP (show APP Proteins)/PS1 (show PSEN1 Proteins) transgenic mice. The results further support the exploration of beta-asarone as a possible disease-modifying agent for the treatment of Alzheimer's disease.
Findings suggested the role of DNA methylation (show HELLS Proteins) on acetylcholinesterase transcriptional regulation and provided insight in elucidating the DNA methylation (show HELLS Proteins)-mediated regulatory mechanism on acetylcholinesterase expression during muscle differentiation.
Nerolidol-loaded nanospheres reverse memory impairment and to prevent increased ROS (show ROS1 Proteins) and TBARS levels due to amelioration of Na(+), K(+)-ATPase (show ATP1A1 Proteins) and AChE activities and to activation of the antioxidant enzymes, respectively.
the amounts of AChE activity, AChE catalytic subunit, structure subunit PRiMA (show PRIMA1 Proteins) and the amount of acetylcholine, in the brain were not, significantly, altered, suggesting the role of P2Y1R in neuron could have different function as that in muscle.
In P2Y1R (-/-) mice, acetylcholinesterase expression in muscle was markedly decreased. The proline-rich membrane anchor subunit was reduced by 60 %; while the collagen tail subunit was reduced by 50 %. AChE molecular forms in the muscle were not changed.
Reduction of AChE levels in prion (show PRNP Proteins)-infected heterozygous AChE knock-out mice leads to slightly but significantly prolonged incubation time.
mRNA expressions of brain specific (show CALY Proteins) fatty acid protein 7 (fabp-7 (show FABP7 Proteins)) and phospholipase A2 (show YWHAZ Proteins) group IV (pla2g4 (show PLA2G4A Proteins)) were significantly downregulated in AChE-deficient mice.
AChE is regulated in two neuronal cell lines by APP (show APP Proteins) in a manner independent of the generation of sAPPalpha, sAPPbeta, and AICD.
Deficiency or inhibition of acetylcholinesterase can decrease apoptosis and protect dopaminergic neurons in the neurotoxin model of Parkinson's disease.
Attribute stress-inducible cognitive impairments to cholinergic-mediated induction of miR (show MLXIP Proteins)-132 and consequently suppressed synaptic ACHE.
Findings provide evidence that brain acetylcholinesterase (AChE) is a potential target for microcystins (MCs (show MOCOS Proteins)).
aryl acylamidase associated with acetylcholinesterase was higher than the esterase (show ESD Proteins) activity on zebrafishembryo
Compared potency of oxime antidotes to reactivate pig brain acetylcholinesterase (AChE) after sarin exposure.
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.
acetylcholinesterase (Yt blood group)
, acetylcholinesterase isoform E4-E6
, acetylcholine esterase
, Yt blood group
, apoptosis-related acetylcholinesterase
, glycolipid-anchored form of acetylcholinesterase