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anti-Human Acetylcholinesterase Antibodies:
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Human Polyclonal Acetylcholinesterase Primary Antibody for IHC - ABIN965502
Meshorer, Toiber, Zurel, Sahly, Dori, Cagnano, Schreiber, Grisaru, Tronche, Soreq: Combinatorial complexity of 5' alternative acetylcholinesterase transcripts and protein products. in The Journal of biological chemistry 2004
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Human Polyclonal Acetylcholinesterase Primary Antibody for IF (p), IHC (p) - ABIN741330
Shao, Yu, Zhou, Li, Yang, Pei: Inhibition of miR-134 Protects Against Hydrogen Peroxide-Induced Apoptosis in Retinal Ganglion Cells. in Journal of molecular neuroscience : MN 2015
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Human Polyclonal Acetylcholinesterase Primary Antibody for ICC, IF - ABIN4277639
El-Akabawy, El-Kholy: Neuroprotective effect of ginger in the brain of streptozotocin-induced diabetic rats. in Annals of anatomy = Anatomischer Anzeiger : official organ of the Anatomische Gesellschaft 2014
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Hamster Monoclonal Acetylcholinesterase Primary Antibody for WB - ABIN1882202
Ohno, Brengman, Tsujino, Engel: Human endplate acetylcholinesterase deficiency caused by mutations in the collagen-like tail subunit (ColQ) of the asymmetric enzyme. in Proceedings of the National Academy of Sciences of the United States of America 1998
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Human Monoclonal Acetylcholinesterase Primary Antibody for WB - ABIN1882203
Soreq, Ben-Aziz, Prody, Seidman, Gnatt, Neville, Lieman-Hurwitz, Lev-Lehman, Ginzberg, Lipidot-Lifson: Molecular cloning and construction of the coding region for human acetylcholinesterase reveals a G + C-rich attenuating structure. in Proceedings of the National Academy of Sciences of the United States of America 1991
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Human Polyclonal Acetylcholinesterase Primary Antibody for ELISA, WB - ABIN4277638
Cottingham, Voskuil, Vaux et al.: The intact human acetylcholinesterase C-terminal oligomerization domain is alpha-helical in situ and in isolation, but a shorter fragment forms beta-sheet-rich amyloid fibrils and protofibrillar ... in Biochemistry 2003
Cat (Feline) Monoclonal Acetylcholinesterase Primary Antibody for ICC, IHC (fro) - ABIN152687
Zeineh, Chen, Kitzler, Hammond, Vogel, Rutt: Activated iron-containing microglia in the human hippocampus identified by magnetic resonance imaging in Alzheimer disease. in Neurobiology of aging 2015
Human Polyclonal Acetylcholinesterase Primary Antibody for IF (p) - ABIN881132
Roch, Trachsel, Lutolf: Brief Reports: Single-Cell Analysis Reveals Cell Division-Independent Emergence of Megakaryocytes from Phenotypic Hematopoietic Stem Cells. in Stem cells (Dayton, Ohio) 2015
Cow (Bovine) Polyclonal Acetylcholinesterase Primary Antibody for IF, IHC - ABIN2786887
Feldman, Joormann, Johnson: Responses to Positive Affect: A Self-Report Measure of Rumination and Dampening. in Cognitive therapy and research 2010
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The activity of human erythrocyte acetylcholinesterase differs in males and females and serves as a biomarker for diverse range of diseases. (Review)
These findings suggest that, during Red Blood Cell ageing, GPI (show GNPDA1 Antibodies)-linked proteins and integral membrane proteins are differentially sorted. Also, the vesicles that are generated in vitro show a fast and extensive loss of AChE activity, but not of AChE expression.
These six-membered carbocycles showed nice inhibitory action against AChE and human carbonic anhydrase (hCA) II and I isoforms. The hCA I, II, and AChE were efficiently inhibited by these molecules, with Ki values in the range of 6.70-35.85 nM for hCA I, 18.77-60.84 nM for hCA II, and 0.74-4.60 for AChE, respectively
Discovery of potent carbonic anhydrase, acetylcholinesterase, and butyrylcholinesterase (show BCHE Antibodies) enzymes inhibitors: The new amides and thiazolidine-4-ones synthesized on an acetophenone base.()
hnRNP H (show HNRNPH1 Antibodies) binds to two specific G-runs in exon 5a of ACHE and activates the distal alternative 3 splice site (ss) between exons 5a and 5b. Furthermore, hnRNP H (show HNRNPH1 Antibodies) competes for binding of CstF64 to the overlapping binding sites in exon 5a, and suppresses the selection of a cryptic polyadenylation site, which additionally ensures transcription of the distal 3 ss required for the generation of AChET isoform.
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 Antibodies) Inhibitors (review)
miR (show MLXIP Antibodies)-124 could directly target the 3'-untranslated region of both signal transducer and activator of transcription 3 (STAT3 (show STAT3 Antibodies)) 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 Antibodies) (192Q/R) is associated with susceptibility to organophosphate poisoning; plasma ACHE activities of exposed workers vary w/ PON1 (show PON1 Antibodies) genotype: 192RR>192QR>192QQ.
To date, AChE and BChE (show BCHE Antibodies) 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 Antibodies) 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
Findings provide evidence that brain acetylcholinesterase (AChE) is a potential target for microcystins (MCs (show MOCOS Antibodies)).
aryl acylamidase associated with acetylcholinesterase was higher than the esterase (show ESD Antibodies) activity on zebrafishembryo
Results indicate that direct inhibition of acetylcholinesterase activity and up-regulation of m1 muscarinic acetylcholine receptor (show CHRNB1 Antibodies) expression in the striatum might contribute to the beneficial effects of alpha-asarone on locomotor hyperactivity in Fmr1 (show FMR1 Antibodies) knock out mice.
Data show that 1-month of oral treatment with beta-asarone reduces AChE, Abeta42, APP (show APP Antibodies) and Beclin-1 (show BECN1 Antibodies) levels and alleviates some behavioral impairments by inhibiting the autophagy via regulating the PI3K/Akt (show AKT1 Antibodies)/mTOR (show FRAP1 Antibodies) pathway in APP (show APP Antibodies)/PS1 (show PSEN1 Antibodies) 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 Antibodies) on acetylcholinesterase transcriptional regulation and provided insight in elucidating the DNA methylation (show HELLS Antibodies)-mediated regulatory mechanism on acetylcholinesterase expression during muscle differentiation.
Nerolidol-loaded nanospheres reverse memory impairment and to prevent increased ROS (show ROS1 Antibodies) and TBARS levels due to amelioration of Na(+), K(+)-ATPase (show ATP1A1 Antibodies) and AChE activities and to activation of the antioxidant enzymes, respectively.
the amounts of AChE activity, AChE catalytic subunit, structure subunit PRiMA 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 Antibodies)-infected heterozygous AChE knock-out mice leads to slightly but significantly prolonged incubation time.
mRNA expressions of brain specific (show CALY Antibodies) fatty acid protein 7 (fabp-7 (show FABP7 Antibodies)) and phospholipase A2 (show YWHAZ Antibodies) group IV (pla2g4 (show PLA2G4A Antibodies)) were significantly downregulated in AChE-deficient mice.
AChE is regulated in two neuronal cell lines by APP (show APP Antibodies) 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.
iNOS (show NOS2 Antibodies) and AChE expression increases in spiral ganglia treated with streptomycin. Salvia miltiorrhiza injection reduces ototoxicity by reducing the levels of iNOS (show NOS2 Antibodies) and AChE.
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.
Yt blood group
, apoptosis-related acetylcholinesterase
, acetylcholinesterase (Yt blood group)
, acetylcholinesterase isoform E4-E6
, glycolipid-anchored form of acetylcholinesterase
, acetylcholine esterase