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anti-Human Acetylcholinesterase Antikörper:
anti-Rat (Rattus) Acetylcholinesterase Antikörper:
anti-Mouse (Murine) Acetylcholinesterase Antikörper:
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Human Polyclonal Acetylcholinesterase Primary Antibody für 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 für 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 Monoclonal Acetylcholinesterase Primary Antibody für ELISA, WB - ABIN534389
Lane, Potkin, Enz: Targeting acetylcholinesterase and butyrylcholinesterase in dementia. in The international journal of neuropsychopharmacology / official scientific journal of the Collegium Internationale Neuropsychopharmacologicum (CINP) 2006
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Cat (Feline) Polyclonal Acetylcholinesterase Primary Antibody für ELISA, WB - ABIN547404
Kooi, Prins, Bajic, Beliën, Gerritsen, van Horssen, Aronica, van Dam, Hoozemans, Francis, van der Valk, Geurts: Cholinergic imbalance in the multiple sclerosis hippocampus. in Acta neuropathologica 2011
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Human Polyclonal Acetylcholinesterase Primary Antibody für 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
Human Polyclonal Acetylcholinesterase Primary Antibody für 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
Cow (Bovine) Polyclonal Acetylcholinesterase Primary Antibody für 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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Cat (Feline) Monoclonal Acetylcholinesterase Primary Antibody für 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
Lower plasma acetylcholinesterase and butyrylcholinesterase activity were independent risk factors for postoperative delirium.
results may explain the role of hAChE-S in Abeta deposition and aggregation, as amyloidogenic hAChE-S beta-sheet species might seed Abeta aggregation.
No statistically significant association of rs17228616 SNP of acetylcholinesterase with substance abuse disorder was found.
Steady-state fluorescence and microscale thermophoresis experiments allowed the authors to confirm the binding of some of mycotoxins to acetylcholinesterase and X-linked neuroligin 4, two proteins involved in synapse activity and, particularly for the second protein, neuronal plasticity and development.
The results of this study confirm the existence of an extensive network of AChE-positive cortical pyramidal neurons in the human cerebral cortex.
Sperm acetylcholinesterase (ACHE) gene hydroxymethylation level is higher in the bisphenol A (BPA) exposure group compared to the control group. A positive linear association between urine BPA concentration and 5-hydroxymethylcytosine (5hmC) rate of the sperm ACHE gene is observed. 5hmC of the sperm ACHE gene is positively associated with BPA exposure, which provides evidence for BPA's effects on male fertility.
1-Naphthyl acetate (1-NA) to be a better alternative substrate for AChE than ATCh in terms of lower Km value. Its specificity appeared at least similar to ATCh. Therefore, we propose that 1-NA can be an attractive chromogenic substrate for the measurement of AChE activity.
AChE polymorphism was significantly associated to reduced activity in both multiple sclerosis patients and controls.
this study concludes and confirms that the aryl acylamidase activity of AChE is actively involved in the process of osteoblast differentiation and mineralization.
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-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.
Our analysis showed that DMSO is a considerably potent and highly selective irreversible mixed-competitive inhibitor of human AChE with IC50 values in the lower millimolar range, corresponding to 0.88% to 2.6% DMSO (v/v). Most importantly, 1-4% (v/v) DMSO, the commonly used experimental concentrations, showed approximately 37-80% inhibition of human AChE activity.
This study found an increase in the protein and transcript levels of the non-cholinergic "readthrough" AChE (AChE-R) variants in Alzheimer's Disease patients compared to controls.
The optimized docking protocol was validated by an external test set of 11 natural galantamine derivatives and the correlation coefficient between the docking scores and the pIC50 values was 0.800. The derived relationship was used to analyze the interactions between galantamine derivatives and AChE.
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 enzymes inhibitors: The new amides and thiazolidine-4-ones synthesized on an acetophenone base.()
hnRNP H 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 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 Inhibitors (review)
miR-124 could directly target the 3'-untranslated region of both signal transducer and activator of transcription 3 (STAT3) and acetylcholinesterase (AChE) mRNAs, and suppress their protein expressions.
To date, AChE and BChE are the only proteins known that include polyproline tetramer organizing peptides in their tetrameric structure.
The monomeric form of AChE in fetal bovine serum is trimmed at the carboxyl-terminus compared to the tetrameric form, consistent with the involvement of C-terminal amino acids in the assembly of monomers into tetramers.
findings show that AChE induces a remarkable aggregation of PrP 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
Endosulfan exposure inhibits brain Ache activity and significantly impairs animals' exploratory performance, and potentially compromises their ecological and interspecific interaction.
Findings provide evidence that brain acetylcholinesterase (AChE) is a potential target for microcystins (MCs).
Results demonstrate that AChE is dispensable for its proposed non-classical roles in muscle fiber formation and sensory neuron development, but is crucial for regulating the stability of neuromuscular synapses.
aryl acylamidase associated with acetylcholinesterase was higher than the esterase activity on zebrafishembryo
Loss of acetylcholinesterase activity with mitochondrial dysfunction is associated with hypercholesterolemia.
In melanoma, MITF overexpression induced ACHE transcription, and mutation of an E-box site in human ACHE promoter blocked this induction
Results indicate that direct inhibition of acetylcholinesterase activity and up-regulation of m1 muscarinic acetylcholine receptor expression in the striatum might contribute to the beneficial effects of alpha-asarone on locomotor hyperactivity in Fmr1 knock out mice.
Data show that 1-month of oral treatment with beta-asarone reduces AChE, Abeta42, APP and Beclin-1 levels and alleviates some behavioral impairments by inhibiting the autophagy via regulating the PI3K/Akt/mTOR pathway in APP/PS1 transgenic mice. The results further support the exploration of beta-asarone as a possible disease-modifying agent for the treatment of Alzheimer's disease.
Results indicate that adult onset hypothyroidism caused significant memory impairment and increased fear/anxiety. Moreover, the activity of both isoforms of AChE was reduced in all brain regions examined in a brain region- and isoform-specific manner.
Unusually high AChE activity may be an effect marker of exposure to ethanol. The relationship between AChE and apoptosis might represent a novel mechanism of ethanol-associated neuronal injury.
Findings suggested the role of DNA methylation on acetylcholinesterase transcriptional regulation and provided insight in elucidating the DNA methylation-mediated regulatory mechanism on acetylcholinesterase expression during muscle differentiation.
Nerolidol-loaded nanospheres reverse memory impairment and to prevent increased ROS and TBARS levels due to amelioration of Na(+), K(+)-ATPase 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.
Our results are discussed in the context of AChE inhibitor therapy as used in dementia.
Reduction of AChE levels in prion-infected heterozygous AChE knock-out mice leads to slightly but significantly prolonged incubation time.
mRNA expressions of brain specific fatty acid protein 7 (fabp-7) and phospholipase A2 group IV (pla2g4) were significantly downregulated in AChE-deficient mice.
In silico studies in probing the role of kinetic and structural effects of different drugs for the reactivation of tabun-inhibited AChE.
AChE is regulated in two neuronal cell lines by APP 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-132 and consequently suppressed synaptic ACHE.
assayed the relative activities of AChE and BChE in membrane fractions and culture medium of three different neuronal cell lines, namely the neuroblastoma cell lines SH-SY5Y and NB7 and the basal forebrain cell line SN56
Long-lasting stress-inducible changes in AChE's promoter choices, identify the chromatin changes that support this long-term transcriptional memory, and reveal HDAC4 as a mediator of these effects in the hippocampus.
binding of AChE to laminin-1 alters AChE activity and leads to increased neurite growth in culture. A possible mechanism of the AChE effect on neurite outgrowth is proposed due to the interaction of AChE with laminin-1.
iNOS and AChE expression increases in spiral ganglia treated with streptomycin. Salvia miltiorrhiza injection reduces ototoxicity by reducing the levels of iNOS and AChE.
differences between human and guinea pig 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