ACHE Antibody

Code CSB-PA547258
Size US$297
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  • Western blot analysis of extracts from HepG2 cells, using ACHE antibody.
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Product Details

Full Product Name
Rabbit anti-Homo sapiens (Human) ACHE Polyclonal antibody
Uniprot No.
Target Names
ACHE
Alternative Names
ACEE antibody; ACES_HUMAN antibody; Acetylcholinesterase antibody; AChE antibody; Apoptosis related acetylcholinesterase antibody; ARACHE antibody; N ACHE antibody; N-ACHE antibody; YT antibody; YT blood group antibody
Raised in
Rabbit
Species Reactivity
Human
Immunogen
Synthesized peptide derived from C-terminal of Human ACHE.
Immunogen Species
Homo sapiens (Human)
Clonality
Polyclonal
Purification Method
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
Concentration
It differs from different batches. Please contact us to confirm it.
Form
Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Tested Applications
ELISA,WB
Recommended Dilution
Application Recommended Dilution
WB 1:500-1:3000
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

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Target Background

Function
Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. Role in neuronal apoptosis.
Gene References into Functions
  1. 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. PMID: 30201403
  2. AChE polymorphism was significantly associated to reduced activity in both multiple sclerosis patients and controls. PMID: 29358722
  3. this study concludes and confirms that the aryl acylamidase activity of AChE is actively involved in the process of osteoblast differentiation and mineralization. PMID: 28852920
  4. The activity of human erythrocyte acetylcholinesterase differs in males and females and serves as a biomarker for diverse range of diseases. (Review) PMID: 28885588
  5. 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. PMID: 28518050
  6. 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. PMID: 29017007
  7. 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. PMID: 27258420
  8. 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. PMID: 27490385
  9. 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 PMID: 28613396
  10. Discovery of potent carbonic anhydrase, acetylcholinesterase, and butyrylcholinesterase enzymes inhibitors: The new amides and thiazolidine-4-ones synthesized on an acetophenone base.() PMID: 28544359
  11. 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. PMID: 28180311
  12. 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. PMID: 27230386
  13. Significance of AChE Genetic Variants to Risk of Toxicity from Cholinesterase Inhibitors (review) PMID: 27551784
  14. 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. PMID: 27977009
  15. AChE activity in smokers was elevated (approx. 3% in males; 8% in females) relative to that in non-smokers. PMID: 28465191
  16. 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. PMID: 28427893
  17. Thus C-547 is one of the most potent and selective reversible inhibitors of AChE with a long residence time, tau=20 min, longer than for other reversible inhibitors used in the treatment of myasthenia gravis. This makes C-547 a promising drug for the treatment of this disease PMID: 26929400
  18. Studies have demonstrated involvement of inherited tendencies of AChE increases in response to stress. PMID: 27138800
  19. 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. PMID: 26369587
  20. These results suggest that the low AChE activity observed in larynx squamous cell carcinoma may be useful for predicting the outcome of patients. PMID: 26002584
  21. toxicogenetics/genetic association study in population in Turkey: Data suggest SNP in PON1 (192Q/R) is associated with susceptibility to organophosphate poisoning; plasma ACHE activities of exposed workers vary w/ PON1 genotype: 192RR>192QR>192QQ. PMID: 23625910
  22. Data suggest cholinesterase 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. PMID: 26202430
  23. Phosphorylated p38, DNMT1 and AChE were aberrantly expressed in a subset of hepatocellular carcinoma tumors. PMID: 26299326
  24. Report acetylcholinesterase kinetics using fluorogenic probe for the investigation of free thiols. PMID: 26494253
  25. Report reactivation kinetics of a large series of bispyridinium oximes with organophosphate-inhibited human acetylcholinesterase. PMID: 26210933
  26. Case Report: repetitive obidoxime treatment induced increase of red blood cell acetylcholinesterase activity even in a late phase of a severe methamidophos poisoning. PMID: 26200596
  27. Low AChE activity in head and neck squamous cell carcinoma can be used to predict survival in patients with head and neck cancer. PMID: 25956553
  28. Data show that the 3D-quantitative structure property relationship (QSAR) models are capable of explaining the experimental phenomenon of ligand recognition and binding to acetylcholinesterase (AChE). PMID: 24905476
  29. The results suggest that interference with the enzymatic activities of AChE and/or interference with necroptosis may be novel approaches to influence ovarian functions. PMID: 25766324
  30. PRX-105 is a plant-derived recombinant version of the human 'read-through' acetylcholinesterase splice variant (AChE-R) which may be used for treatment/prevention of organophosphate poisoning. PMID: 26051873
  31. Data suggest that natural antisense RNA may play an important role in acetylcholinesterase (AChE) regulation via affecting the epigenetic modification in the AChE promoter region. PMID: 25240585
  32. QSAR analysis on tacrine-related acetylcholinesterase inhibitors. PMID: 25239202
  33. In symptomatic methylphosphonic difluoride poisoning high methylphosphonofluoridic acid concentrations in blood/tissues may lead to the formation of toxic phosphonyloximes after treatment with oximes. PMID: 25240274
  34. The results showed that AChE clusters colocalized with neurexin assemblies in the neurites of hippocampal neurons. PMID: 24594013
  35. Results suggest that AChE 7-20, a beta-hairpin region in AChE, might be a new motif in AChE capable of triggering Abeta aggregation and deposition PMID: 23981668
  36. Synaptic acetylcholinesterase may be a tumor suppressor and is modulated by miR-212 in non-small cell lung cancer. PMID: 23974008
  37. the T14 peptide derived from AChE produced a dose-dependent biphasic modulation of cortical networks activity dependent on the alpha-nAChR: study of a novel bioactive agent of high potential relevance to neurodegenerative disorders such as Alzheimer disease PMID: 23711548
  38. The mesenteric lymphatic vessels show many AChE positive nerve fibres around their wall with an almost plexiform distribution. PMID: 24402754
  39. The aim of this work is to review and discuss the recent findings about acetylcholinesterase, including its sensitivity to other pollutants and the expression of different splice variants. PMID: 23936791
  40. There is decreased expression of ACHE and CHRM3 in eccrine glands of cholinergic urticaria patients. PMID: 23748235
  41. AChE is regulated in two neuronal cell lines by APP in a manner independent of the generation of sAPPalpha, sAPPbeta, and AICD. PMID: 23897820
  42. Low AChE activity was associated with deficits in neurodevelopment, particularly in attention, inhibition, and memory in boys but not in girls. PMID: 24249815
  43. Data indicate that high AChE affinity of the compounds was achieved by optimizing different substituents on the pyridazinone ring, without sacrificing the AChE/BuChE selectivity profile. PMID: 23466605
  44. verify amplification and/or deletion in the ACHE, BCHE, EPHB4 and MME genes in 32 samples of sporadic breast cancer PMID: 23063927
  45. 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 PMID: 23047022
  46. AChE contains a deep active site gorge with two sites of ligand binding, an acylation site (or A-site) containing the catalytic triad at the base of the gorge and a peripheral site (or P-site) near the gorge entrance. PMID: 23047027
  47. Free energy landscape for the binding process of Huperzine A to acetylcholinesterase PMID: 23440190
  48. Acetylcholinesterase inhibitor huperazine A improved, or partly reversed, the Abeta-induced damage of neurite outgrowth. PMID: 23119107
  49. AChE and BChE activities were decreased in prostate cancer patients PMID: 22560633
  50. results suggest that the glycosylation may affect AChE(H) enzymatic activity and trafficking, but not dimer formation. The present findings indicate the significance of N-glycosylation in controlling the biosynthesis of the AChE(H) dimer form PMID: 22805525

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Subcellular Location
Cell junction, synapse. Secreted. Cell membrane; Peripheral membrane protein.; [Isoform T]: Nucleus. Note=Only observed in apoptotic nuclei.; [Isoform H]: Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side.
Protein Families
Type-B carboxylesterase/lipase family
Tissue Specificity
Isoform H is highly expressed in erythrocytes.
Database Links

HGNC: 108

OMIM: 100740

KEGG: hsa:43

STRING: 9606.ENSP00000303211

UniGene: Hs.154495

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