No Products on your Comparison List.
Your basket is empty.
Find out more
Show all species
Show all synonyms
Select your species and application
anti-Human Butyrylcholinesterase Antibodies:
anti-Mouse (Murine) Butyrylcholinesterase Antibodies:
anti-Rat (Rattus) Butyrylcholinesterase Antibodies:
Go to our pre-filtered search.
Human Monoclonal Butyrylcholinesterase Primary Antibody for ELISA - ABIN2192416
Sporty, Lemire, Jakubowski, Renner, Evans, Williams, Schmidt, van der Schans, Noort, Johnson: Immunomagnetic separation and quantification of butyrylcholinesterase nerve agent adducts in human serum. in Analytical chemistry 2010
Show all 5 Pubmed References
Human Monoclonal Butyrylcholinesterase Primary Antibody for ELISA - ABIN2192418
Knaack, Zhou, Abney, Prezioso, Magnuson, Evans, Jakubowski, Hardy, Johnson: High-throughput immunomagnetic scavenging technique for quantitative analysis of live VX nerve agent in water, hamburger, and soil matrixes. in Analytical chemistry 2012
Show all 5 Pubmed References
Human Polyclonal Butyrylcholinesterase Primary Antibody for IHC, IHC (p) - ABIN4285607
Kato, Nicholson, Neiman, Rantalainen, Holmes, Barrett, Uhlén, Nilsson, Spector, Schwenk: Variance decomposition of protein profiles from antibody arrays using a longitudinal twin model. in Proteome science 2011
Cow (Bovine) Polyclonal Butyrylcholinesterase Primary Antibody for IHC, WB - ABIN2781762
Mizukami, Akatsu, Abrahamson, Mi, Ikonomovic: Immunohistochemical analysis of hippocampal butyrylcholinesterase: Implications for regional vulnerability in Alzheimer's disease. in Neuropathology : official journal of the Japanese Society of Neuropathology 2016
Results found that the SNP rs1803274, defining K-variant BCHE, interacted significantly with pesticide exposure and increased the risk of Parkinson's disease (PD) only in pesticide-exposed patients. The K-variant BCHE reduces serum activity of butyrylcholinesterase, a known bioscavenger for pesticides. These results suggest that K-variant BCHE appear to have an increased risk for PD after exposition to pesticides.
both the low Ki value and the high number of BChE-fluoxetine interactions suggest that fluoxetine is a potent inhibitor of BChE, although in vivo mechanisms for the direct effects of BChE inhibition on various pathologies remain to be further investigated.
SNPs localized outside the coding sequence, in 5'UTR or/and in intron 2 of BCHE gene, but not solely in K-variant alteration (p.A539T) itself, are responsible for reduced enzyme activity.
Decreased ChE is associated with shorter recurrence-free survival in patients with non-muscle-invasive bladder cancer undergoing transurethral resection of the bladder. Preoperative ChE could improve patients' risk stratification and selection for adjuvant therapy.
Plasma BChE levels were found to be significantly higher in drug addicts than in non-addicts. No statistically significant association for SNPs rs3495 and rs1803274 with substance abuse disorder was observed.
Double heterozygous recessive mutations are the cause of BChE deficiency, including a novel mutation c.73A > T. Intellectual disability is a new phenotype that is probably associated with this mutation.
A positive association of BuChE activity with nutritional status and serum Triglycerides in Mexican children.
Although BuChE-K alone does not seem to play a major role in progression to Alzheimer's disease, in mild cognitive impairment (MCI) patients a synergistic effect with the ApoE varepsilon4 allele was found, highlighting the importance of assessing these combined genotypes for evaluating risk progression in MCI patients.
The tetramer organization of BChE is unique in that the four subunits are joined at their C-termini through noncovalent contacts with a short polyproline-rich peptide. This tetramer structure could serve as a model for the design of highly stable glycosylated tetramers.
An increased frequency of the BChE K-allele in multiple sclerosis patients as compared to controls was found.
This study validated preoperative serum BChE levels as an independent prognostic factor for urinary tract urothelial carcinoma after radical nephroureterectomy.
we present and examine means of manipulating brain BChE levels by viral gene transfer, either regionally or globally, to modulate ghrelin signaling for long-term therapeutic purposes and to set the stage for exploring the neurophysiological impact of such an intervention.
The BChE-K polymorphisms are associated with deleterious changes in cognitive decline in MCI patients treated with donepezil for 3 years.
BCHE-K* positive subjects (and APOE-epsilon4) display an earlier age of onset of Alzheimer's Disease and an accelerated cognitive decline.
Discovery of potent carbonic anhydrase, acetylcholinesterase, and butyrylcholinesterase enzymes inhibitors: The new amides and thiazolidine-4-ones synthesized on an acetophenone base.()
HuBChE sequesters OP nerve agent in the bloodstream preventing the nerve agent from reaching critical target organ systems. HuBChE was effective when used as both a pre-treatment and as a post-exposure therapy.
Significance of BChE Genetic Variants to Risk of Toxicity from Cholinesterase Inhibitors (review)
Age, sex or smoking status did not influence butyrylcholinesterase activity in a healthy population.
Mutations in the butyrylcholinesterase gene were associated with prolonged effect of succinylcholine or mivacurium.
prolonged apnea after suxamethonium came about as a result of butyrylcholinesterase deficiency or mutation or acquired conditions leading to a decrease in the plasma cholinesterase activity
The structure of bovine pancreatic RNase A has been determined in complex with 2'-deoxyguanosine-5'-monophosphateat 1.33 A resolution.
BChE strongly affects fat metabolism, has an important impact on fat accumulation and may be a promising tool for combating obesity.
the absence of BChE leads to diminished fibrillar Abeta deposition in amygdala, hippocampal formation, thalamus and basal ganglia.
It was concluded that in adult murine bone the role of BChE is limited to bone specific changes in microarchitecture and to an increase in relative number of bone resorbing osteoclasts.
Mice that had undergone gene transfer with mouse CocH (mCocH) showed no place preference or aversion after repeated treatments with a near-lethal 80 mg/kg cocaine dose.
we conclude that toxoplasmosis reduces BChE activity in mice, and this alteration is probably related to the liver damage caused by the parasitism
Ex vivo autoradiograms, after intravenous injection with a BuChE radioligand, demonstrate increased accumulation of radioactivity especially in cortical regions in the AD mouse.
For metacarb and isocarb, inhibition of BChE w.t. was 260 and 35 times, respectively, faster than inhibition of AChE w.t. For four mutants inhibition was faster than for AChE w.t. but none reached the inhibition rate of BChE.
The localization of BChE in the secondary folds of the neuromuscular junction suggests that this enzyme is not a strict surrogate of AChE and that the two enzymes have two different roles.
The effects of porphyrinogenic drugs on the brain cholinergic system (Ache, Bche, and Chrm1 levels in various regions of the brain) were examined to establish a mechanism for neurological syndrome displayed in acute porphyrias.
A possible mechanism for partial compensation of tetanic fade in acetylcholinesterase knockout mice is hydrolysis of acetylcholine by normal levels of endogenous butyrylcholinesterase.
The BChE knockout mouse will allow us to test the hypothesis that the function of BChE is to detoxify poisons and will allow testing the role of BChE in other physiological functions.
These findings show that BCHE can hydrolyze 2-Arachidonoylglycerol which may be evidence of a more specific role for BCHE in endocannabinoid regulation.
Data indicate that polyproline peptides of various lengths and sequences are included in the tetramer structure of butyrylcholinesterase, and the function of these polyproline peptides is to serve as tetramer-organizing peptides.
proline-rich peptides organize the 4 subunits of BChE into a 340 kDa tetramer, by interacting with the C-terminal BChE tetramerization domain
Mutant alleles at the BCHE locus are responsible for suxamethonium sensitivity. Homozygous persons sustain prolonged apnea after administration of the muscle relaxant suxamethonium in connection with surgical anesthesia. The activity of pseudocholinesterase in the serum is low and its substrate behavior is atypical. In the absence of the relaxant, the homozygote is at no known disadvantage.
, acylcholine acylhydrolase
, butyrylcholine esterase
, choline esterase II
, cholinesterase (serum) 2
, cholinesterase 1