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anti-Human Butyrylcholinesterase Antikörper:
anti-Mouse (Murine) Butyrylcholinesterase Antikörper:
anti-Rat (Rattus) Butyrylcholinesterase Antikörper:
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Human Monoclonal Butyrylcholinesterase Primary Antibody für ELISA - ABIN2192418
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
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Human Monoclonal Butyrylcholinesterase Primary Antibody für ELISA - ABIN2192416
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
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Cow (Bovine) Polyclonal Butyrylcholinesterase Primary Antibody für 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
Human Polyclonal Butyrylcholinesterase Primary Antibody für 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
BCHE-K* positive subjects (and APOE (zeige APOE Antikörper)-epsilon4) display an earlier age of onset of Alzheimer's Disease and an accelerated cognitive decline.
Discovery of potent carbonic anhydrase, acetylcholinesterase (zeige AChE Antikörper), and butyrylcholinesterase enzymes inhibitors: The new amides and thiazolidine-4-ones synthesized on an acetophenone base.()
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 molecular mechanisms by which point mutations may lead to silent BChE variant or alter catalytic activity, is reported.
BChE expression might be regulated by alpha-linolenic acid in HepG2 cells.
Nine out of 18 (50%) individuals with butyrylcholinesterase activity below 2000 U/L had a mutation in 5'UTR (zeige UTS2R Antikörper) (32G/A), intron 2 (c.1518-121T/C) or exon 4 (c.1699G/A; the K variant mutation).
No significant difference in BChE levels of healthy pregnant women and high-risk pregnant women who had undergone a cesarean section under general anesthesia.
The structure of bovine pancreatic RNase A (zeige RNASE1 Antikörper) 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 (zeige APP Antikörper) 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 (zeige COCH Antikörper) (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
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 (zeige CHRM1 Antikörper) 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 (zeige AChE Antikörper) 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