Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Mutant alleles at the BCHE locus are responsible for suxamethonium sensitivity. Additionally we are shipping Butyrylcholinesterase Proteins (19) and Butyrylcholinesterase Kits (18) and many more products for this protein.
Showing 10 out of 135 products:
Human Polyclonal Butyrylcholinesterase Primary Antibody for EIA, WB - ABIN360174
Primo-Parmo, Lightstone, La Du: Characterization of an unstable variant (BChE115D) of human butyrylcholinesterase. in Pharmacogenetics 1997
Show all 3 references for ABIN360174
Human Polyclonal Butyrylcholinesterase Primary Antibody for WB - ABIN392290
Primo-Parmo, Bartels, Wiersema, van der Spek, Innis, La Du: Characterization of 12 silent alleles of the human butyrylcholinesterase (BCHE) gene. in American journal of human genetics 1996
Low BChE activity as a predictor of mortality in acute myocardial infarction might be related to its association with poor cardiac function.
rs1803274 polymorphism of the BCHE gene represents a risk factor for in-stent restenosis after percutaneous coronary intervention.
Complement component C3 and butyrylcholinesterase activity are associated with neurodegeneration and clinical disability in multiple sclerosis.
BChE is a strong predictor for cardiac mortality specifically in younger patients with acute coronary syndrome aged between 45 and 64 years.
High resolution melting analysis for the butyrylcholinesterase atypical variant genotyping is a simple, rapid, sensitive and low cost method
There is a significant decrease in serum ChE activity after severe trauma
This study proves that the p.Ala34Val BChE variant determines the "silent" phenotype (unable to hydrolyze succinylcholine and mivacurium).
Data indicate that butyrylcholinesterase (BChE) was significantly associated with overall survival (OS).
analysis of the T920C mutation allele frequency in butyrylcholinesterase gene in an Indian population
Plasma arylesterase activity is positively associated with plasma ChE specific activity in a nested case-control study.
The structure of bovine pancreatic RNase A (show RNASE1 Antibodies) has been determined in complex with 2'-deoxyguanosine-5'-monophosphateat 1.33 A resolution.
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 (show COCH Antibodies) (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 (show CHRM1 Antibodies) 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 (show AChE Antibodies) 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