Recommended Products
Quality Level
Assay
≥98%
form
powder
storage temp.
−20°C
SMILES string
O.[Cl-].CCCC(=O)OCC[N+](C)(C)C
InChI
1S/C9H20NO2.ClH/c1-5-6-9(11)12-8-7-10(2,3)4;/h5-8H2,1-4H3;1H/q+1;/p-1
InChI key
VCOBYGVZILHVOO-UHFFFAOYSA-M
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Customers Also Viewed
Journal of biochemistry and molecular biology, 36(2), 149-153 (2003-04-12)
The dibucaine number (DN) was determined for serum cholinesterase (EC 3.1.1.8, SChE) in plasma samples. The ones with a DN of 79-82 were used, because they had the "usual" SChE variant. The enzyme was assayed colorimetrically by the reaction of
Ukrainskii biokhimicheskii zhurnal (1978), 67(4), 40-46 (1995-07-01)
Cetyltrimethyl ammonium and cetylpyridinium, both being cationic detergents, have been studied for their effect on the catalytic activity of horse blood serum cholinesterase (BuHChE) in reactions of hydrolysis of carbonic acid esters. It is shown that the detergents tested are
Prikladnaia biokhimiia i mikrobiologiia, 34(3), 326-331 (1998-06-30)
Potentiometric choline electrodes were developed on the basis of the mediator-free bioelectrocatalysis. The electrodes made of a composite carbon-polymer material contain choline oxidase and peroxidase coimmobilized on the surface of the electrode. The rate of the potential increase was shown
Talanta, 83(2), 357-363 (2010-11-30)
A highly sensitive disposable screen-printed butyrylcholine (BuCh) potentiometric sensor, based on heptakis (2,3,6-tri-o-methyl)-β-cyclodextrin (β-CD) as ionophore, was developed for butyrylcholinesterase (BuChE) activity monitoring. The proposed sensors have been characterized and optimized according to the constituents of homemade printing carbon ink
Journal of enzyme inhibition, 14(3), 193-201 (1999-08-13)
Acetylcholinesterases from Drosophila melanogaster and Torpedo marmorata possess 35% identical residues. We built a homology model of the Drosophila enzyme on the basis of the known three-dimensional structure of Torpedo acetylcholinesterase, which revealed an oval rim of the active site
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service