Octaethylene glycol monododecyl ether is a nonionic detergent.
Application
Detergent used for the study of membrane proteins in a native-like state, e.g. ATPase. Used in a mixed micellar assay for lipoxygenase acting at neutral pH and for functional reconstitution of influenza virus envelopes.
The journal of physical chemistry. B, 114(35), 11371-11376 (2010-08-19)
In the current work, we studied the effect of the nonionic detergent dodecyloctaethyleneglycol, C(12)E(8), on the structure and oligomeric form of the Na,K-ATPase membrane enzyme (sodium-potassium pump) in aqueous suspension, by means of small-angle X-ray scattering (SAXS). Samples composed of
The effects of a nonionic surfactant, octaethyleneglycol mono n-dodecyl ether (C12E8), on the electroporation of planar bilayer lipid membranes made of the synthetic lipid 1-pamitoyl 2-oleoyl phosphatidylcholine (POPC), was studied. High-amplitude ( approximately 100-450 mV) rectangular voltage pulses were used
[Relationship between activity and tetraprotomeric structure of ion-transporting ATPases].
Kazuhiro Abe et al.
Seikagaku. The Journal of Japanese Biochemical Society, 79(6), 527-534 (2007-08-01)
Biochemical and biophysical research communications, 391(1), 1067-1069 (2009-12-17)
Many membrane proteins become labile when they are solubilized by detergent. Here we show that the presence of high concentrations of glycyl betaine stabilizes one of these proteins, the sarcoplasmic reticulum Ca(2+)-ATPase (SERCA1a), solubilized with nonionic detergents like n-dodecyl beta-d-maltopyranoside
The Biochemical journal, 333 ( Pt 2), 285-290 (1998-07-11)
The glutamine carrier from rat kidney mitochondria, solubilized in dodecyl octaoxyethylene ether (C12E8) and partly purified on hydroxyapatite, was identified and completely purified by Celite chromatography. On SDS/PAGE, the purified glutamine carrier consisted of a single protein band with an
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