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.
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 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)
We have studied the effect of two cosolvents, urea and glycerol, on the association and interactions of a surfactant, octaethyleneglycol dodecyl ether (C(12)EO(8)) and a phospholipid (POPC). We have measured the CMC, the partition coefficient, the effective mole fractions X(e)(sat)
Biochimica et biophysica acta, 1514(1), 76-86 (2001-08-22)
Many attempts have been made to rationalize the use of detergents for membrane protein studies [J. Biol. Chem. 264 (1989) 4907]. The barrier properties of the detergent headgroup may be one parameter critically involved in protein protection. In this paper
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