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n-Octyl-oligo-oxyethylene (biochemical grade)

Non-ionic detergent.
ALX-500-002-L100 100 ml Inquire for pricing
ALX-500-002-L025 25 ml Inquire for pricing
ALX-500-002-L005 5 ml Inquire for pricing
Do you need bulk/larger quantities?
Detergent for solubilization, purification and crystallization of membrane proteins.

Product Specification

Alternative Name:Octyl-POE, OPOE
x = 1 to 10
Appearance:Colorless liquid.
Solubility:Soluble in water.
Long Term Storage:+4°C
Use/Stability:Low temperatures may lead to cloudiness/turbidity. This cloudiness/turbidity disappears by slight heating and stirring, without any loss of quality.
ALX-500-002 structure
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ALX-500-002 structure

Product Literature References

Structural and Functional Stability of DNA Nanopores in Biological Media: J.R. Burns & S. Howorka; Nanomaterials (Basel) 9, 490 (2019), Abstract; Full Text
Lipopolysaccharide regions involved in the activation of Escherichia coli outer membrane protease OmpT: R.A. Kramer, et al.; Eur. J. Biochem. 269, 1746 (2002), Abstract;
Crystal structures explain functional properties of two E. coli porins: W.S. Cowman, et al.; Nature 358, 727 (1992), Abstract;
Crystallization and preliminary X-ray characterization of maltoporin from Escherichia coli: K.A. Stauffer, et al.; J. Mol. Biol. 211, 297 (1990), Abstract;
Membrane protein crystallization: observations and use of short chain phospholipids as amphiphiles: J.L. Eiselé, et al.; J. Cryst. Growth 110, 96 (1990),
The critical role of detergents in the crystallization of membrane proteins: J.P. Rosenbusch; J. Struct. Biol. 104, 134 (1990), Abstract;
Critical micellar concentrations of detergents: M. Zulauf, et al.; Meth. Enzymol. 172, 528 (1989), Abstract;
Densely packed beta-structure at the protein-lipid interface of porin is revealed by high-resolution cryo-electron microscopy: H.J. Sass, et al.; J. Mol. Biol. 209, 171 (1989), Abstract;
Isolation and crystallization of bacterial porin: R.M. Garavito & J.P. Rosenbusch; Meth. Enzymol. 125, 309 (1986), Abstract;
Topographic labelling of pore-forming proteins from the outer membrane of Escherichia coli: M.G.P. Page & J.P. Rosenbusch; Biochem. J. 235, 651 (1986), Abstract;
Porin channel triplets merge into single outlets in Escherichia coli outer membranes: A. Engel, et al.; Nature 317, 643 (1985), Abstract;
A new procedure for the isolation of the brain myelin basic protein in a lipid-bound form: P. Riccio, et al.; FEBS Lett. 177, 236 (1984), Abstract;
Stimulatory GTP regulatory unit Ns and the catalytic unit of adenylate cyclase are tightly associated: mechanistic consequences: H. Arad, et al.; PNAS 81, 6579 (1984), Abstract;
Topology of phage lambda receptor protein. Mapping targets of proteolytic cleavage in relation to binding sites for phage or monoclonal antibodies: S. Schenkman, et al.; J. Biol. Chem. 259, 7570 (1984), Abstract; Full Text
Micelle clusters of octylhydroxyoligo(oxyethylenes): M. Zulauf & J.P. Rosenbusch; J. Phys. Chem. 87, 856 (1983),
Bacterial phosphotransferase system. Solubilization and purification of the glucose-specific enzyme II from membranes of Salmonella typhimurium: B. Erni, et al.; J. Biol. Chem. 257, 13726 (1982), Abstract; Full Text
Solubilized cytochrome c oxidase from Paracoccus denitrificans is a monomer: B. Ludwig, et al.; J. Biol. Chem. 257, 5576 (1982), Abstract; Full Text
Characterization of the major envelope protein from Escherichia coli. Regular arrangement on the peptidoglycan and unusual dodecyl sulfate binding: J.P. Rosenbusch; J. Biol. Chem. 249, 8019 (1974), Abstract; Full Text

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