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Description: A non-ionic detergent intended for solubilizing membrane-bound proteins in their native state and for the preparation of lipid vesicles. Its well defined chemical structure, small uniform micelles and high water solubility make it superior to most other non-ionic detergent for membrane solubilization Because of its high critical micelle concentration (CMC) (20-26 mM), it has become one of the most important detergents for purification of membrane proteins because it can readily be removed via dialysis compared to bile salts from final protein extracts. Has been shown to increase the resolution of proteins in 2D gels. Aggregation number: 75 ±10. Absorbance (10% H2O, 260nm).
In basic terms, How does OG work?: Detergents solubilize membrane proteins by mimicking the lipid-bilayer environment. Micelles formed by detergents are analogous to the bilayers of the biological membranes. Proteins incorporate into these micelles via hydrophobic interactions. Hydrophobic regions of membrane proteins, normally embedded in the membrane lipid bilayer, are now surrounded by a layer of detergent molecules and the hydrophilic portions are exposed to the aqueous medium. This keeps the membrane proteins in solution. Complete removal of detergent could result in aggregation due to the clustering of hydrophobic regions and, hence, may cause precipitation of membrane proteins.
Micellar Properties: CMC: 24-26 mM in water (Other CMC values have been reported as low as 13.5 mM).
Micellar size: Reported aggregation numbers from 27 to 100 corresponding to micellar molecular weights of 8,000 to29,000 have been reported. Hydrodynamic radii of 15 ±1 angstroms (micellar MW 8000 ±1,000; aggregation number 27) to 23 ±3 angstroms (micellar MW 22,000 ±3,000; aggregation number 75 ±10) have been reported.
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