Tween™ 20 Surfact-Amps™ Detergent Solution

Tween-20 Surfact-Amps Detergent Solution is a highly-purified Tween 20 detergent stabilized as a 10% solution and packaged under nitrogen in glass ampules or non-leaching HDPE bottles, ensuring its stability and eliminating the accumulation of peroxides and degradation products.

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The detergent is screened for:
- Visualization: clear, light yellow liquid, free of particulates
- Concentration: 10.0 +/- 1.0%
- Oxidant concentration: less than or equal to 1.0 µeq/mL
- Carbonyl concentration: less than or equal to 1.0 µeq/mL
- suspended solids: residue present must not exceed Residue Reference

See the COA for further details.

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Detergents are amphipathic molecules, meaning they contain both a nonpolar “tail” having aliphatic or aromatic character and a polar “head”. Like the components of biological membranes, detergents have hydrophobic-associating properties as a result of their nonpolar tail groups. Nevertheless, detergents are themselves water soluble.

Consequently, detergent molecules allow the dispersion (miscibility) of water-insoluble, hydrophobic compounds into aqueous media, including the extraction and solubilization of membrane proteins. Detergent monomers solubilize membrane proteins by partitioning into the membrane bilayer. With increasing amounts of detergents, membranes undergo various stages of solubilization.

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Detergents can be denaturing or non-denaturing with respect to protein structure. Denaturing detergents can be anionic such as sodium dodecyl sulfate (SDS) or cationic such as ethyl trimethyl ammonium bromide. These detergents totally disrupt membranes and denature proteins by breaking proteinprotein interaction. These detergents are considered harsh. Non-denaturing detergents can be divided into nonionic detergents (i.e., Triton X-100), bile salts (i.e., cholate), and zwitterionic detergents (i.e., CHAPS). These detergents do not denature proteins and do not break protein-protein interactions. These detergents are considered mild.

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Cell lysis is the first step in cell fractionation, organelle isolation, and protein extraction and purification. As such, cell lysis opens the door to a myriad of proteomics research methods. Many techniques have been developed and used to obtain the best possible yield and purity for different species of organisms, sample types (cells or tissue), and target molecule or subcellular structure. Subcellular fractionation and protein enrichment are important methods in the rapidly growing field of proteomics. Isolation of subcellular fractions and concentration of proteins in low abundance allow for more efficient identification and study of proteins of interest. Examples are the isolation of integral membrane proteins and nuclear proteins.

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