Triton™ X-100 Surfact-Amps™ Detergent Solution, 50 mL - FAQs

One thing you should do is to permeabilize well, by including 0.1% to 0.2% Triton X-100 in all washes and incubations. Another recommendation is to extend the labeling times to overnight at 4^oC for both primary antibody and secondary antibody. Finally, label the section free-floating, rather than adhered to a slide, to gain penetration for the antibody from both sides.

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After opening, we recommend storing the unused solution sealed in an air-tight vial containing minimal air space or from which the air has been purged with nitrogen gas. Frequent opening should be avoided because Triton X-100 is susceptible to autoxidation upon exposure to air.

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Triton X-100 Surfact-Amps Detergent Solution is covered under our general 1-year warranty and is guaranteed to be fully functional for 12 months from the date of shipment, if stored as recommended (20-25 degrees C). Please see section 8.1 of our Terms & Conditions of Sale (https://www.thermofisher.com/content/dam/LifeTech/Documents/PDFs/Terms-and-Conditions-of-Sale.pdf).

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Thermo Scientific Pierce Surfact-Amps detergents are highly purified, precisely diluted (10%) formulations that are ideal for applications or assays that are sensitive to contaminants that are present in unpurified detergents. We test every batch to insure that our detergents contain less than 1.0 µeq/mL peroxides and carbonyls and package them under nitrogen, to prevent oxidization during storage.

Superior quality - lower measurable contaminant levels than other leading vendors
Accurate -precise 10% detergent solution in ultrapure water
Easy-to-use - solution is simple to dispense and dilute for use
Exceptionally pure - less than 1.0 µeq/mL peroxides and carbonyls

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Ionic detergents, or those that carry a charge, are the most likely to be denaturing to proteins. 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 protein-protein interactions through changes in the three-dimensional structure of the proteins. Nondenaturing detergents can be divided into nonionic detergents (i.e., Triton X-100), bile salts (i.e., cholate), and zwitterionic detergents (i.e., CHAPS).



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Detergents are amphipathic molecules containing both a nonpolar “tail” having aliphatic or aromatic character, and a polar “head”. The ionic character of the polar head group forms the basis for broad classification of detergents as ionic, nonionic, or zwitterionic.

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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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Historically, physical lysis was the method of choice for cell disruption and extraction of cellular contents; however, it often requires expensive, cumbersome equipment and involves protocols that can be difficult to repeat due to variability in the apparatus (such as loose-fitting compared with tight-fitting homogenization pestles). Also, traditional physical disruption methods are not conducive for high-throughput and smaller volumes typical of modern laboratory research.
In recent years, detergent-based cell lysis methods have become the norm. Through empirical testing by trial and error, different detergent-based solutions composed of particular types and concentrations of detergents, buffers, salts and reducing agents have been developed to provide the best possible results for particular species and types of cells. Detergents have both lysing and solubilizing effects.

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