Triton® X100

Triton X-100 is a polymerization product of isooctylphenol and ethylene oxide with an average value of 9.5 ethylene oxide units/molecule. It is one of the most frequently used surfactants for the isola¬tion, purification and analysis of membrane components. This surfactant possesses a high solubilization potential whilst in many cases preserving biological properties to a maximum degree. It can be used in place of Nonidet NP-40 (Shell) which is no longer produced.

Triton X-100 is the surfactant of choice for the solubilization and characterization of many enzymes e.g. acetylcholinesterases, protein kinases and adenosinetriphosphatases. It can also be applied to the investigation of mem¬brane proteins like photosystems, ion channels and receptors. Recently, it has frequently been used in combination with other detergents for the isolation and characterization of lipid rafts.

Furthermore, Triton X-100 is used for cell permeabilization, for electrophoretic and chromatographic separations of proteins, in chemiluminescence and fluorescence assays, for some cell culture techniques etc.

Registered trademark of  the DOW Chemical Company

Synonyms: TX-100; Octylphenol Ethoxylate, Octoxynol-9, Octylphenoxy polyethoxyethanol

CAS registry number: [9002-93-1]

Relative molecular mass (Mr): ca. 625

Classification: Non-ionic surfactant

Literature specification:
•    Critical micellar concentration (CMC): 0.3 mM
•    Aggregation number (Na): 140
•    Cloud point (cp): 63-69 °C (1% in H20)
•    Moles EO: 9.5 (average)
•    Partial specific volume (Zi): 0.908 cm3/g
•    Hydrophilic-lipophilic balance (HLB): 13.5
•    Viscosity (cP, 25°C): 240


Solubilization and Characterization of Enzymes

Campoy, F.J., Canovas-Munoz, M.D., Vidal, C.J. (1989) Acetylcholinesterase from muscle microsomes: molecular forms obtained by solubilization with Triton X-100 and trypsin. Biochem. Soc. Trans. 17, 676-7.

Clapham, J.C., Price, S.J. a. Wilderspin, A.F. (1989) Effect of non-ionic detergent on the activity of dog heart cyclic-nucleotide phos¬phodiesterases. Biochem. Soc. Trans. 17, 718-9.

Dawson, R.M., Gray, P.J., Upsher, C.M. a. Michaelson, S. (1989) Modification of the kin¬etic properties of Triton-solubilized rabbit brain acetylcholinesterase by allosteric effectors at low ionic strength. Neurochem. Int. 15, 49-54.

Dygas, A.a. Zborowski, J. (1989) Effect of Triton X-100 on the activity and solubilization of rat liver mitochondrial phosphatidylserine decar¬boxylase. Acta Biochim. Pol. 36, 131-41.

Gazdzik, D. a. Sitkievvicz, D. (1989) Effect of Triton X-100 on the inhibition of human ery¬throcyte acetylcholinesterase by organophosphorous insecticide DDVP. Pestic. Biochem. Physiol. 34, 126-9.

Kato, Y. a. Spiro, R.G. (1989) Characterization of a thyroid sulfotransferase responsible for the 3-O-sulfation of terminal ß-D-gatactosyl resi¬dues in N-linked carbohydrate units. J. Biol. Chem. 264, 3364-71.

Murphy, D.J. a. Mukherjee, K.D. (1989) Elonga¬ses synthesizing very long chain monounsatu-rated fatty acids in developing oilseeds and their solubilization. Z. Naturforsch., C.:Biosci. 44, 629-34.

Saha, A.K., Dowling J.N., Mukhopadhyay, N.K. a. Glew, R.H. (1989) Legionella micdadei protein kinase catalyzes phosphorylation of tubulin and phosphatidylinositol. J. Bacteriol.171, 5103-10.

Sandstrom, R.P. a. Cleland, R.E. (1989) Selective delipidation of the plasma membrane by sur¬factants. Enrichment of sterols and activation of ATPase. Plant Physiol. 90, 1524-31.

Spence, M.W., Byers, D.M., Palmer, F.B.S.C. a. Cook, H.W. (1989) A new zinc-stimulated sphingomyelinase in fetal bovine serum. J. Biol. Chem. 264, 5358-63.

Dey, C.S.a. Majumder, G.C. (1990) Type I and II cAMP-dependent ecto-protein kinases in goat epididymal spermatozoa and their enriched activities in forward-motile spermatozoa. Bio¬chem. Cell Biol. 68, 459-70.

Garza-Ramos, G., Darszon, A.,Tuena de Gomez-Puyou, M.a. Gomez-Puyou, A. (1990) Enzyme catalysis in organic solvents with low water content at high temperatures. The adenosinetriphosphatase of submitochon¬drial particles. Biochemistry 29, 751-7.

Lin, Y.P. a. Carman, G.M. (1990) Kinetic analysis of yeast phosphatidate phosphatase toward Triton X-100/phosphatidate mixed micelles. J. Biol. Chem. 265, 166-70.

Alba, F. et al. (1995) Properties of rat brain dipeptidyl aminopeptidases in the presence of detergents. Peptides 16, 325-9.

Das, A. et al. (1999) Retinal neovascularization is suppressed with a matrix metalloproteinase inhibitor. Arch. Ophthalmol. 117, 498-503.

Phillips, A.L. et al. (2000) Bovine placental protease specifity toward muscle connective tissue proteins. J. Anim. Sci. 78, 1861-6.

Mitsutake, S. et al. (2001) Purification, characterization, molecular cloning, and subcellular distribution of neutral ceramidase of rat kidney. J. Biol. Chem. 276, 26249-59.

Zhao, F. a. Yu, J. (2001) L-asparginase release from Escherichia coli cells with K2HPO4 and Triton X-100. Biotechnol. Prog. 17, 490-4.

Alderton, A.L. et al. (2004) Bovine metalloprotease characterization and in vitro connective tissue degradation. J. Anim. Sci. 82, 1475-81.
Linke, T. et al. (2005) Isolation and characterization of a microsomal acid retinyl ester hydrolase. J. Biol. Chem. 280, 23287-94.

Solubilization and Characterization of Receptors

Awad, M., Gavish, M. (1989) Heterogeneity between rat and calf peripheral-type benzodia-zepine binding sites: differential sensitivity to Triton X-100. J. Recept. Res. 9, 369-84.

Elberg, G., Ashkenazi, A., Gertler, A. (1989) Solubilization and characterization of lacto¬genic hormone receptor from kidney of lading cow. Mol. Cell. Endocrinol. 61, 77-85.

Roessle, M., Mullen, K. D., Jones E. A. (1989) Cortical benzodiazepine receptor binding in a rabbit model of hepatic encephalopathy: the effect of Triton X-100 on receptor solubiliza-tion. Metab. Brain. Dis. 4, 203-12.

Yoneda, Y. a. Ogita, K. (1989) Labeling of NMDA receptor channels by [3H]MK-801 in brain synaptic membranes treated with Triton X-100. Brain Res. 499, 305-14.

Yoneda, Y., Ogita, K., Ohgaki, T., Uchida, S., Meguri, H. (1989) N-Methyl-D-asparatate-sen¬sitive [3H]glutamate binding sites in brain synaptic membranes treated with Triton X-100. Biochim. Biophys. Acta 1012, 74-80.

Ogita, K., Nabeshima, T., Yoneda, Y. (1990)  [3H]Thienylcyclohexylpiperidine binding activity in brain synaptic membranes treated with Triton X-100. J. Neurochem. 55, 1639-46.

Ishige, K. et al. (1993) Differential effects of Triton X-100 on ligand binding to GABAB receptors in mouse cerebral cortex, cerebellum and whole brain. Gen. Pharmacol. 24, 1533-40.

Kimberley, A. et al. (2007) System of Shigella dysenteriae. Substrate specifity and identification of the heme protein ligands. J. Biol. Chem. 282, 15126-36

Solubilization and Characterization of Photosystems/Photosynthesis Pigments

Gounaris, K., Chapman, D. J. a. Barber, J. (1988) Reconstitution of plastoquinone in the D1 /D2/ cytochrome b-559 photosystem II reaction center complex. FEBS Lett 240, 143-7.

Hermann, P., Hladik, J. a. Sofrova, D. (1988) Effect of detergents on thylakoid membranes of chloroplasts. Photosynthetica 22, 411-22.

Mansfield, R. W. a. Evans, M. C. W. (1988) EPR characteristics of the electron acceptors Ao, A1, and (iron-sulfur)X in digitonin and Triton X-100 solubilized pea Photosystem I. Isr. J. Chem. 28, 97-102.

Montoya, G. et al. (1994) Detergent-induced reversible denaturation of the photosystem II reaction center: implications for pigment-protein interactions. Biochemistry 33, 11798-804.

Solubilization and Characterization of Various Proteins/Protein Complexes

Weiner, J.S. a. Rudy, B. (1988) Effects of detergent on the binding of solubilized sodium channels to immobilized wheat germ agglutinin: structural implications. Biochim. Biophys. Acta 944, 521-6.

Paternostre, M. T., Lowry, R. J., Blumenthal, R. (1989) PH-dependent fusion of reconstituted vesicular stomatitis virus envelopes with Vero cells. Measurement by dequenching of fluor¬escence. FEBS Lett. 243, 251-258.

Shiao, Y. J., Chen, J. C., Wang, C. T. (1989) The solubilization and morphological change in human platelets in various detergents. Bio¬chim. Biophys. Acta 980, 56-68.

Turner, C. E., Shotton, D. M. (1989) Effects of capping on the non-ionic detergent solubility of rat thymocyte glycoproteins. Eur. J. Cell. Biol. 50, 324-32.

Gonzalez-Manas, J.M., Virto, M.D. a.Gurtubay, J.I.G. a. Goni, F.M. (1990) The interac¬tion of Triton X-100 with purple membranes. Detergent binding, spectral changes and mem¬brane solubilization. Fur. J. Biochem. 188, 673-8.

Mo, C. et al. (2002) Protein-protein interactions among C-4 demethylation enzymes involved in yeast sterol biosynthesis. PNAS 99, 9739-44.

Protein Assays

Friedenauer, S. a. Berlet, H. H. (1989) Sensitivity and variability of the Bradford protein assay in the presence of detergents. Anal. Biochem. 178, 263-8.

Loeffler, B. M. a. Kunze, H. (1989) Refinement of the Coomassie brilliant blue G assay for quan¬titative protein determination. Anal. Biochem. 177, 100-102.

Rodriguez-Vico, F., Martinez-Cayuela, M., Garcia-Peregrin, E. a. Ramirez, H. (1989) A procedure for eliminating interferences in the Lowry method of protein determination. Anal. Biochem. 183, 275-8.

Immunological Determination Procedures

Ezan, E., Drieu, K. a. Dray, F. (1989) Triton X-100 eliminates plasma proteins interference in a  radioimmunoassay for luteinizing hormone-re¬leasing hormone (LH-RH) and LH-RH analogs. J. Immunol. Methods 122, 291-6.

Khristova, M. L., Busse, T.L., Egorenkova, E.M., Leonov, S. V., Sokolova, M.V., Giteimann, A.K., Herrmann, J., Doehner, L. a. Kharitonenkov, I.G. (1989) Antigenic reactivity of matrix protein and nucleoprotein of influenza virus as detec¬ted by EIA after dissociation with different detergents. Acta Virol. 33, 1-7.

Chemiluminescence Analysis/Fluorometry

Javier, B.F., Luis, G.J., Diequez, C., Weeks, I. a. Woodhead, J.S. (1988) Effect of surfactants on the intensity of chemiluminescence emission from acridinium labeled proteins. J. Biolumin. Chemilumin. 2, 121-8.

Baeyens, W., Bruggeman, J. a. Lin, B. (1989) Enhanced chemiluminescence detection of some dansyl amino acids in liquid chromato¬graphy. Chromatographia 27, 191-3.

Bayens, W.R.G., Ling, B.L., Corbisier, V. a.  Raemdonck, A. (1990)  Enhanced fluorescence from o-phthalaldehyde and fluorescamine flu¬orophores using Triton and ß-cyclodextrin. Anal. Chim. Acta 234, 187-92.

Cell Culture Techniques

Hommel, R., Goetzrath, M. a. Kleber, H. P. (1989) Enzyme production by growing cells of Acineto¬bacter in presence of sophoroselipid and Triton X-100. Acta Biotechnol. 9, 461-5.
Electrophoretic Sepaarations

Persson, H. a. Corneliuson, 0. (1989) Isoelectric focusing of membrane proteins: high resol-ution separation of myelin proteins. Electro¬phoresis 10, 747-51.

Vanfleteren, J. R. (1989) Sequential two-dimensional and acetic/urea/Triton X-100 gel electrophoresis of proteins. Anal. Biochem. 177, 388-91.

Sprott, S., Hammond, K.D. a. Savage, N. (1990) Electrophoretic separation of protein kinases: altered mobility with different crosslinking agents in the presence of certain detergents. Electrophoresis 11, 29-33.

Isolation and Investigation of Lipid Rafts

Röper, K. et al. (2000) Retention of prominin in microvilli reveals distinct cholesterol-based lipid microdomains in the apical plasma membrane. Nature Cell Biology 2, 582-92.

Chamberlaine, L.H. et al. (2001) SNARE proteins are highly enriched in lipid rafts in PC12 cells: implications for the spatial control of exocytosis. PNAS 98, 5619-24.

Kalus, I. et al. (2002) Interaction of syncollin with GP-2, the major membrane protein of pancreatic zymogen granules, and association with lipid microdomains. Biochem. J. 362, 433-42.

Mairhofer, M. et al. (2002) Stomatin is a major lipid.raft component of platelet  granules. Blood 100, 897-904

Sakyo, T. & Kitagawa, T. (2002) Differential localization of glucose transporter isoforms in non-polarized mammalian cells: distribution of GLUT1 but not GLUT3 to detergent-resistant membrane domains. BBA Biomembranes 1567, 165-75.

Schuck, S. et al. (2003) Resistance of cell membranes to different detergents. PNAS 100, 5795-800.

Slimane, T.A. et al. (2003) Raft-mediated trafficking of apical resident proteins occurs in both direct and transcytotic pathways in polarized hepatic cells: role  of distinct lipid microdomains. Mol. Biol. Cell 14, 611-24.

Vetrivel, K.S. et al (2004) Association of -secretase with lipid rafts in post-golgi and endosome membranes. J. Biol. Chem. 279, 44945-54

Garner, A.E. et al. (2008) Visualization of detergent solubilization of membranes: implications for the isolation of rafts. Biophys. J. 94, 1326-40.

Huttner, H.B. et al. (2008) The stem cell marker prominin-1/CD133 on membrane particles in human cerebrospinal fluid offers novel approaches for studying central nervous system disease. Stem Cells 26, 698-705.     

Woudenberg, J. et al. (2010) Lipid rafts are essential for peroxisome biogenesis in HepG2 cells. Hepatology 52, 623-33.

Further Applications

Ashizawa, K., Suzuki, Y. a. Okauchi, K. (1989) Flagellar movement in demembranated prep¬arations of ejaculated fowl spermatozoa. J. Reprod. Fertil. 86, 263-70.

Graham, M. L. II., Bunn, P.A. Jr., Jewett, P.B., Gonzalez-Aller, C. a. Horwitz, K.B. (1989) Simul¬taneous measurement of progesterone recep¬tors and DNA indexes by flow cytometry: characterization of an assay in breast cancer cell lines. Cancer Res. 49, 3934-42.

Hettwer, D. a. Wang, H. (1989) Protein release from Escherichia coli cells permeabilized with guanidine hydrochloride and Triton X100. Bio¬technol. Bioeng. 33, 886-95.

Katada, J., Shingyoji, C. a. Takahashi, K. (1989) Effects of detergents used to demembranate the sea urchin spermatozoa on the reactivated flagellar movement, with special reference to the rotatability of the plane flagellar boat. Cell Struct. Fund. 14, 751-8.

Lasch, J., Hoffmann, J., Omelyanenko, V.G., Klibanov, A.A., Torchilin, V.P., Binder, H. a. Gawrisch, K. (1990) Interaction of Triton X-100 and octyl glucoside with liposomal membranes at sublytic and lytic concentrations. Spectro¬scopic studies. Biochim. Biophys. Acta 1022, 171-80.

Komatsuzawa, H. et al. (1995) Triton X-100 alters the resistance level of methicillin-resistant Staphylococcus aureus to oxacillin. FEMS Microbiol. Lett. 134, 209-12.

Liochev, S.I. et al. (1995) The effect of detergents on the reduction of tetrazolium salts. Arch. Biochem. Biophys. 324, 48-52.

Neu, T.R. (1996) Significance of bacterial surface-active compounds in interaction of bacteria with interfaces. Microbiol. Reviews, March 1996, 151-66.

Molano, F. et al. (1999) Rat liver lysosomal and mitochondrial activities are modified by anabolic-androgenic steroids. Med. Sci. Sports Exerc. 31, 243-50.

Owoyomi, O. et al. (2005) Interaction between sodium dodecylsulphate and Triton X-100: Molecular properties and kinetics investigations. J. Applied Sciences 5, 729-34.

Paul, V. et al. (2008) A novel enzyme immunoassay specific for ABCA1 protein quantification in human tissues and cells. J. Lipid Res. 49, 2259-67.

Roberts, P.L. (2008) Virus inactivation by solvent/detergent treatment using Triton X-100 in a high purity factor VIII.  Biologicals 36, 330-5.

Park, S.H. a. Opella, S.J. (2010) Triton X-100 as the „short-chain lipid“ improves the magnetic alignment and stability of membrane proteins in phosphatidylcholine bilayers for oriented-sample solid-state NMR spectroscopy. J. Am. Chem. Soc. 132, 12552-3.

Fenster schließen
SERVA Markthalle 2020:
Februar - März

• Gel-Medien
• Fluoreszenz-Farbstoffe
• Sicher & Komfortabel
• Probenvorbereitung
• Affinitäts-Chromatographie

Hier geht es zur Aktion

Fenster schließen
Produkt des Monats März:
Tergitol™ 15-S-9

Tergitol™ 15-S-9 - eine biologisch abbaubare Alternative für Triton X-100

→ Hier geht es zur Aktion

SERVA InfoMail - Erhalten Sie die neuesten Informationen

Fenster schließen

Mit der Anmeldung zu »SERVA InfoMail« erhalten Sie Informationen über neue Produkte, Werbeaktionen, Stellenangebote bei SERVA und vieles mehr. Dieser Service ist selbstverständlich kostenlos.
Sie können sich jederzeit wieder abmelden.


Fenster schließen

Mit der Funktion Schnelleinkauf können Sie mit nur einem Klick ein Produkt in Ihren Warenkorb legen. Geben Sie einfach die Kat.-Nr. wie im Katalog angegeben im Format xxxxx.yy ein und klicken Sie auf Go!