TWEEN® 20
Tween 20 ist ein Polyoxyethylen-Sorbitolester mit ca. 20 Einheiten Ethylenoxid pro Einheit Sorbitol. Die Fettsäurezusammensetzung ist heterogen mit Laurinsäure als Hauptkomponente (40 - 60 %).
Tween 20 ist bei immunologischen Bestimmungsverfahren von Bedeutung. Es unterdrückt effektiv unspezifische Reaktionen zwischen Antikörpern, Antigenen und anderen Molekülen.
Tween 20 kann auch als Lösungsvermittler in der Membranchemie und als Additiv für Zellkulturmedien eingesetzt werden.
In der thiophilen Interaktionschromatographie hat sich Tween 20 bei der Elution von stark adsorbierten Proteinen bewährt.
Weitere nennenswerte Anwendungen sind z. B. die turbidimetrische Bestimmung von lipolytischen Enzymen und die Dichtegradientenzentrifugation von Viren.
TWEEN 20 ist ein eingetragenes Warenzeichen der CRODA International Plc.
Synonyme: Polysorbat 20, Montanox 20, PEG (20) Sorbitanmonolaureat
CAS-Registriernummer: [9005-64-5]
Relative Molmasse (Mr): ca. 1200
Klassifizierung: Nichtionisches Tensid
Literaturangaben:
- Kritische mizellare Konzentration (CMC): 0,059 mM
- Trübungspunkt (cp): 76 °C (3 % in 1 N NaCl-Lösung)
- Partielles spezifisches Volumen: 0,869 cm3/g
- Hydrophil-Lipophilie-Gleichgewicht (HLB): 16,7
BibliographIE
Immunologische Bestimmungsverfahren
Hunger, H.D., Flachmeier, C., Schmidt, G., Behrendt, G. a. Coutelle, C. (1988) A protein-free blocking system for the covalently binding matrix cyanuric chloride-activated paper in immunological procedures. J. Biochem. Biophys. Methods 17, 43-50
Ming, C.H. a. Fan, Y.S. (1988) Enhancement of anti-phospholipid antibody activity by Tween 20. J. Immunol. Methods 109, 253-5.
Mohammad, K. a. Esen, A. (1989) A blocking agent and a blocking step are not needed in ELISA, immunostaining dot-blots and Western blots. Immunol. Methods 117, 141-5.
Thean, E.T. a. Toh, B.H. (1989) Western immuno‑blotting: temperature-dependent reduction in background staining. Anal. Biochem. 177, 256-8.
Tovey, E.R., Ford, S.A. a. Baldo, B.A. (1989) Enhanced immunodetection of blotted house dust mite protein allergens on nitrocellulose following blocking with Tween 20. Electrophoresis 10, 243-9.
Tsang, V.C.W. a. Wilkins,P.P. (1991) Optimum dissociation condition for immunoaffinity and preferential isolation of antibodies with high specific activity. J. Immunol. Methods 138, 291-9.
Mushens, R.E. et al. (1993) Quantitation of monoclonal antibodies by ELISA: The use of purified mouse IgG and mouse IgM monoclonal antibodies as standards in a quantitative ELISA measuring monoclonal antibodies produced by cell culture. J.Immunol.. Methods 162, 77-83.
Cheng, H.M. (1996) Tween 20 selectively enhances naturally occurring anticardiolipin antibody binding in ELISA procedures. J. Immunol. Methods 191, 87-91.
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.
Solubilisierung und Charakterisierung von Enzymen
Lund, S., Orlowski, S., De Foresta, B., Champed, P., Le Maire a. M., Moeller, J. V. (1989) Detergent structure and associated lipid as determinants in the stabilization of solubilized Ca2+-ATPase from sarcoplasmic reticulum. J. Biol. Chem. 264, 4907-15.
Stocklein, W. et al. (1993) Purification and properties of a lipase from Penicillium expansum. Biochim. Biophys. Acta 1168, 181-9.
Schilstra, M.J. et al. (1994) Effect of non-ionic detergents on lipoxygenase catalysis. Lipids 29, 225-31
Mitsutake, S. et al. (2001) Purification, characterization, molecular cloning, and subcellular distribution of neutral ceramidase of rat kidney. J. Biol. Chem. 276, 26249-59.
Zellkulturtechniken
Baykusheva, S. a. Ilieva, K. (1988) Sporulation and extracellular alkaline protease activity of Bacillus subtilis 168 grown in the presence of Tween. Biotekhnol. Biotekh. 4, 22-4.
Gomez-Lopez, A. et al. (2005) Analysis of the influence of Tween concentration, inoculum size, assay medium, and reading time on susceptibility testing of Aspergillus spp. J. Clin. Microbiol.43, 1251-5.
Chromatographische und elektrophoretische Trennungen
El Rassi, Z. (1989) High performance liquid chromatography of proteins with silica-bound sulfone-thioether functions. BioChromatography 4, 184-90.
Matsubara, N. et al. (1995) Separation of eleven angiotensin II analogs by capillary electrophoresis with a nonionic surfactant in acidic media. Electrophoresis 16, 580-3.
Weitere Anwendungen
Watanabe, T., Kitabatake, N. a. Doi, E. (1988) Protective effects of nonionic surfactants against denaturation of rabbit skeletal myosin by freezing and thawing. Agric. Biol. Chem. 52, 2517-23.
Boeye, A. a. De Rees, A. (1989) Wall effects in sucrose density gradient centrifugation of viruses. Arch. Virol. 107, 77-84.
Takahashi, T., Mitsuda, T. a. Okuda, K. (1989) An alternative nonradioactive method for labeling DNA using biotin. Anal. Biochem. 179, 77-85.
Von Tigerstrom, R. G. a. Stelmaschuk, S. (1989) The use of Tween 20 in a sensitive turbidimetric assay of lipolytic enzymes. Can. J. Micro-biol. 35, 511-4.
Holloway, P.J. et al. (1992) Effects of some non-ionic polyoxyethylene surfactants on uptake of ethirimol and diclobutrazol from suspension formulations applied to wheat leaves. Pesticide Science 34, 109-18.
Knoche, M. a. Bukovac, M.J. (1992) Surfactants influence foliar absorption of gibberellic acid by sour cherry leaves. J. Amer. Soc. Hort. Sci. 117, 80-4.
Neu, T.R. (1996) Significance of bacterial surface-active compounds in interaction of bacteria with interfaces. Microbiol. Reviews, March 1996, 151-66.
Das, A. et al. (1999) Retinal neovascularization is suppressed with a matrix metalloproteinase inhibitor. Arch. Ophthalmol. 117, 498-503.
Slawecki, R.A. et al. (2002) Novel fungitoxicity assays for inhibition of germination-associated adhesion of Botrytis cinerea and Puccinia recondite spores. Appl. Environ. Microbiol. 68, 597-601.
Schuck, S. et al. (2003) Resistance of cell membranes to different detergents. PNAS 100, 5795-800.
Yoshimura, S.H. et al. (2011) Fluorescence labeling of carbon nanotubes and visualization of a nanotube-protein hybrid under fluorescence microscope. Biomacromolecules 12, 1200-4.