282103
Triton™ X-100 reduced
Sinónimos:
Polyoxyethylene (10) isooctylcyclohexyl ether
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About This Item
Fórmula lineal:
4-(C8H17)C6H10(OCH2CH2)nOH, n~10
Número de CAS:
MDL number:
UNSPSC Code:
12162002
NACRES:
NA.23
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Quality Level
refractive index
n20/D 1.473 (lit.)
density
1.029 g/mL at 25 °C (lit.)
SMILES string
CC(C)(C)CC(C)(C)C1CCC(CC1)OCCOCCOCCOCCOCCOCCOCCO
InChI
1S/C28H56O8/c1-27(2,3)24-28(4,5)25-6-8-26(9-7-25)36-23-22-35-21-20-34-19-18-33-17-16-32-15-14-31-13-12-30-11-10-29/h25-26,29H,6-24H2,1-5H3
InChI key
QQJNBKDKLMCALZ-UHFFFAOYSA-N
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General description
Triton™ X-100 reduced (RTX-100) is formed when the benzene moiety of TX-100 is fully hydrogenated to a cyclohexane derivative. RTX-100 might enhance enzyme digestion and is also known to exhibit some effects on the photoisomerization of bacteriorhodopsin.
Triton™ X-100 reduced is a versatile nonionic surfactant with a hydrophilic polyethylene oxide chain, widely utilized as a laboratory detergent. Its applications span various areas, including cell biology and biochemical research. This detergent is commonly employed for tasks such as cell lysis to extract proteins or organelles, permeabilizing the membranes of living cells, and serving as a crucial component in lysis buffers. Triton™ X-100 plays a key role in the isolation of lipid rafts, contributing to enhanced solubility and dispersibility of substances. With a reduced polyoxyethylene content of approximately 10, Triton™ X-100 exhibits excellent wetting properties and facilitates emulsification.
In biochemical and cell biology research, Triton™ X-100 is instrumental in solubilizing membrane-bound proteins and isolating lipid rafts. Its unique properties allow for the preservation of the native conformation of proteins obtained from cellular membranes in solution. Triton™ X-100 reduced is derived from the full hydrogenation of the benzene moiety of TX-100 to a cyclohexane derivative. This modified version, RTX-100, has demonstrated potential in enhancing enzyme digestion and influencing the photoisomerization of bacteriorhodopsin, showcasing its versatility and utility in advanced research applications.
In biochemical and cell biology research, Triton™ X-100 is instrumental in solubilizing membrane-bound proteins and isolating lipid rafts. Its unique properties allow for the preservation of the native conformation of proteins obtained from cellular membranes in solution. Triton™ X-100 reduced is derived from the full hydrogenation of the benzene moiety of TX-100 to a cyclohexane derivative. This modified version, RTX-100, has demonstrated potential in enhancing enzyme digestion and influencing the photoisomerization of bacteriorhodopsin, showcasing its versatility and utility in advanced research applications.
Application
Triton™ X-100 reduced has been used:
- as a component of LB-TT for the extraction of total protein from rat brains
- in ADP-Glo assay and Cytophos adenosine triphosphatase (ATPase) assay
- in phosphate-buffered saline (PBS) solution for the permeabilization of fibroblasts in 5′ ethynyl uridine staining, immunofluorescence, and immunolabeling
Features and Benefits
- Non-ionic surfactant
- Reduced polyoxyethylene content (~10)
- Improves solubility and dispersibility of substances
- Excellent wetting properties
- Enhances emulsification
- High purity product for research applications
Other Notes
For additional information on our range of Biochemicals, please complete this form.
Legal Information
Triton is a trademark of The Dow Chemical Company or an affiliated company of Dow
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Referencia del producto
Descripción
Precios
signalword
Warning
Hazard Classifications
Aquatic Chronic 2 - Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Storage Class
10 - Combustible liquids
wgk_germany
WGK 3
flash_point_f
235.4 °F - closed cup
flash_point_c
113 °C - closed cup
ppe
Eyeshields, Gloves, type ABEK (EN14387) respirator filter
Certificados de análisis (COA)
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S J Milder et al.
Biochemistry, 30(7), 1751-1761 (1991-02-19)
Time-resolved difference spectra have been obtained for the photocycle of delipidated bacteriorhodopsin monomers (d-BR) in six different detergent micelle environments that were prepared by two new detergent-exchange techniques. A global kinetic analysis of the photocycle spectra for d-BR in each
J Fernandez et al.
Analytical biochemistry, 218(1), 112-117 (1994-04-01)
An improved and simplified procedure for enzymatic digestion of proteins bound to polyvinylidene difluoride (PVDF) membranes for obtaining internal protein sequence data is presented. This improved procedure is compatible with various enzymes (trypsin, endoproteinase Lys-C, endoproteinase Glu-C, and clostripain) and
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A procedure for the generation and isolation of internal peptide fragments for less than 10 micrograms of protein bound to either polyvinylidene difluoride (PVDF) or nitrocellulose membranes after electrophoretic transfer from sodium dodecyl sulfate-polyacrylamide gels (SDS-PAGE) is presented. This technique
G E Tiller et al.
Analytical biochemistry, 141(1), 262-266 (1984-08-15)
The ultraviolet-light absorption and fluorescence of Triton X-100 were virtually eliminated by hydrogenation to its reduced cyclohexyl analog, RTX-100. The critical micelle concentration of RTX-100 was 12% higher than that of Triton X-100. RTX-100 and Triton X-100 were quite similar
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