Triton x 114

Manufactured by Thermo Fisher Scientific

Sourced in Germany

Triton X-114 is a non-ionic surfactant used in biochemical applications. It is a widely used detergent for the solubilization and extraction of proteins from biological samples.

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Lab products found in correlation

Triton x 100, by Thermo Fisher Scientific (2 mentions) Triton x 114, by Merck Group (2 mentions) Triton x 100, by Merck Group (1 mentions) Hplc grade, by Thermo Fisher Scientific (1 mentions) Sodium carbonate na2co3, by Thermo Fisher Scientific (1 mentions) Acetate buffer, by Merck Group (1 mentions) Tween 20, by Carl Roth (1 mentions) Tween 80, by Carl Roth (1 mentions) Brij 35, by Carl Roth (1 mentions) Nitric acid 65 hno3, by Merck Group (1 mentions) Dichloromethane, by Thermo Fisher Scientific (1 mentions) Methanol ch3oh, by Thermo Fisher Scientific (1 mentions) Colorimetric assay kits, by Horiba (1 mentions) Amicon ultra centrifugal filter, by Merck Group (1 mentions) Dc protein assay, by Bio-Rad (1 mentions) Peptide m agarose, by InvivoGen (1 mentions)

Spelling variants of this product

Triton-X (74 citations) Triton (14 citations)

6 protocols using triton x 114

Optimizing Oil Sludge Remediation Using Surfactants

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Two synthetic surfactants, Triton X-100 and Triton X-114 (Sigma-Aldrich, UK), and a biosurfactant, rhamnolipid (AGAE Technologies, Corvallis, Oregon, USA)], were chosen for the co-solvent selection. Each surfactant was added at a 1:1 S/OS ratio and 2CMC because these surfactants had the maximum ORR values at this ratio and concentration in a previous OSW study with an oil-water separator sludge, WSS (Ramirez and Collins 2018 (link)).
A full-factorial experimental design was used. Three factors were included: Surfactant type (Triton X-100, Triton X-114, rhamnolipid), co-solvent (n-pentane, n-hexane, toluene, cyclohexane, and isooctane; high-purity, HPLC grade, Fisher Scientific) and co-solvent to oil sludge ratio, C/OS, (1:1, 2:1). The response variable was ORR (%). A total of 30 experimental runs in triplicate were analysed. A three-way ANOVA was used with the effect of the three factors. Paired t-tests (α=0.05) were performed for comparison of the means between co-solvents. Minitab 17.3.1 (Minitab Inc.) was used for the statistical analyses.

Ramirez D., Shaw L.J, & Collins C.D. (2020). Oil sludge washing with surfactants and co-solvents: oil recovery from different types of oil sludges. Environmental Science and Pollution Research International, 28(5), 5867-5879.

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Trace Metal Spiking in Water Samples

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Potassium iodide (KI), sulfuric acid (H₂SO₄), sodium carbonate Na₂CO₃, and Triton X-114 were purchased from Fisher Scientific and used without further purification. House distilled water was further purified with a D2798 Barnstead water purification system and was used for all standard solutions. A 1000 mg/L Cd²⁺ atomic absorption standard solution was purchased from Acros Organics and diluted to desired concentrations. Acetate buffer (pH 4.65, 0.2 M) was purchased from Sigma Aldrich. Mercury and bismuth solutions were made by diluting mercuric nitrate (HgNO₃, J.T Baker Chemical Co.) and a 1000 mg/L bismuth (Bi³⁺) atomic absorption standard solution (Sigma) in deionized water. Tap water samples were collected in Crosley Tower at the University of Cincinnati on July 18^th, 2014. River water samples were collected from the Little Miami River (Cincinnati, Ohio) and Burnet Woods Pond (Cincinnati, Ohio) on July 18^th, 2014. No further treatment of the water samples was done and they were immediately used. All water samples were spiked with various concentrations of Cd²⁺ standard.

Rusinek C.A., Bange A., Papautsky I, & Heineman W.R. (2015). Cloud Point Extraction for Electroanalysis: Anodic Stripping Voltammetry of Cadmium. Analytical chemistry, 87(12), 6133-6140.

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Hydrophobic Membrane Modification for ATPS

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As hydrophobic membrane materials, polypropylene (PP ACCUREL^®, 3M, Wuppertal, Germany), polyvinylidene fluoride (PVDF, Pall, New York, NY, USA), polytetrafluoroethylene (PTFE, Sartorius, Göttingen, Germany) and hydrophobized polyether sulfone (hydrophobized PES, Sartorius, Göttingen, Germany) with a mean pore diameter of approximately 0.4 µm were investigated. For modification, the membrane was incubated overnight in the LP of each ATPS supplemented with different surfactants (Tween20, Tween80, Brij 35 (Carl Roth, Karlsruhe, Germany), TritonX-100 and TritonX-114 (Fisher Scientific, Pittsburgh, PA, USA). The used surfactant concentration (1 w%) was a trade-off between surfactant solubility in the LP and membrane wettability by the solution [37 ]. After incubation the modified membrane was dried before use for at least 1 h.

Kruse T., Schmidt A., Kampmann M, & Strube J. (2019). Integrated Clarification and Purification of Monoclonal Antibodies by Membrane Based Separation of Aqueous Two-Phase Systems. Antibodies, 8(3), 40.

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Synthesis and Photolysis of XDPAdeCage

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The XDPAdeCage chelator (see Scheme 1) was synthesized as described previously.^{42 ,43 (link)} The substrate strand (/5FAM/-ACTCACTATrAGGAAGAGATGGACGTG-/3BHQ/), and enzyme strand (CACGTCCATCTCTTCTCCGAGCCGGTCGAAATAGTGAGT-/3Dab/) of the 8–17 DNAzyme were synthesized by the IDT. 4-(2-Hydroxyethyl)-1-piperizineethanesulfonic acid (HEPES), tris(hydroxymethyl)aminomethane (Tris), sodium chloride (NaCl, 99.8%), zinc chloride (ZnCl₂,99.8%), dichloromethane (CH₂Cl₂), methanol (CH₃OH), bovine newborn calf serum (BNCS), 4-(2-pyridylazo)resorcinol (PAR), and Triton X-114 were purchased from Fisher Scientific. Trace element serum L-2 RUO was purchased from Sero. Nitric acid (HNO₃ 65%) was purchased from Merck. The Zn²⁺ stock solution was prepared from ZnCl₂ using Millipore water. CH₃OH was routinely used as a co-solvent for preparing the stock solutions of the chelator. Photolysis was carried at 25 °C in a 1.0 cm quartz cuvette illuminated by 3 W UV light-emitting diode (LED) purchased from LED Engin (365 nm, 200 mW) powered by a 700 Ma LuxDriveFlexBox using a variable DC source set at 12 V DC.

Xing S., Lin Y., Cai L., Basa P.N., Shigemoto A.K., Zheng C., Zhang F., Burdette S.C, & Lu Y. (2021). Detection and Quantification of Tightly Bound Zn2+ in Blood Serum Using a Photocaged Chelator and a DNAzyme Fluorescent Sensor. Analytical chemistry, 93(14), 5856-5861.

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Liver Triglyceride Quantification Protocol

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Frozen liver tissue (20–50 mg) was homogenized in 1 mL chloroform/methanol (v/v = 2:1) with vigorous shaking for 1 hour at room temperature. Subsequently, 200 μL Millipore water was added into the mix and centrifuged at 3000 × g for 5 minutes. The lower lipid phase was collected and dried in a fume hood overnight, and the pellet was dissolved in 60 μL tert-butanol and 40 μL Triton X-114 (Thermo)/methanol (v/v = 2:1) mix. Liver TG levels were measured with colorimetric assay kits, following the manufacturer’s instructions (Pointe Scientific, Canton, MI), and normalized to tissue weight. The tert-butanol and Triton X-114/methanol mixture was used as a blank control.

Li Y., Jiang J.X., Fan W., Fish S.R., Das S., Gupta P., Mozes G., Vancza L., Sarkar S., Kunimoto K., Chen D., Park H., Clemens D., Tomilov A., Cortopassi G, & Török N.J. (2022). Shc Is Implicated in Calreticulin-Mediated Sterile Inflammation in Alcoholic Hepatitis. Cellular and Molecular Gastroenterology and Hepatology, 15(1), 197-211.

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Isolation and Purification of IgA Subclasses

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IgA was isolated from pooled sera of healthy donors using peptide M agarose (Invivogen) according to the manufacturer’s instructions. After an additional washing step with 0.1 M glycine buffer (pH 5.0) to remove nonspecifically bound proteins, bound IgA was eluted with 0.1 M glycine buffer (pH 2.7), immediately neutralized using 1 M Tris buffer (pH 9), and dialyzed against phosphate-buffered saline (PBS) (pH 7.2). IgA1 and IgA2 were separated using jacalin agarose (Thermo Scientific) according to the manufacturer’s instructions. IgA2 was collected with the flow through. IgA1 bound to the agarose and was eluted with 0.1 M galactose buffer. Both IgA fractions were concentrated and buffered to PBS using Amicon Ultra Centrifugal Filters (Merck) followed by treatment with Triton-X114 (Sigma) to remove possible traces of endotoxins. Traces of Triton-X114 were subsequently removed with detergent removal columns (Thermo Scientific). Protein concentration was determined with the DC protein assay (Bio-Rad). Purity of IgA1 and IgA2 was tested with western blot analysis using antibodies against IgA1 and IgA2 (Southern biotech), as well as Coomassie staining to exclude contaminations by other serum proteins.
IgA aggregates were obtained by heat aggregation at 63 °C for 30 min.

Steffen U., Koeleman C.A., Sokolova M.V., Bang H., Kleyer A., Rech J., Unterweger H., Schicht M., Garreis F., Hahn J., Andes F.T., Hartmann F., Hahn M., Mahajan A., Paulsen F., Hoffmann M., Lochnit G., Muñoz L.E., Wuhrer M., Falck D., Herrmann M, & Schett G. (2020). IgA subclasses have different effector functions associated with distinct glycosylation profiles. Nature Communications, 11, 120.

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