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Triton X-114

Triton X-114 is a non-ionic detergent commonly used in biochemical and cell biology research.
It is effective for solubilizing membrane proteins and has been widely employed in protein purification, phase separation, and other applications.
The PubCompare.ai tool can help researchers identify the most accurate and reproducible Triton X-114 protocols from literature, preprints, and patents, enhancing the quality and accuracy of their work.
By leveraging AI-driven comparisons, PubCompare.ai enables researchers to optimize their Triton X-114 processes and take their research to the next level.

Most cited protocols related to «Triton X-114»

Protein Expression Regulation by TetR-DOZI System

Cited 8 times

Western blotting for SpCas9 and T7 RNAP was described previously ^{13 (link)}. To determine regulation of target protein expression by the TetR- or TetR-DOZI-aptamer system, parasites cultured with 0 nM or 50 nM aTc for 72 h were saponin-lysed, washed with 1 × PBS, and proteins solubilized in lysis buffer containing 4% sodium dodecyl sulfate (SDS) and 0.5% Triton X-114 in 1 × PBS. Protein extracts were mixed with loading buffer containing SDS and dithiothreitol (DTT) and loaded onto Mini-PROTEAN TGX Precast Gels (4–15% gradient; Bio-Rad 4,561,084) in Tris–Glycine buffer. After separation by polyacrylamide gel electrophoresis (PAGE), proteins were transferred to a polyvinylidene fluoride (PVDF) membrane using the Mini Trans-Blot Electrophoretic Transfer Cell system (Bio-Rad) per the manufacturer’s instructions and blocked with 100 mg/mL skim milk in 1 × TBS/Tween 20. PVDF membrane-bound proteins were first probed with mouse anti-HA (1:3000; Sigma, H3663) and rabbit anti-GAPDH (1:5000; Abcam, AB9485) primary antibodies and anti-mouse (1:5000; Thermo Fisher Scientific, 62–6520) and anti-rabbit (1:5000; Cell Signaling, 7074S) horseradish peroxidase (HRP)-conjugated secondary antibodies. Following incubation in SuperSignal West Pico Chemiluminescent substrate (Thermo Fisher Scientific, PI34080), protein blots were imaged and analysed using the ChemiDoc MP System and Image Lab 5.2.0 (Bio-Rad).

Nasamu A.S., Falla A., Pasaje C.F., Wall B.A., Wagner J.C., Ganesan S.M., Goldfless S.J, & Niles J.C. (2021). An integrated platform for genome engineering and gene expression perturbation in Plasmodium falciparum. Scientific Reports, 11, 342.

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Publication 2021

Antibodies Buffers Cells Dithiothreitol Electrophoresis GAPDH protein, human Gels Glycine Horseradish Peroxidase Membrane Proteins Milk, Cow's Mus Parasites Polyacrylamide Gel Electrophoresis polyvinylidene fluoride Proteins Protein Targeting, Cellular Rabbits Saponin Sulfate, Sodium Dodecyl Tissue, Membrane Triton X-114 Tromethamine Tween 20

Expression and Purification of D381C E2 Protein

Cited 7 times

The D381C E2 protein (E2) was prepared as previously described.^{13 (link)} D381C is an E2 mutant with a non-native cysteine introduced to the internal cavity of the nanoparticle for site-directed functionalization. Briefly, proteins were expressed in E. coli, cells were lysed, and soluble cell lysates were applied to a HiPrep Q Sepharose anion exchange column (GE Healthcare) followed by a Superose 6 (GE Healthcare) size exclusion column for purification. The purified proteins were analyzed by dynamic light scattering (Zetasizer Nano ZS, Malvern) for size measurements. Electrospray ionization mass spectrometry and SDS-PAGE were performed for molecular weight and purity confirmation. Final protein preparations were stored in 50 mM potassium phosphate at pH 7.4 with 100 mM NaCl at 4°C for short-term and −80°C for long-term storage.
Lipopolysaccharide (LPS), a component of gram-negative bacterial cell walls, is recognized by Toll-like receptor 4 expressing immune cells (e.g. DCs), causing potentially unwanted immune activation. Residual LPS was removed following the method described by Aida and Pabst.^{51 (link)} Briefly, Triton X-114 (Sigma) was added to the purified protein at 1% (v/v), chilled to 4°C, vortexed vigorously, and heated to 37°C. The mixture was then centrifuged at 18,000 × g and 37°C for 30 seconds, and the protein-containing aqueous portion was separated from the detergent. This total process repeated ≥ 8 times. Residual Triton was removed with detergent removal spin columns (Pierce). LPS levels were below 8 EU (0.8 ng) per milligram of E2 protein (LAL ToxinSensor gel clot assay, Genscript), significantly lower than levels that activate DCs in our assays.

Molino N.M., Anderson A.K., Nelson E.L, & Wang S.W. (2013). Biomimetic Protein Nanoparticles Facilitate Enhanced Dendritic Cell Activation and Cross-Presentation. ACS nano, 7(11), 9743-9752.

Publication 2013

Anions Biological Assay Cells Cellular Structures Clotrimazole Cysteine Dental Caries Detergents Escherichia coli Gram Negative Bacteria Lipopolysaccharides Neoplasm Metastasis potassium phosphate Proteins SDS-PAGE Sepharose Sodium Chloride Spectrometry, Mass, Electrospray Ionization TLR4 protein, human Triton X-114

Isolation and Fractionation of Flagella

Cited 7 times

Flagellar isolation using the dibucaine method and flagellar amputation by pH shock were performed as previously described by Witman (1986) (link) and Lefebvre (1995) (link), respectively. Isolated flagella were extracted with 1% NP-40 Alternative (EMD) for 20 min on ice, and the suspension was separated by centrifugation into a pellet containing the axonemes and a supernatant consisting of the membrane-plus-matrix. For MS quantitation of BBS1 and IFT81 in the membrane-plus-matrix, the AQUA peptide technique was used (see Quantitative MS and Fig. S4). The membrane-plus-matrix was further separated by sucrose gradient centrifugation (36,000 rpm for 12.5 h at 4°C on an SW41 rotor [Beckman Coulter]), and fractions were analyzed by SDS-PAGE and Western blotting. For phase partitioning, isolated flagella were extracted using 1% Triton X-114 for 20 min on ice; after removal of the axonemes by centrifugation (Witman, 1986 (link)), the supernatant was incubated briefly at 37°C, and phases were separated by centrifugation (3,300 g for 10 min at RT). The AP was treated with 1% Triton X-114, the DP was diluted with buffer, and the phase separation was repeated to yield the final APs and DPs.

Lechtreck K.F., Johnson E.C., Sakai T., Cochran D., Ballif B.A., Rush J., Pazour G.J., Ikebe M, & Witman G.B. (2009). The Chlamydomonas reinhardtii BBSome is an IFT cargo required for export of specific signaling proteins from flagella. The Journal of Cell Biology, 187(7), 1117-1132.

Publication 2009

Amputation Axoneme Bardet-Biedl syndrome 1 Buffers Centrifugation Dibucaine Flagella Nonidet P-40 Peptides SDS-PAGE Shock Sucrose Tissue, Membrane Triton X-114

Immunofluorescent Analysis of Lymph Nodes

Cited 6 times

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Publication 2017

Acetone Antibodies Biotin Cloning Vectors CR1 protein, human Goat Mice, House Microscopy, Confocal Microtomy Nodes, Lymph paraform Rabbits Serum Streptavidin Sucrose Tissues Triton X-114

Fabrication of DNA Nanostructures

Cited 5 times

The design-specific staple strands were purchased from IDT Technologies in 250 μM scale. The sequence of the staple strands and the design is reported in the Supplementary Information. The p7308 scaffold strand was produced from M13 phage replication in Escherichia coli and was endotoxin-purified using Triton X-114 as described previously13 (link).
For the synthesis of DNs, 10 nM p7308 scaffold was mixed with tenfold excess of staples in TE buffer (5 mM Tris and 1 mM EDTA) containing 10–20 mM MgCl₂. The amount of MgCl₂ varied with the structure: DN1 (10 mM), DN2 (6 mM), DN3 (10 mM), DN4 (10 mM), DN5 (10 mM), DN6 (12 mM), DN7 (14 mM), DN8 (12 mM) and DN9 (6 mM). The solutions were subjected to a thermal annealing ramp on a Tetrad 2 Peltier thermal cycler (Bio-Rad) according to the following schedule: incubate at 65 °C for 15 min, decrease to 50 °C, incubate at 50 °C for 6 h 30 min and decrease to 40 °C at 6 h 30 min °C⁻¹. The quality of folding was analysed by AGE. Solutions of folded DN were concentrated tenfold using a 30k MWCO Amicon Ultra centrifugal filter device (Millipore) and then purified by glycerol gradient ultracentrifugation30 (link). The 45% and 15% glycerol solutions were made in 1 × TE buffer containing the same levels of MgCl₂ as required for folding. The glycerol fractions containing nanostructures was concentrated and buffer exchanged to remove glycerol using a 30k MWCO Amicon Ultra centrifugal filter device. Following purification, the stock solution was diluted appropriately for TEM imaging to verify quality. The stock concentration was determined by ultraviolet absorbance at 260 nm on a Nanodrop spectrophotometer (Thermo Scientific), assuming that A₂₆₀=1 for 50 μg ml⁻¹ DNs. Stock solutions were stored at 4 °C until use.

Ponnuswamy N., Bastings M.M., Nathwani B., Ryu J.H., Chou L.Y., Vinther M., Li W.A., Anastassacos F.M., Mooney D.J, & Shih W.M. (2017). Oligolysine-based coating protects DNA nanostructures from low-salt denaturation and nuclease degradation. Nature Communications, 8, 15654.

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Publication 2017

Anabolism Bacteriophage M13 Buffers DNA Replication Edetic Acid Endotoxins Escherichia coli Glycerin Magnesium Chloride Medical Devices Staple, Surgical Triton X-114 Tromethamine

Most recents protocols related to «Triton X-114»

Parasite Membrane Protein Extraction

Schizont-stage parasites were lysed with 0.1% saponin and washed 3 times with ice-cold PBS. Parasite pellets were resuspended in ice-cold lysis buffer (1× PBS, 1% Triton X-114 [Thermo Scientific 28332], 2 mM EDTA, 1× protease inhibitors [Pierce A32955]) and incubated on ice for 30 min. Cell debris was removed by a 10-minute centrifugation at 16,000 × g, 4°C. Supernatant was transferred to a fresh Eppendorf tube, incubated for 2 min at 37°C to allow phase separation, and centrifuged for 5 min at 16,000 × g at room temperature. The top (aqueous) layer was transferred to another tube. The interphase was removed to avoid cross-contamination between the layers. The bottom (detergent) layer was resuspended in 1× PBS-0.2 mM EDTA to equalize the volumes of the two fractions. Both fractions were subjected to methanol-chloroform precipitation, resuspended in PBS containing 2× NuPAGE lithium dodecyl sulfate sample buffer, boiled for 5 min at 95°C, and analyzed by Western blotting. Quantification of band intensities was done using Image Studio Lite. The percentage of each GFP fusion protein that was membrane bound was calculated and normalized to the percentage of endogenous Atg8 in the membrane.

Walczak M., Meister T.R., Nguyen H.M., Zhu Y., Besteiro S, & Yeh E. (2023). Structure-Function Relationship for a Divergent Atg8 Protein Required for a Nonautophagic Function in Apicomplexan Parasites. mBio, 14(1), e03642-21.

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Publication 2023

Buffers Cells Centrifugation Chloroform Cold Temperature Detergents dodecyl sulfate, lithium salt Edetic Acid Interphase Methanol Parasites Pellets, Drug Protease Inhibitors Proteins Saponin Schizonts Tissue, Membrane Triton X-114

Recombinant Nanobody Purification Protocol

The sequences of proteins were designed according to the literature [4 (link),16 (link),36 (link),37 (link)]. Coding sequences were subcloned into the E. coli periplasmic expression vector pET-22b(+) with 6 His-tag in the C-terminal. Rosetta E. coli containing the plasmid were grown at 37 °C in LB plus ampicillin. After inducing with 1 mM IPTG at 30 °C for 16 h, the cells were harvested by centrifugation, resuspended in buffer (50 mM Tris, 300 mM NaCl, pH = 8.0), and lysed by ultrasonic. The periplasmic fraction was isolated by centrifugation at 10,000 g for 20 min at 4 °C and then loaded onto Ni-NTA in buffer (50 mM Tris, 300 mM NaCl, 10 mM imidazole, pH = 8.0). Proteins were eluted by a gradient to 50 mM Tris, 300 mM NaCl, 500 mM imidazole, 10% glycerin, pH = 8.0. The eluted proteins were loaded onto a Superdex S-200 column to increase purity. Recombinant nanobodies were assessed by 15% SDS-PAGE. The purified proteins were stored at −80 °C.
To remove bacterial endotoxin, proteins were immobilized on HisTrap HP 5 mL column (GE Healthcare) in PBS. The proteins were washed with PBS containing 0.1% Triton X-114, and eluted with LPS-free PBS with 500 mM imidazole. Imidazole was removed by dialysis. LPS concentration was measured using an LAL Chromogenic Endotoxin Quantitation Kit (Thermo Fisher Scientific, Waltham, MA, USA), and all proteins were LPS purified (<2 IU/mg).

Zhou Y., Lu X., Wang X., Ying T, & Tan X. (2023). Potent Therapeutic Strategies for COVID-19 with Single-Domain Antibody Immunoliposomes Neutralizing SARS-CoV-2 and Lip/cGAMP Enhancing Protective Immunity. International Journal of Molecular Sciences, 24(4), 4068.

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Publication 2023

Amino Acid Sequence Ampicillin azo rubin S Buffers Cells Centrifugation Cloning Vectors Dialysis Endotoxins Escherichia coli Exons Glycerin imidazole Isopropyl Thiogalactoside Periplasm Plasmids Proteins SDS-PAGE Sodium Chloride Triton X-114 Tromethamine Ultrasonics VHH Immunoglobulin Fragments

Antifungal Activity of PHMB Assessed

PHMB and PHMB labelled with rhodamine (PHMB–rhodamine) were obtained from Tecrea Ltd, UK and stock solutions were made in sterile dH₂O. Terbinafine (Sigma-Aldrich) stock solutions were made in 80% ethanol. To determine a suitable concentration range for the membrane permeabilisation assays, the minimum inhibitory concentrations of PHMB, negative control (Terbinafine) and positive control (Triton x-114) were determined against all fungal species in RPMI-1640, 2% glucose using the broth microdilution method^{20 (link),21 (link)}. A 96 well microplate with serial dilutions of drug was inoculated with fungi (S. cerevisiae, F. oxysporum, P. glabrum and C. albicans R1) at 1 × 10⁴ cells/ml. Plates were incubated at 30 °C for 48 h and absorbance was measured at OD600nm. The lowest concentration of PHMB that inhibited ~ 90% fungal growth was determined as the MIC₉₀ and ~ 50% growth was determined as the MIC₅₀ respectively.

Ntow-Boahene W., Papandronicou I., Miculob J, & Good L. (2023). Fungal cell barriers and organelles are disrupted by polyhexamethylene biguanide (PHMB). Scientific Reports, 13, 2790.

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Publication 2023

Biological Assay Candida albicans Cells Ethanol Fungi Glucose Minimum Inhibitory Concentration Pharmaceutical Preparations Rhodamine Saccharomyces cerevisiae Sterility, Reproductive Technique, Dilution Terbinafine Tissue, Membrane Triton X-114

Immunization with Engineered Capsid Proteins

10–12 week-old mice (C57BL/6) were used for immunization. Mice were injected intraperitoneally with vehicle (capsid assembly buffer), 5μg of mPNMA2 capsids, or 5μg of mPNMA2 L270QL325Q capsid mutant on day 0. The immunized proteins were not mixed with any adjuvant. Blood was collected on day 21 via the tail vein. A second injection of 5μg of mPNMA2 L270QL325Q capsid mutant and vehicle were performed on day 21 and blood was collected on day 42. Blood was coagulated at 4°C overnight and serum was harvested by centrifuging twice at 2,000g for 10min to collect the supernatant. Endotoxin was removed from the purified protein by Triton X-114 wash. Preparations were checked for the presence of capsids via negative stain EM, prior to injection.

Xu J., Erlendsson S., Singh M., Regier M., Ibiricu I., Day G.S., Piquet A.L., Clardy S.L., Feschotte C., Briggs J.A, & Shepherd J.D. (2023). PNMA2 forms non-enveloped virus-like capsids that trigger paraneoplastic neurological syndrome. bioRxiv.

Publication Preprint 2023

BLOOD Buffers Capsid Capsid Proteins Endotoxins Mus Pharmaceutical Adjuvants Proteins Serum Stains Tail Triton X-114 Vaccination Veins

Purification and Assembly of PNMA2 Protein Capsids

Bacterial protein expression plasmids were transformed into E. coli Rosetta2 strain (Novagen, Gibbstown, NJ) and the protein was expressed in ZY autoinduction media. E. coli were grown to 0.6–0.8 of OD600 at 37°C 150rpm, then switched to 19°C for 16–20h shaking. Afterwards, bacteria were pelleted down at 5000g for 15min at 4°C, resuspended in lysis buffer (500mM NaCl, 50mM Tris, 5% glycerol, 1mM DTT, complete Protease Inhibitor Cocktail, pH 8.0). The resuspended bacteria were frozen by liquid nitrogen and then thawed. The thawed lysates were sonicated and centrifuged at 21,000g for 45mins at 4°C. The supernatant was filtered through 0.45μm filters and incubated with Sepharose 4B beads (Cytiva, Marlborough, MA) overnight at 4°C. GST-tagged proteins were eluted from Sepharose beads by incubating with L-reduced glutathione (20mM, pH 8.0) and exchanged to cleavage buffer (50mM Tris, 150mM NaCl, 1mM DTT, 1mM EDTA, pH 7.2) using a Vivaspin column (Cytiva, Marlborough, MA). The cleavage of GST was performed by PreScission Protease (Cytiva, Marlborough, MA) overnight at 4°C. The cleaved PNMA2 protein was run through a HiLoad 16/600 Superdex 200 pg (Cytiva, Marlborough, MA) size-exclusion column in the capsid assembly buffer (500mM phosphate, 50mM Tris, 0.5mM EDTA, pH 7.5) to further purify PNMA2 and facilitate capsid formation. For protein purified for mice immunization, Triton X-114 was used to wash GST-tagged protein bound to Sepharose beads to remove endotoxin.

Publication Preprint 2023

Bacteria Bacterial Proteins Buffers Capsid Proteins Cytokinesis Edetic Acid Endotoxins Escherichia coli Freezing Glutathione Glycerin Mus Nitrogen Peptide Hydrolases PG 600 Phosphates Plasmids Protease Inhibitors Proteins Sepharose Sepharose 4B Sodium Chloride Triton X-114 Tromethamine Vaccination

Top products related to «Triton X-114»

Triton x 114 by Merck Group

Sourced in United States, Germany, Italy

Triton X-114 is a non-ionic detergent used in biochemical applications. It is a polyethylene glycol tert-octylphenyl ether that exhibits temperature-dependent phase separation, allowing for the separation and purification of proteins and other biomolecules.

Protease inhibitor cocktail by Merck Group

Sourced in United States, Germany, China, United Kingdom, Italy, Japan, Sao Tome and Principe, France, Canada, Macao, Switzerland, Spain, Australia, Israel, Hungary, Ireland, Denmark, Brazil, Poland, India, Mexico, Senegal, Netherlands, Singapore

The Protease Inhibitor Cocktail is a laboratory product designed to inhibit the activity of proteases, which are enzymes that can degrade proteins. It is a combination of various chemical compounds that work to prevent the breakdown of proteins in biological samples, allowing for more accurate analysis and preservation of protein integrity.

Toxinsensor chromogenic lal endotoxin assay kit by GenScript

Sourced in United States, China

The ToxinSensor™ Chromogenic LAL Endotoxin Assay Kit is a laboratory assay designed to detect and quantify endotoxin levels. It utilizes a Limulus Amebocyte Lysate (LAL) reaction to produce a chromogenic signal in the presence of endotoxin.

Protease inhibitor cocktail by Roche

Sourced in United States, Switzerland, Germany, China, United Kingdom, France, Canada, Japan, Italy, Australia, Austria, Sweden, Spain, Cameroon, India, Macao, Belgium, Israel

Protease inhibitor cocktail is a laboratory reagent used to inhibit the activity of proteases, which are enzymes that break down proteins. It is commonly used in protein extraction and purification procedures to prevent protein degradation.

Bovine serum albumin (bsa) by Merck Group

Sourced in United States, Germany, United Kingdom, China, Italy, Japan, France, Sao Tome and Principe, Canada, Macao, Spain, Switzerland, Australia, India, Israel, Belgium, Poland, Sweden, Denmark, Ireland, Hungary, Netherlands, Czechia, Brazil, Austria, Singapore, Portugal, Panama, Chile, Senegal, Morocco, Slovenia, New Zealand, Finland, Thailand, Uruguay, Argentina, Saudi Arabia, Romania, Greece, Mexico

Bovine serum albumin (BSA) is a common laboratory reagent derived from bovine blood plasma. It is a protein that serves as a stabilizer and blocking agent in various biochemical and immunological applications. BSA is widely used to maintain the activity and solubility of enzymes, proteins, and other biomolecules in experimental settings.

Fetal bovine serum (fbs) by Thermo Fisher Scientific

Sourced in United States, China, United Kingdom, Germany, Australia, Japan, Canada, Italy, France, Switzerland, New Zealand, Brazil, Belgium, India, Spain, Israel, Austria, Poland, Ireland, Sweden, Macao, Netherlands, Denmark, Cameroon, Singapore, Portugal, Argentina, Holy See (Vatican City State), Morocco, Uruguay, Mexico, Thailand, Sao Tome and Principe, Hungary, Panama, Hong Kong, Norway, United Arab Emirates, Czechia, Russian Federation, Chile, Moldova, Republic of, Gabon, Palestine, State of, Saudi Arabia, Senegal

Fetal Bovine Serum (FBS) is a cell culture supplement derived from the blood of bovine fetuses. FBS provides a source of proteins, growth factors, and other components that support the growth and maintenance of various cell types in in vitro cell culture applications.

Methanol by Merck Group

Sourced in Germany, United States, Italy, India, United Kingdom, China, France, Poland, Spain, Switzerland, Australia, Canada, Sao Tome and Principe, Brazil, Ireland, Japan, Belgium, Portugal, Singapore, Macao, Malaysia, Czechia, Mexico, Indonesia, Chile, Denmark, Sweden, Bulgaria, Netherlands, Finland, Hungary, Austria, Israel, Norway, Egypt, Argentina, Greece, Kenya, Thailand, Pakistan

Methanol is a clear, colorless, and flammable liquid that is widely used in various industrial and laboratory applications. It serves as a solvent, fuel, and chemical intermediate. Methanol has a simple chemical formula of CH3OH and a boiling point of 64.7°C. It is a versatile compound that is widely used in the production of other chemicals, as well as in the fuel industry.

Acetonitrile by Merck Group

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Acetonitrile is a colorless, volatile, flammable liquid. It is a commonly used solvent in various analytical and chemical applications, including liquid chromatography, gas chromatography, and other laboratory procedures. Acetonitrile is known for its high polarity and ability to dissolve a wide range of organic compounds.

Ni nta agarose by Qiagen

Sourced in Germany, United States, United Kingdom, Netherlands, China, Switzerland, Italy, Canada, Spain, India

Ni-NTA agarose is a solid-phase affinity chromatography resin designed for the purification of recombinant proteins containing a histidine-tag. It consists of nickel-nitrilotriacetic acid (Ni-NTA) coupled to agarose beads, which selectively bind to the histidine-tagged proteins.

Sodium dodecyl sulfate (sds) by Merck Group

Sourced in United States, Germany, United Kingdom, France, Italy, India, Canada, China, Poland, Sao Tome and Principe, Spain, Switzerland, Japan, Macao, Malaysia, Brazil, Belgium, Finland, Ireland, Netherlands, Singapore, Austria, Australia, Sweden, Denmark, Romania, Portugal, Czechia, Argentina

Sodium dodecyl sulfate (SDS) is a commonly used anionic detergent for various laboratory applications. It is a white, crystalline powder that has the ability to denature proteins by disrupting non-covalent bonds. SDS is widely used in biochemical and molecular biology techniques, such as protein electrophoresis, Western blotting, and cell lysis.

More about "Triton X-114"

Triton X-114 is a non-ionic surfactant widely used in biochemical and cell biology research for its ability to solubilize membrane proteins.
This detergent has been extensively employed in various applications, including protein purification, phase separation, and other related techniques.
Researchers often utilize Triton X-114 in conjunction with other reagents and tools to enhance their experimental workflows.
Protease inhibitor cocktails, for instance, are commonly used alongside Triton X-114 to protect proteins from degradation during purification and analysis.
The ToxinSensor™ Chromogenic LAL Endotoxin Assay Kit can also be employed to assess the endotoxin levels in Triton X-114 solutions, ensuring the quality and reliability of the reagent.
Bovine serum albumin (BSA) and fetal bovine serum (FBS) are additional biomolecules that may be utilized in Triton X-114-based protocols, serving as blocking agents or stabilizers for sensitive proteins.
Organic solvents, such as methanol and acetonitrile, are sometimes employed in Triton X-114 extraction and purification procedures to facilitate phase separation and remove contaminants.
Furthermore, Ni-NTA agarose, a common affinity resin, can be utilized in conjunction with Triton X-114 to purify His-tagged recombinant proteins.
Sodium dodecyl sulfate (SDS) is another detergent that may be used in combination with or as an alternative to Triton X-114, depending on the specific requirements of the research.
The PubCompare.ai tool can be particularly useful for researchers working with Triton X-114, as it enables the identification of the most accurate and reproducible protocols from the scientific literature, preprints, and patents.
By leveraging AI-driven comparisons, researchers can optimize their Triton X-114 processes and enhance the quality and accuracy of their work.