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Brij 35

Brij 35 is a nonionic surfactant commonly used in biochemical and molecular biology applications.
It is a polyoxyethylene(23)lauryl ether with the chemical formula C12H25(OCH2CH2)23OH.
Brij 35 is known for its ability to solubilize and stabilize proteins, enzymes, and other biomolecules.
It is frequently employed in cell lysis buffers, immunoprecipiation assays, and chromatographic techniques to enhance analyte recovery and separation.
Researchers can leverage PubCompare.ai's AI-powered optimization to quickly identify the most reproducible and accurate protocols involving Brij 35, streamlining their experimental design and saving time.

Most cited protocols related to «Brij 35»

Yeast and HeLa Cell Lysis Protocols

Cited 10 times

Wild type yeast (Saccharomyces cerevisiae) strain SUB62 (MATa his3-Δ200 lys2–801 leu2–3, 112 trp1–1 ura3–52) was cultured in synthetic complete medium. At OD₆₀₀ 1, cells were harvested by addition of sodium azide to a final concentration of 10 mM, followed by centrifugation at 1,700 × g (Eppendorf), washed once with cold deionized water, pelleted and snap frozen at −80 °C. Pellets were thawed and resuspended in modified RIPA buffer containing 150 mM NaCl, 1% Nonidet P-40, 0.5% sodium deoxycholate, 0.1% SDS, 50 mM Tris-HCl pH 8.0, 5 mM DTT, and yeast specific protease inhibitor (Sigma-Aldrich). Cells were mechanically lysed using a minibead beater (BioSpec Products) as previously described,^{10 (link)} where cells were beaten with 1 mL of chilled zirconia beads (Biospec Products) in four 30 s cycles, with 30 s rest on ice between cycles.
HeLa cells were maintained in Dulbecco’s modified Eagle’s medium (Invitrogen) supplemented with 10% dialyzed fetal bovine serum (HyClone, Thermo Scientific). For cell lysis, the media was removed, the cells harvested by scraping, the cell pellet was washed with ice-cold PBS and then lysed with ice-cold lysis buffer composed of 10 mM K₂HPO₄ pH 7.5, 1 mM EDTA, 10 mM MgCl₂, 50 mM β-glycerophosphate, 5 mM EGTA, 0.5% Nonidet P-40, 0.1% Brij 35, 0.1% sodium deoxycholate, 1 mM sodium orthovanadate, 1 mM PMSF, 5 μg/ml leupeptin and 5 μg/ml pepstatin A. The lysate was centrifuged at 20,000 × g for 10 min to remove cell debris.

Ting L., Rad R., Gygi S.P, & Haas W. (2011). MS3 eliminates ratio distortion in isobaric labeling-based multiplexed quantitative proteomics. Nature methods, 8(11), 937-940.

Publication 2011

beta-glycerol phosphate Brij 35 Buffers Cell Cycle Cells Centrifugation Cold Temperature Deoxycholic Acid, Monosodium Salt Eagle Edetic Acid Egtazic Acid Fetal Bovine Serum Freezing HeLa Cells leupeptin Magnesium Chloride Nonidet P-40 Orthovanadate Pellets, Drug pepstatin potassium phosphate, dibasic Protease Inhibitors Radioimmunoprecipitation Assay Saccharomyces cerevisiae Sodium Sodium Azide Sodium Chloride Strains Tromethamine tyrosinase-related protein-1 Yeast, Dried zirconium oxide

Characterization of Radiolabeled Nanobodies

Cited 8 times

Protocol full text hidden due to copyright restrictions

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Publication 2012

Biotin Brij 35 Buffers Chimera Cyclonic Storms Electrophoresis erbb2 Gene Forests Gels herstatin protein, human Homo sapiens Laemmli buffer link protein Phosphorus Proteins Radioactivity SDS-PAGE Silicon Dioxide Sodium Azide Streptavidin Thin Layer Chromatography Trichloroacetic Acid

Fluorescence-based Histone H3/H4-Asf1 Interaction Assay

Cited 8 times

The X. laevis H3^C110A mutant (xH3^C110A) was used to mimic the yeast histone dimerization surface and to avoid any unwanted cysteine / dye reaction (46 (link)). X. laevis histone H4^T71C mutant (xH4^T71C) was fluorescently labeled (26 (link),46 (link)) (Supplementary Figure S1) with the Qsy9 fluorescence quencher or fluorescein (FM) (Invitrogen) as previously described (46 (link)). The xH3^C110A and Qsy9 or FM labeled xH4^T71C were then prepared as tetramers yielding either H3/H4*^Q or H3/H4*^FM. yAsf1 was labeled with Alexa Fluor 532 (Invitrogen) yielding yAsf1*. The position of the labeled cysteine is shown in Supplementary Figure S1, while the other two cysteines in yAsf1 (Cys³⁰ and Cys⁹⁹) are not near the histone-binding interface and are not labeled efficiently in this procedure (as verified by mass spectrometry, data not shown). Measurements were performed at a yAsf1 concentration of 1 nM in buffer [10 mM Tris-HCl (pH 7.5), 150 mM KCl, 2 mM MgCl₂, 1% glycerol and 0.05% Brij-35]. Double measurements were made with an integration time of 0.5 s on a Horiba Fluorolog-3 spectrometer at 20°C, using a 0.5 cm path-length cuvette. The excitation wavelength was 528 nm, with a slit width of 7 mm; emission was recorded at 547 nm with a slit width of 7 mm. H3/H4 labeled with Qsy9 was titrated to the cuvette containing yAsf1* and the decrease of yAsf1* fluorescence was monitored. Control samples with buffer or unlabeled histones were analyzed likewise to discount buffer effects on fluorescence. The buffer was scanned in the same range used in all experiments for background contributions to the readings and was corrected for in each spectrum. Varying incubation times (0–30 min) confirmed that the fluorescence signal had reached equilibrium by 5 min. The reactions were allowed to equilibrate at 20°C for at least 5 min prior to measurement, and at least three independent experiments were performed for each sample. Data were fitted with the ligand-depleted binding model [Equation (1 (link))] in cases where the concentration of yAsf1* was within 10-fold of the K_d value.

with the variable i indicating the varying concentrations of H3/H4 that were titrated into the yAsf1*.

Donham DC I.I., Scorgie J.K, & Churchill M.E. (2011). The activity of the histone chaperone yeast Asf1 in the assembly and disassembly of histone H3/H4–DNA complexes. Nucleic Acids Research, 39(13), 5449-5458.

Publication 2011

Brij 35 Buffers Cysteine Dimerization Fluorescein Fluorescence Glycerin Histones Ligands Magnesium Chloride Mass Spectrometry QSY-9 Saccharomyces cerevisiae Tetrameres Tromethamine Xenopus laevis

Urea Assay with Modified Reagent

Cited 8 times

Urea reagents were prepared as described in Jung et al. (1975) (link). The final Jung working reagent consisted of 100 mg/L o-phthalaldehyde, 215 mg/L N-(1-naphthyl)ethylenediamine, 2.5 mol/L sulfuric acid, 2.5 g/L boric acid, and 0.03% Brij-35. The modified reagent used 513 mg/L primaquine bisphosphate in place of the 215 mg/L N-(1-naphthyl)ethylenediamine reagent. The urea standard was prepared in double-distilled water and contained 5.00 mg/dL urea. To perform the assay, 50 μL of water, 50 μL of the 5.00 mg/dL standard, and 50 μL samples were transferred into separate wells of a clear flat-bottom 96-well plate. Then to each well, 200 μL of freshly prepared working reagent was added and mixed quickly by gently rocking the plate. The reaction was incubated for 1 h at room temperature. Optical densities (OD) at 430 and 505 nm were measured on the plate reader for assays using the modified reagent and the original Jung reagent, respectively.
The calibration curve (Fig. 1A) shows that the assay is linear between 0.00 and 5.00 mg/dL urea. For calculation of the sample urea concentration, the experimenter can choose either to use the slope of the standard curve or to use a single urea concentration (see below). We found that it is sufficient to use one blank (water) and one single urea concentration (5.00 mg/dL) to calculate the sample urea concentrations. In this work, urea concentration in the sample was calculated from the OD values:

\begin{array}{l} [Urea] = \frac{{OD}_{SAMPLE} - {OD}_{BLANK}}{{OD}_{STANDARD} - {OD}_{BLANK}} \times n \\ \times [Standard] (mg / dL) \end{array}

where OD_SAMPLE, OD_STANDARD, and OD_BLANK are OD_{430 nm} values of the sample, standard, and water blank, respectively. [Standard] is the concentration of the urea standard (5.00 mg/dL or 0.83 mmol/L) and n is the dilution factor. Dilution of samples in distilled water is necessary when sample OD_{430 nm} values are higher than the OD_{430 nm} value for the 5.00 mg/dL urea standard.

Zawada R.J., Kwan P., Olszewski K.L., Llinas M, & Huang S.G. (2009). Quantitative determination of urea concentrations in cell culture medium. Biochemistry and cell biology = Biochimie et biologie cellulaire, 87(3), 541-544.

Publication 2009

Biological Assay boric acid Brij 35 Ethylenediamines o-Phthalaldehyde Primaquine Sulfuric Acids Technique, Dilution Urea Vision

Immunohistochemical Detection of Histone Modifications

Cited 7 times

Immunohistochemistry was performed with the indirect enzyme-labelled antibody method, as described previously [1 (link), 17 (link), 27 (link)]. For the detection of histone H3, H3K4me3, H3K9ac, H3K18, H3K23ac, H3K27me3, and H3S10phos, paraffin sections of mouse testis were deparaffinized with toluene and dehydrated in serially graded ethanol solutions. The sections were autoclaved in a 10 mM citrate buffer (pH 6.0) for 15 min at 120°C. Then, the sections were preincubated with 500 µg/ml normal goat IgG dissolved in 1% BSA in PBS, pH 7.4, for 1 hr. Unless otherwise specified, all reactions were conducted at room temperature. Then the sections were reacted 16 hr with first antibodies in 1% BSA in PBS. After incubation, the sections were washed with 0.075% Brij 35 in PBS three times for 15 min each. The sections were then incubated with HRP-conjugated goat anti-rabbit IgG in 1% BSA in PBS for 1 hr. After washing with 0.075% Brij 35 in PBS three times for 15 min each, the sites of HRP were visualized with DAB and H₂O₂ in the presence of nickel and cobalt ions [4 ]. As a negative control, some sections were reacted with normal rabbit IgG instead of the specific antibodies.

Song N., Liu J., An S., Nishino T., Hishikawa Y, & Koji T. (2011). Immunohistochemical Analysis of Histone H3 Modifications in Germ Cells during Mouse Spermatogenesis. Acta Histochemica et Cytochemica, 44(4), 183-190.

Publication 2011

anti-IgG Antibodies Brij 35 Buffers Citrates Cobalt Enzymes Ethanol Goat Histone H3 histone H3 trimethyl Lys4 Immunoglobulins Immunohistochemistry Ions Mice, House Nickel Paraffin Peroxide, Hydrogen Rabbits Testis Toluene

Most recents protocols related to «Brij 35»

Matrix Metalloproteinase Inhibition Assay

Not available on PMC !

Example 6

Individual inhibitors were dissolved in TCN buffer (50 mM Tris-HCl, 10 mM CaCl₂, 150 mM NaCl₂, 0.05% Brij 35 at pH 7.5) at appropriate dilutions then added to the wells of a microtiter plate (10 μL/well) in triplicate. Each well of test agent (and appropriate control wells) was then treated with activated MMP-2 or 9 (10 μL of a 40 nM solution in 50 mM Hepes, 10 mM CaCl₂), 1% Brij 35 at pH 7.5; R&D Systems) followed by 30 μL TCN buffer and 150 μL the fluorogenic peptide substrate (Mca-PLGL-Dpa-AR-NH₂; R&D Systems). The resulting mixtures were incubated 1 h at 27° C. then analyzed using a FL600 fluorescent plate reader (excitation=310/20; emission=420/50; optics=bottom; sensitivity=225) and KC4 Software.

TABLE 2

MMP inhibition data

Imaging

AgentMMP-2MMP-9

15.193.54

231.620.2

34.612.59

415.415.3

50.580.74

62.742.98

RP8056.507.40

US11865195B2. Evaluation of presence of and vulnerability to atrial fibrillation and other indications using matrix metalloproteinase-based imaging (2024-01-09). Lantheus Medical Imaging, Inc. [US], Yale University [US]. Inventors: Albert J. Sinusas [US], Joseph G. Akar [US], Richard R. Cesati [US], Heike S. Radeke [US], Stephen B. Haber [US].

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Patent 2024

Biological Assay Brij 35 Buffers Eye Fluorogenic Substrate HEPES Hypersensitivity Matrix Metalloproteinase 9 Matrix Metalloproteinase Inhibitors MMP2 protein, human Peptides Psychological Inhibition Technique, Dilution Tromethamine

Gelatin Zymography Assay for MMP-9 and MMP-2 Inhibition

Gelatin zymography was performed to assess MMP-9 and -2 activity following treatment of THP-1 cells with DTG, CAB, BIC, or DOX. This assay was used as preliminary confirmation of the inhibition of MMPs by individual INSTIs. Due to the nature of this assay, only the gelatinases, MMP-2 and -9, could be assessed. Cells were plated at a density of 1 × 10⁶ in 12 well plates and treated with phorbol-12-myristate-13-acetate (PMA) for 24 h. This was done to promote cell differentiation to stimulate MMP secretion. Following PMA treatment, cells were treated with DTG, CAB, BIC, or DOX at concentrations of 25, 50, 75, or 100 µM or control vehicle for 24 h. In our previous study, no DTG-induced cytotoxicity was recorded in PMA-stimulated THP-1 cells up to 100 µM (Bade et al., 2021 (link)). Thus, for comparative assessments among different INSTIs (DTG, BIC, and CAB) and DOX (positive control) drug concentrations of up to 100 µM were utilized. Each of the experimental tests were performed in triplicate. Following treatment, media was collected and centrifuged at 15,000 x g for 10 min at 4°C. Supernatant was collected and stored at −80°C for further analysis. For gelatin zymography, 3 µg of protein from cell medium was loaded in a 10% SDS-polyacrylamide gel containing 0.1% gelatin. Gels were ran at 55 V until the loading dye passed through its bottom. The gel was then removed and washed with water for 15 min, then incubated with renaturation buffer [2.5% (v/v) Triton X-100 in Milli-Q water] for 90 min at room temperature. The used renaturation buffer was replaced with fresh buffer every 30 min. Renaturation buffer was then replaced with developing buffer (50 mM Tris–HCl, pH 7.5, 5 mM CaCl2, 0.2 M NaCl, and 0.02% Brij-35) and the gel was incubated at 37°C in a shaker (Innova 42, New Brunswick Scientifc, Edison, NJ) for 48 h. After 48 h, the gel was washed with water for 15 min and then stained using 0.2% Coomassie Brilliant Blue R-250 (BIO-RAD, Hercules, CA) for 1 h. After staining, the gel was washed with water for 15 min before washing with destaining solution (30% methanol, 10% acetic acid, 60% water) for 45 min. The gel was then washed with water for 20 min to remove any destaining solution. Finally, the stained gel was imaged using the iBright 750 Imaging System (Invitrogen, Carlsbad, CA). ImageJ software was used to quantitate band density recorded as a measure of relative MMP activity.

Foster E.G., Palermo N.Y., Liu Y., Edagwa B., Gendelman H.E, & Bade A.N. (2023). Inhibition of matrix metalloproteinases by HIV-1 integrase strand transfer inhibitors. Frontiers in Toxicology, 5, 1113032.

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Publication 2023

Acetic Acid BID protein, human Biological Assay Brij 35 Buffers Cells Coomassie brilliant blue R Cytotoxin Differentiations, Cell Gelatinases Gelatins Methanol MMP2 protein, human MMP9 protein, human Pharmaceutical Preparations polyacrylamide gels Proteins Psychological Inhibition secretion Sodium Chloride THP-1 Cells Triton X-100 Tromethamine

Measuring β-1,3-Glucan Synthase Activity

β-1,3-glucan synthase activity was measured referring to the method of Belewa et al. (2017) (link). Microsomal proteins were obtained by crushing mycelia and pulverizing by ultracentrifugation. The microsomal proteins were resuspended in 500 μl buffer (1 mmol/l EDTA; 1 mmol/l DTT; 33% (v/v) glycerol; 50 mmol/l Tris–HCl, pH 7.5) and stored at −80°C until use. A 50 μl reaction system was established consisting of 50 mmol/l Tris–HCl (pH 7.5), 20 μmol/l GTP, 4 mmol/l EDTA, 0.5% Brij-35, 6.6% glycerol, 2 mmol/l UDP-Glc, and 100 μg microsomal protein. After incubation at 25°C for 30 min, the reaction was stopped by adding 10 μl of 6 mol/l NaOH. The dextran produced by the previous process was dissolved at 80°C for 30 min. The glucan content was measured by the aniline blue method. One unit of enzymatic activity (U/mg protein) is defined as 1 mg protein catalyzed to produce 1 μg of glucan.

Zhao L., Wang J., Zhang H., Wang P., Wang C., Zhou Y., Li H., Yu S, & Wu R. (2023). Inhibitory effect of carvacrol against Alternaria alternata causing goji fruit rot by disrupting the integrity and composition of cell wall. Frontiers in Microbiology, 14, 1139749.

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Publication 2023

aniline blue Brij 35 Buffers Dextran Edetic Acid enzyme activity Glucans glucan synthase Glycerin Microsomes Mycelium Proteins Tromethamine Ultracentrifugation

Enzymatic Assay for PDK1-4 Inhibition

Protocol full text hidden due to copyright restrictions

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Publication 2023

Amino Acids Biological Assay Brij 35 Buffers Egtazic Acid Enzyme Assays Enzymes Fluorescence Glutathione S-Transferase Glycerin HEPES Kinetics Magnesium Chloride PDK1 protein, human PDK2 protein, human PDK3 protein, human PDK4 protein, human Phosphotransferases prisma Sulfoxide, Dimethyl Technique, Dilution

Gelatin Zymography for Protease Activity

Fresh brain tissues were immersed in RIPA lysis buffer (P0013K, Beyotime, China) at a ratio of 1:4 (w: v) and centrifuged at 4°C (12,000 rpm, 15 min) after homogenization. The protein concentration was determined by a BCA concentration determination kit (P0010, Beyotime, China). The supernatant and loading buffer (P0016N, Beyotime, China) were mixed at a ratio of 4:1. A total of 120 μg of total protein was loaded into an 8% SDS‒PAGE gel containing 10% gelatin. After electrophoresis at 80 V in ice water for 3 h, each gel was washed in 2.5% Triton X-100 for 30 min 3 times. Then, gels were treated with incubation buffer (50 mM Tris-HCL, 0.2 M NaCl, 5 mM CaCl2, 1 µM ZnCl2, 0.02% Brij-35, pH 7.5) for 48 h at 37°C on a shaking table. Gels were stained with 0.5% Coomassie brilliant blue R250 (ST1123, Beyotime, China) for 3 h and then dyed with 30% methanol containing 10% acetic acid until the emergence of an appropriate color discrepancy. The clear bands on the zymogram represented gelatinase activity.

Ma P., Huang N., Tang J., Zhou Z., Xu J., Chen Y., Zhang M., Huang Q, & Cheng Y. (2023). The TRPM4 channel inhibitor 9-phenanthrol alleviates cerebral edema after traumatic brain injury in rats. Frontiers in Pharmacology, 14, 1098228.

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Publication 2023

Acetic Acid Brain Brij 35 brilliant blue G Buffers Electrophoresis Gelatinases Gelatins Gels Ice Methanol Proteins Radioimmunoprecipitation Assay SDS-PAGE Sodium Chloride Staphylococcal Protein A Tissues Triton X-100 Tromethamine

Top products related to «Brij 35»

Brij 35 by Merck Group

Sourced in United States, Germany

Brij 35 is a non-ionic surfactant used in various laboratory applications. It functions as a solubilizing agent, emulsifier, and detergent. Brij 35 can be utilized in a range of scientific experiments and procedures that require the properties of a non-ionic surfactant.

Brij 35 by Thermo Fisher Scientific

Sourced in United States, Germany

Brij-35 is a non-ionic surfactant commonly used in various laboratory applications. It functions as a detergent to solubilize and disperse biological and chemical samples.

Gelatin by Merck Group

Sourced in United States, Germany, China, Italy, United Kingdom, France, Canada, Switzerland, Sao Tome and Principe, Australia, Spain, Macao, Japan, Poland, India, Belgium, Sweden, Czechia, Denmark

Gelatin is a natural, water-soluble protein derived from the partial hydrolysis of collagen. It is commonly used as a gelling agent, thickener, and stabilizer in various food and pharmaceutical applications.

Triton x 100 by Merck Group

Sourced in United States, Germany, United Kingdom, Italy, China, Japan, Canada, France, Sao Tome and Principe, Switzerland, Macao, Poland, Spain, Australia, India, Belgium, Israel, Sweden, Ireland, Denmark, Brazil, Portugal, Panama, Netherlands, Hungary, Czechia, Austria, Norway, Slovakia, Singapore, Argentina, Mexico, Senegal

Triton X-100 is a non-ionic surfactant commonly used in various laboratory applications. It functions as a detergent and solubilizing agent, facilitating the solubilization and extraction of proteins and other biomolecules from biological samples.

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.

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.

Synergy h4 by Agilent Technologies

Sourced in United States, United Kingdom, Germany

The Synergy H4 is a multi-mode microplate reader designed for high-performance detection of various assays. It features advanced optics and filters for absorbance, fluorescence, and luminescence measurements.

Tween 80 by Merck Group

Sourced in United States, Germany, United Kingdom, India, Italy, France, Sao Tome and Principe, Spain, Poland, China, Belgium, Brazil, Switzerland, Canada, Australia, Macao, Ireland, Chile, Pakistan, Japan, Denmark, Malaysia, Indonesia, Israel, Saudi Arabia, Thailand, Bangladesh, Croatia, Mexico, Portugal, Austria, Puerto Rico, Czechia

Tween 80 is a non-ionic surfactant and emulsifier. It is a viscous, yellow liquid that is commonly used in laboratory settings to solubilize and stabilize various compounds and formulations.

γ 32p atp by PerkinElmer

Sourced in United States, United Kingdom, Japan, China, France, Australia, Germany, Italy, Sweden, Canada

[γ-32P]ATP is a radiolabeled compound containing the radioactive isotope phosphorus-32 (32P) attached to the gamma phosphate group of adenosine triphosphate (ATP). This product is commonly used as a tracer in various biochemical and molecular biology applications, such as nucleic acid labeling and analysis.

Tween 20 by Merck Group

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

Tween 20 is a non-ionic detergent commonly used in biochemical applications. It is a polyoxyethylene sorbitan monolaurate, a surfactant that can be used to solubilize and stabilize proteins and other biomolecules. Tween 20 is widely used in various laboratory techniques, such as Western blotting, ELISA, and immunoprecipitation, to prevent non-specific binding and improve the efficiency of these assays.

What is Brij 35 and how is it commonly used in biochemistry and molecular biology?

Brij 35 is a nonionic surfactant that is widely used in biochemical and molecular biology applications. It is a polyoxyethylene(23)lauryl ether with the chemical formula C12H25(OCH2CH2)23OH. Brij 35 is known for its ability to solubilize and stabilize proteins, enzymes, and other biomolecules. It is frequently employed in cell lysis buffers, immunoprecipitation assays, and chromatographic techniques to enhance analyte recovery and separation.

What are some common challenges researchers face when working with Brij 35?

One of the main challenges with Brij 35 is ensuring optimal usage for specific applications. Different concentrations, incubation times, and buffer conditions can significantly impact the solubilization and stabilization of target biomolecules. Researchers may also encounter issues with interference or unwanted interactions when using Brij 35 in combination with other reagents or experimental setups.

Are there different types or variations of Brij 35 that researchers should be aware of?

Yes, there are several variations of Brij 35 that have slightly different properties. For example, Brij 35P is a purer form of Brij 35 that may be preferred for more sensitive applications. Additionally, there are Brij surfactants with different polyoxyethylene chain lengths, such as Brij 30 (4 ethylene oxide units) or Brij 58 (20 ethylene oxide units), which can be used depending on the specific needs of the experiment.

What are some common applications of Brij 35 in biochemistry and molecular biology?

Brij 35 is widely used in a variety of biochemical and molecular biology applications. Some of the most common uses include: 1. Cell lysis and protein extraction: Brij 35 is often included in cell lysis buffers to help solubilize and extract proteins and other biomolecules from cells. 2. Immunoprecipitation assays: Brij 35 can be used to help stabilize and solubilize the target proteins or complexes during the immunoprecipitation process. 3. Chromatographic techniques: Brij 35 is frequently employed in column chromatography, such as size-exclusion or affinity chromatography, to enhance the recovery and separation of analytes. 4. Enzyme assays: The detergent properties of Brij 35 can help solubilize and stabilize enzymes, making it useful for enzyme activity assays and kinetic studies.

How can PubCompare.ai's AI-powered optimization help researchers working with Brij 35?

PubCompare.ai's AI-powered optimization can be a valuable tool for researchers working with Brij 35. The platform allows you to: 1. Screen protocol literature more efficiently: PubCompare.ai's AI-driven analysis can quickly identify the most relevant and reproducible protocols involving Brij 35 from the literature, pre-prints, and patents. 2. Leverage AI to pinpiont critical insights: The platform's AI-powered comparison can highlight key differences in protocol effectiveness, such as optimal Brij 35 concentrations, incubation times, and buffer conditions, enabling you to choose the best option for your specific research goals. By streamlining the identification and comparison of Brij 35 protocols, PubCompare.ai can save researchers time and help them make more informed decisions, leading to more accurate and reproducible results.

More about "Brij 35"

Brij 35 is a non-ionic surfactant commonly used in biochemical and molecular biology applications.
It is a polyoxyethylene(23)lauryl ether, also known as polyoxyethylene(23)dodecyl ether, with the chemical formula C12H25(OCH2CH2)23OH.
This versatile compound is prized for its ability to solubilize and stabilize proteins, enzymes, and other biomolecules.
Researchers frequently employ Brij 35 in cell lysis buffers, immunoprecipitation assays, and chromatographic techniques to enhance analyte recovery and separation.
It is often used in conjunction with other reagents like gelatin, Triton X-100, bovine serum albumin, protease inhibitor cocktails, and Tween 80 to optimize experimental conditions.
PubCompare.ai's AI-powered optimization can help researchers quickly identify the most reproducible and accurate protocols involving Brij 35, streamlining their experimental design and saving valuable time.
The platform allows users to easily locate protocols from literature, pre-prints, and patents, and compare them using advanced analytics to pinpoint the most effective options.
Whether you're working with Synergy H4 instruments, labeling proteins with [γ-32P]ATP, or using Tween 20 for Western blotting, PubCompare.ai can provide insights to enhance your Brij 35-based experiments and drive your research forward more efficiently.