Triton x 100

Manufactured by Boston BioProducts

Sourced in United States

Triton X-100 is a non-ionic detergent commonly used in biochemical applications. It is a clear, viscous liquid that can be used to solubilize and extract proteins from biological samples. Triton X-100 disrupts lipid-lipid and lipid-protein interactions, making it useful for cell lysis and protein purification procedures.

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Lab products found in correlation

Cocktail of protease inhibitor, by Merck Group (2 mentions) Quantichrom calcium assay kit, by BioAssay Systems (1 mentions) Paraformaldehyde (pfa), by Thermo Fisher Scientific (1 mentions) Nbp1 32440, by Novus Biologicals (1 mentions) Eclipse ti inverted microscope, by Nikon (1 mentions) Glycine, by Merck Group (1 mentions) Poly d lysine coated 6 well plates, by Corning (1 mentions) Ab6721, by Abcam (1 mentions) A3854, by Merck Group (1 mentions) Clear blue x ray film, by Thermo Fisher Scientific (1 mentions) Complete mini protease inhibitor cocktail tablet, by Roche (1 mentions) Milli q, by Merck Group (1 mentions) Lyophilizer, by Labconco (1 mentions) Anti tubulin antibody, by Merck Group (1 mentions) Phospho rb, by Cell Signaling Technology (1 mentions) Anti nras antibody, by Abcam (1 mentions) Anti ascl1 antibody, by BD (1 mentions) Phospho akt, by Cell Signaling Technology (1 mentions) Vimentin, by Cell Signaling Technology (1 mentions) Alexa fluor dye, by Thermo Fisher Scientific (1 mentions)

9 protocols using triton x 100

Quantification of Cellular Calcium Content

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To measure calcium content, cells were harvested by centrifugation at 13,500 rpm for 1 minutes, resuspended in lysis buffer (0.1% Triton X-100, Boston BioProducts, Inc.) and sonicated on ice for 1 minute to destroy the cell membranes. The resulting supernatant was used for calcium measurements made with a QuantiChrom™ Calcium Assay Kit (DICA-500, BioAssay Systems, Hayward, CA, USA). Calcium content was estimated by measuring absorbance at 612 nm in a microplate reader.

Kim E.C., Park J., Kwon I.K., Lee S.W., Park S.J, & Ahn S.J. (2017). Static magnetic fields promote osteoblastic/cementoblastic differentiation in osteoblasts, cementoblasts, and periodontal ligament cells. Journal of Periodontal & Implant Science, 47(5), 273-291.

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Quantitative Immunofluorescence Characterization of FTSEC and HGSOC Cells

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10⁴ cells from each FTSEC and HGSOC line were seeded onto imaging plates (Eppendorf: 0030741030) and allowed to grow for 24 hours. Cells were washed twice in PBS, and fixation was performed for 15 min with paraformaldehyde 4% (Thermo-Fisher: AAJ19943K2) at room temperature. Cells were then washed twice in PBS and permeabilized with Triton X-100 0.25% (Boston BioProducts: P-924) for 15 min. Aldehyde residues were quenched with glycine 100 mM (Sigma-Aldrich: 50046-50G) for 15 min. The unspecific sites were blocked with a solution of 1% bovine serum albumin, and 0.1% Tween 20 in PBS for 30 min. Samples were incubated for 16 hours at 4 °C with a dilution of 1:500 of antibody to PAX8 (Novus: NBP1-32440) or SOX17 (Novus: NBP1-47996). Cells were then washed three times for 5 min each in a solution of 1% bovine serum albumin and 0.1% Tween 20 in PBS followed by incubation for one hour with AlexaFluor488-conjugated anti-mouse IgG antibody or AlexaFluor594-conjugated anti-rabbit IgG antibody. Cells were washed three times in PBS, mounted in Fluoromount-G with DAPI, and images were acquired at 60X magnification with a Nikon Eclipse Ti inverted microscope.

Chaves-Moreira D., Mitchell M.A., Arruza C., Rawat P., Sidoli S., Nameki R., Reddy J., Corona R.I., Afeyan L.K., Klein I.A., Ma S., Winterhoff B., Konecny G.E., Garcia B.A., Brady D.C., Lawrenson K., Morin P.J, & Drapkin R. (2022). The transcription factor PAX8 promotes angiogenesis in ovarian cancer through interaction with SOX17. Science signaling, 15(728), eabm2496.

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Efficient Gene Delivery in Primary Neurons

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PNGCs were plated into poly-D-lysine coated 6-well plates (Corning Life Sciences) in 2 mL of media per well. Cells were maintained in the Neurobasal-A growth media mentioned above without fetal bovine serum (FBS) at 37 °C in a humidified 5% CO2 chamber. Unpurified media containing rAAV or lysate purified rAAV was applied directly into the culture medium on the fourth day of culture (4 DIV) at 1.0 × 10¹⁰ vector genomes per mL of culture media (final concentration of 2.0 × 10¹⁰ total vector genomes per well). PNGCs were maintained with half media changes every 3 days until 10DIV, at which point they were harvested for western blot analysis. Each well was treated as an n = 1 and individually re-suspended in ice-cold PBS. PNGCs were then centrifuged at 500 x g for 3 minutes and PBS was removed from the cell pellet. Cell pellets were lysed in radio immunoprecipitation assay buffer containing 1% triton X-100 (Boston Bioproducts) and a cocktail of protease inhibitors (Sigma-Aldrich). Lysates were centrifuged at 1000 x g and soluble supernatants were subjected to western blot analysis.

Goodwin M.S., Croft C.L., Futch H.S., Ryu D., Ceballos-Diaz C., Liu X., Paterno G., Mejia C., Deng D., Menezes K., Londono L., Arjona K., Parianos M., Truong V., Rostonics E., Hernandez A., Boye S.L., Boye S.E., Levites Y., Cruz P.E, & Golde T.E. (2020). Utilizing minimally purified secreted rAAV for rapid and cost-effective manipulation of gene expression in the CNS. Molecular Neurodegeneration, 15, 15.

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PARP1 Expression Analysis by Western Blot

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Cell pellets obtained from 80% confluent flasks were washed twice with PBS and lysed with 200 μL ice cold RIPA buffer with Triton X100 (Boston BioProducts) and one Mini Complete Protease Inhibitor Cocktail tablet (Roche, Indianapolis, IN) The samples were spun at 4 °C at 12,000 rpm for 10 minutes and the supernatant was collected. Protein quantification was performed using bicinchoninic acid (BCA) protein assay (Pierce, Rockford, IL). For PARP expression, 20 μg of protein was loaded on the gel. Proteins were separated with SDS/PAGE gel electrophoresis and transferred to a Nitrocellulose membrane. Proteins were detected using antibodies specific for PARP1 (1:1,000, Invitrogen; PA5–16452) and ß-actin (1:40,000; Sigma; A-3854) with a corresponding horseradish peroxidase (HRP) conjugated secondary antibody (1:20,000, ab6721, Abcam, USA). Detection was performed using a chemiluminescent substrate (Thermo Scientific #34077, Super Signal West Pico, USA). The bands were visualized using an automated blot processing machine (Ewen-Parker X-Ray corporation, New York, USA) with a light sensitive clear blue x-ray film (Thermo Scientific, 24x30 cm, SB2324231, Belgium) with 1 min exposure time.

Wilson T.C., Jannetti S.A., Guru N., Pillarsetty N., Reiner T, & Pirovano G. (2020). Improved radiosynthesis of 123I-MAPi, an Auger theranostic agent. International journal of radiation biology, 99(1), 70-76.

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Porcine Pancreatic Extracellular Matrix Decellularization

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The porcine pancreas was obtained from four six-month-old pigs (Midwest Research Swine LLC, Gibbon, MN, USA). The pancreas was first washed to remove the lipid layer and the blood and cut into small pieces. Then, the material was immersed in phosphate buffer saline (PBS) under rotation for 1 h. The tissue samples were decellularized in a solution of 1% (v/v) Triton-X-100 (Boston BioProducts, Ashland, MA, USA) at 4 °C under rotation for a total of 8 h until the tissues turned translucent. The solution was changed every 30 min for the first 2 h and every 2 h after until the process was completed. The resulting ECM was washed with a large volume of sterile MilliQ (Millipore Sigma, Burlington, MA, USA) water and placed in a tube with sterile PBS to be washed for a total of 2 days with the washing solution being changed frequently for complete removal of any detergent residues remaining. The decellularized ECM was then sterilized in 70% ethanol for 2 h followed by sterile PBS wash and freeze-dried using a lyophilizer (Labconco, Kansas City, MO, USA). The sterile lyophilized tissue was kept frozen until further use.

Hao L., Khajouei F., Rodriguez J., Kim S, & Lee E.J. (2024). Unlocking the Promise of Decellularized Pancreatic Tissue: A Novel Approach to Support Angiogenesis in Engineered Tissue. Bioengineering, 11(2), 183.

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Isolation and Analysis of Insoluble Tau

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Slice cultures for assessment of insoluble tau from three wells (nine slices in total) were harvested into ice-cold PBS and presented as n = 1. Slices were washed in PBS, pelleted, and sarkosyl extractions were performed as previously described [29 (link)]. Slice cultures for comparison of lysate purified and unpurified media preparations from three wells (nine slices in total) were harvested into ice-cold PBS and presented as n = 1. Slices were lysed in radio immunoprecipitation assay buffer containing 1% triton X-100 (Boston Bioproducts) and a cocktail of protease inhibitors (Sigma-Aldrich). Lysates were centrifuged at 1000 x g and soluble supernatants were subjected to western blot analysis.

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Immunoblotting Antibody Profiling Protocol

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Cells were grown and treated as described and lysed with RIPA buffer with Triton X‐100 (Boston BioProducts) supplemented with protease and phosphatase inhibitors. Immunoblotting was performed according to the antibody manufacturers’ recommendations. The following antibodies were obtained from Cell Signaling Technology (Danvers, MA, USA): Anti‐Synaptophysin (SYP), phospho‐ERK1/2 (Thr202/Tyr204), ERK1/2, phospho‐RSK (Thr359/Ser363), RSK, phospho‐S6 (Ser235/236), phospho‐S6 (Ser240/244), S6, phospho‐4EBP (Thr37/46), 4EBP, phospho‐Akt (Ser473), Akt, Hsp90, phospho‐RB (Ser780), phospho‐RB (Ser807/811), RB, Vimentin, ZEB1, Snail, and Lamin B1. Anti‐ASCL1 antibody was purchased from BD Biosciences. Anti‐tubulin antibody is purchased from Sigma‐Aldrich. Anti‐NRAS antibody is purchased from Abcam.

Ogino A., Choi J., Lin M., Wilkens M.K., Calles A., Xu M., Adeni A.E., Chambers E.S., Capelletti M., Butaney M., Gray N.S., Gokhale P.C., Palakurthi S., Kirschmeier P., Oxnard G.R., Sholl L.M, & Jänne P.A. (2020). Genomic and pathological heterogeneity in clinically diagnosed small cell lung cancer in never/light smokers identifies therapeutically targetable alterations. Molecular Oncology, 15(1), 27-42.

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Localization of Nuclear p65 Protein

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Cells were fixed with freshly prepared 3% paraformaldehyde for 15 minutes and permeabilized with 0.5% Triton X-100 (Boston BioProducts, Inc.) for 15 minutes. After 1 hours of incubation with 10% normal goat serum/PBS, cells were incubated with anti-p65 antibody (Santa Cruz Laboratories, Santa Cruz, CA, USA) diluted 1:50 in PBS for 2 hours, washed and incubated with fluorescein isothiocyanate (FITC)-conjugated immunoglobulin G, and diluted at 1:100 in PBS for 1 hour. In order to identify the nuclei, the FITC-labeled samples were counterstained with 10 μg/mL of propidium iodide for 2 minutes. To acquire the immunofluorescence images, a confocal microscope (Cell Voyager, Yokogawa, Japan) was used.

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Immunofluorescence Analysis of Endogenous Proteins

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For immunofluorescence analysis of endogenous proteins, cells were grown overnight on coverslips in a 6-well culture plate. Cells were then fixed in 4% paraformaldehyde for 10 minutes, permeabilized in 0.5% Triton X-100 (Boston BioProducts) for 5 minutes, and incubated with primary and then secondary antibodies at 37°C for 1 hour. The following primary antibodies were used: PAX8 (Proteintech, 10336-1-AP), pan-TEAD (Cell Signaling Technology, 13295), YAP (Cell Signaling Technology, 4912), and ep300 (EMD Millipore, NA46). Detection was performed using secondary antibodies conjugated to Alexa Fluor Dyes (Molecular Probes). Cells were then stained with DAPI (0.5 µg/ml, Sigma-Aldrich, D9564) prior to microscopy using a Nikon E400 microscope under ×100 magnification.

Elias K.M., Emori M.M., Westerling T., Long H., Budina-Kolomets A., Li F., MacDuffie E., Davis M.R., Holman A., Lawney B., Freedman M.L., Quackenbush J., Brown M, & Drapkin R. (2016). Epigenetic remodeling regulates transcriptional changes between ovarian cancer and benign precursors. JCI Insight, 1(13), e87988.

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