Ecolite scintillation fluid

Manufactured by MP Biomedicals

Sourced in United States

EcoLite scintillation fluid is a liquid scintillation cocktail designed for use in liquid scintillation counting. It is a clear, ready-to-use solution that provides high counting efficiency and low background for a variety of radioisotopes, including tritium, carbon-14, and others.

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Lab products found in correlation

Qae sephadex, by GE Healthcare (2 mentions) Bca protein assay kit, by Thermo Fisher Scientific (2 mentions) Silica gel f260 tlc plate, by Merck Group (2 mentions) Bisphenol a, by Merck Group (1 mentions) Tocopherol stripped corn oil, by MP Biomedicals (1 mentions) Tri carb 2800tr liquid scintillation counter, by PerkinElmer (1 mentions) Whatman, by Cytiva (1 mentions) 2 14c iaa, by Hartmann Analytic (1 mentions) Ls 6500 multi purpose scintillation counter, by Beckman Coulter (1 mentions)

Close spelling variants of this product

EcoLite (16 citations)

9 protocols using ecolite scintillation fluid

Bisphenol A Dosing in Silastic Capsules

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Bisphenol A (≥99% pure) was obtained from Aldrich (St. Louis, MO). Authentic tritiated BPA (10.8 Ci/mmol) was obtained from Moravek Biochemicals (Brea, CA). Tocopherol-stripped corn oil and Ecolite(+) scintillation fluid were obtained from MP Biomedical (Santa Ana, CA). Silastic tubing (Dow Corning 2415569, 0.062 in I.D. x 0.125 in O.D.) was obtained from Fisher Scientific (Waltham, MA). ß-glucuronidase (type H-1) was obtained from Sigma Aldrich (St. Louis, MO). Other reagents were obtained from Fisher Scientific (Waltham, MA) and were HPLC grade where available.
For BPA capsules, BPA was dissolved in Tocopherol-stripped corn oil at 0 (oil vehicle alone), 6, 60 or 600 μg BPA in 20 μl oil, and these solutions were used to fill Silastic capsules (20 μl/capsule, 1 cm between the capped ends).

Taylor J.A., Sommerfeld-Sager J.M., Meng C.X., Nagel S.C., Shioda T, & vom Saal F.S. (2018). Reduced body weight at weaning followed by increased post-weaning growth rate interacts with part-per-trillion fetal serum concentrations of bisphenol A (BPA) to impair glucose tolerance in male mice. PLoS ONE, 13(12), e0208846.

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GlcNAc-P Transferase Activity Assay in GNPTAB-/- Cells

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Constructs encoding WT and mutant proteins were expressed in GNPTAB^−/− HeLa cells or HEK 293 cells by transfection with jetOPTIMUS transfection reagent from Polyplus (Illkirch, France) according to the manufacturer’s protocol. Cells in 6-well plates were harvested 24 h post-transfection and lysed in 250 μl of buffer A (25 mM Tris-Cl, pH 7.2, 150 mM NaCl, 1% Triton-X 100 and protease inhibitor cocktail). 50 μg of cell lysate (5 μg in the case of cells expressing ΔS1-S3) in a final volume of 50 μl was incubated for 1 h at 37°C in buffer containing 100 mM α-methyl mannoside, 50 mM Tris-HCl, pH 7.4, 10 mM MgCl₂, 2 mM ATP, 75 μM UDP-[³H]GlcNAc (1 μCi), and 2 mg/mL bovine serum. The reactions were terminated by addition of 950 μl of 2 mM EDTA, pH 8.0. The sample was applied to a 1 mL column of QAE-Sephadex (GE Healthcare, Chicago, IL) equilibrated with 2 mM Tris base, pH 8.0. The column was washed with 5 mL of 2 mM Tris base and phosphorylated products were eluted with 5 mL of 2 mM Tris base containing 30 mM NaCl. The incorporated [³H]GlcNAc-P was determined by addition of 8.5 mL of EcoLite scintillation fluid (MP Biomedicals Inc., Irvine, CA). The background activity in non-transfected cells was less than 1% of that obtained with cells transfected with WT human GNPTAB cDNA.

Li H., Lee W.S., Feng X., Bai L., Jennings B.C., Liu L., Doray B., Canfield W.M., Kornfeld S, & Li H. (2022). Structure of the human GlcNAc-1-phosphotransferase αβ subunits reveals regulatory mechanism for lysosomal enzyme glycan phosphorylation. Nature structural & molecular biology, 29(4), 348-356.

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GlcNAc-1-phosphotransferase Activity Assay

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Constructs encoding the WT and TMD mutant precursors were expressed in HEK 293 cells by transfection with the jetOPTIMUS transfection reagent from Polyplus (Illkirch, France) according to the manufacturer’s protocol. Cells in 6-well plates were harvested 48 h post-transfection and lysed in 100 μl of buffer A (25 mM Tris-Cl, pH 7.2, 150 mM NaCl, 1% Triton-X 100 and protease inhibitor cocktail). 30 μg of each cell lysate was incubated for 2 h at 37 °C in a buffer containing 100mM α-methyl mannoside, 50 mM Tris-HCl, pH 7.4, 10 mM MgCl₂, 10 mM MnCl₂, 75 μM UDP-[³H]GlcNAc (1 μCi), and 2 mg/mL bovine serum albumin in a final volume of 50 μl. The reactions were terminated by addition of 950 μl of 5 mM EDTA, pH 8.0. The sample was applied to a 1 mL column of QAE-Sephadex (GE Healthcare, Chicago, IL) equilibrated with 2 mM Tris base, pH 8.0. The column was washed with 5 mL of 2 mM Tris base and the phosphorylated products were eluted with 5 mL of 2 mM Tris base containing 30 mM NaCl. The incorporated [³H]GlcNAc-P was determined by addition of 8.5 mL of EcoLite scintillation fluid (MP Biomedicals Inc., Irvine, CA). The background activity in non-transfected cells less than 1% of that obtained with cells transfected with WT GlcNAc-1-phosphotransferase cDNA.

Lee W.S., Jennings B.C., Doray B, & Kornfeld S. (2020). Disease-causing Missense Mutations within the N-terminal Transmembrane Domain of GlcNAc-1-phosphotransferase Impair Endoplasmic Reticulum Translocation or Golgi Retention. Human mutation, 41(7), 1321-1328.

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Measuring Intracellular Drug Accumulation with [3H]-Saquinavir

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Radio-labeled ³H-SQV (specific activity: 1.0 Ci/mM) was obtained from Moravek Biochemicals (Brea, CA, USA) and was used to measure intracellular drug accumulation [7 (link)]. Briefly, HuT78 cells were cultured in 24-well plates (5 × 10⁵ per well) and pre-exposed to CyO2 (0.5 and 1.5 μM) for either 10 min or 30 min, followed by washing off with PBS and addition of ³H-SQV (1.7 pM) and incubation at 37 °C for 2 h. Cells were harvested by centrifugation and extracts obtained by lysing with 1.0 M ammonium hydroxide (NH₄OH). Intracellular levels of ³H-SQV were monitored in the lysates, and 100 μL of the lysate was used to measure protein levels by using the BCA protein assay kit (ThermoFisher, Waltham, MA, USA). The remaining 100 μL of the lysate was dissolved in 10 mL of EcoLite scintillation fluid from MP Biomedicals (Santa Ana, CA, USA) and count per minute (CPM) were determined by using a Tri-Carb 2800TR Liquid Scintillation counter (Perkin Elmer, Waltham, MA, USA). In respective samples, data were normalized to the protein contents and presented as CPM/μg of protein.

Gerlach S.L., Chandra P.K., Roy U., Gunasekera S., Göransson U., Wimley W.C., Braun S.E, & Mondal D. (2019). The Membrane-Active Phytopeptide Cycloviolacin O2 Simultaneously Targets HIV-1-infected Cells and Infectious Viral Particles to Potentiate the Efficacy of Antiretroviral Drugs. Medicines, 6(1), 33.

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MRP4 Substrate Transport Assay

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Transport assays for MRP4 were carried out using two reported MRP4 substrates [adenine-8-³H-tenofovir disoproxil (TFV) (3.8 Ci/mmol, 98.1% purity); ³H-9-(2-phosphonylmethoxyethyl)-adenine (PMEA)] (Moravek Biochemicals, Brea, CA, USA) as described previously (19 (link),20 (link),30 (link)). Briefly, MRP4 and empty vector cells were seeded at 2.5×10⁵ cells/well in triplicate in poly-D-lysine-coated 24-well plates (BD Biosciences, San Jose, CA, USA). After preincubation for 24 h, cells were incubated with 1 µM TFV or 100 nM PMEA in glucose-free DMEM supplemented with 10 µM NaN₃ and 10 µM 2-deoxy-D-glucose, respectively, for 2 h at 37°C. After accumulation, cells were washed with ice-cold PBS and supplemented with complete DMEM. Supernatant fractions were collected at 0, 30 and 90 min, and cells were washed and lysed with 800 µl/well of an aqueous solution of 10% sodium dodecyl sulfate and 1 N NaOH. Supernatants were added to Ecolite scintillation fluid (MP Biomedicals, Santa Ana, CA, USA) and extracellular amounts of TFV and PMEA were analyzed by scintillation counting. The remaining cell lysate was used to determine the protein concentration with a BCA™ Protein Assay kit (Pierce Biotechnology, Rockford, IL, USA); TFV and PMEA levels were normalized to protein concentrations.

Yuan B., Yoshino Y., Fukushima H., Markova S., Takagi N., Toyoda H, & Kroetz D.L. (2015). Multidrug resistance-associated protein 4 is a determinant of arsenite resistance. Oncology Reports, 35(1), 147-154.

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Aminoacylation Assay for Hp tRNA

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Each tRNA was pre-folded as previously described [29 (link)]. Aminoacylation assays were conducted in buffer containing 100 mM Na-HEPES, pH 7.5, 30 mM KCl, 12 mM MgCl₂, 2 mM ATP, 0.1 mg/mL BSA, 20 μM amino acid, 50 μCi/mL ³H-labeled amino acid, and 10 μM Hp tRNA^Asn or tRNA^Gln as noted. Assays were conducted at 37 °C and were initiated with the addition of 200 nM Hp ND-AspRS or GluRS2. Aliquots were removed and quenched on Whatman filter pads containing TCA. The pads were washed 3 times for 15 min with chilled 5% TCA. Pads were dried and counted in 3 mL ECOLITE (+) scintillation fluid (MP Biomedicals, Solon, OH, USA). Aminoacylation assays with total Ec tRNA were carried out in the same buffer containing 50–100 μM total tRNA. Hp ND-AspRS (100 nM or 500 nM) or Hp GluRS2 (100 nM or 500 nM) were used in these assays as noted.

Rathnayake U.M, & Hendrickson T.L. (2019). Bacterial Aspartyl-tRNA Synthetase Has Glutamyl-tRNA Synthetase Activity. Genes, 10(4), 262.

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Assay of IAGlc Synthase Activity

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Enzymatic activity of IAGlc synthase was determined in a total volume of 8 μL containing 74.1 mM HEPES buffer, pH 7.4, 10.9 mM UDPG, 5.8 mM IAA, 592 Bq [2’-¹⁴C]IAA (2.035 GBq mmol⁻¹; Hartmann Analytic GmBH, Braunschweig, Germany), 18 mM D-gluconic acid lactone and 3.6 mM MgCl₂, with 3 μL of the supernatant fluid from tissue homogenates. The reaction was stopped after 30 min incubation at 30 °C by drying 4 μL of aliquots on Silica Gel F₂₆₀ TLC plate (Merck, Darmstadt, Germany). TLC was performed using ethyl acetate: n-butanone: ethanol: water (5: 3: 1: 1, by vol.) as a solvent. For indole compounds visualization, the plate was stained with van Urk-Salkowski reagent (Ehmann 1977 (link)). Bands corresponding to IAGlc were excised and placed in a vial with 2 mL EcoLite ( +) scintillation fluid (MP Biomedicals, Irvine, CA, USA). Radioactivity level was measured in Wallac 1409 liquid scintillation counter (Wallac Oy, Turku, Finland).

Ciarkowska A., Wojtaczka P., Kęsy J, & Ostrowski M. (2022). Auxin homeostasis in maize (Zea mays) is regulated via 1-O-indole-3-acetyl-myo-inositol synthesis at early stages of seedling development and under abiotic stress. Planta, 257(1), 23.

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IAInos Biosynthesis Enzyme Activity Assay

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Enzymatic activity of IAInos synthase towards IAInos biosynthesis was determined in a total volume of 8 μL containing 25.2 mM HEPES buffer, pH 7.4, 12 mM UDPG, 6.4 mM IAA, 592 Bq [2’-¹⁴C]IAA (2.035 GBq mmol⁻¹; Hartmann Analytic GmBH), 15 mM myo-inositol, 18 mM D-gluconic acid lactone, 4 mM MgCl₂ and 3 μU of recombinant IAGlc synthase, with 3 μL of the supernatant fluid from tissue homogenates. The reaction was stopped after 30 min incubation at 30 °C by drying 4 μL of aliquots on Silica Gel F₂₆₀ TLC plate (Merck). TLC was performed using ethyl acetate: n-butanone: ethanol: water (5: 3: 1: 1, by vol.) as a solvent. For indole compounds visualization, the plate was stained with van Urk-Salkowski reagent (Ehmann 1977 (link)). Bands corresponding to IAInos were excised and placed in a vial with 2 mL EcoLite ( +) scintillation fluid (MP Biomedicals). Radioactivity level was measured in Wallac 1409 liquid scintillation counter (Wallac Oy).

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Quantifying Brain Region-Specific Radioactivity

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Radioactive samples were mixed with 4 mL of ECOLITE scintillation fluid (MP biomedicals, Santa Ana CA) in 5 mL scintillation vials (Lake Charles, Lake Charles LA) and counted for 1 min in LS 6500 Multipurpose Scintillation Counter (Beckman Coulter, Brea, CA) operating in auto-DPM mode (all results are reported in disintegrations-per-minute, DPM). The activities in an aliquot of the lower dicholoromethane phase of a Bligh–Dyer extract (BD_L) and in a suspension of the upper and middle phases (BD_MU) were measured, scaled by the volume of each phase (V_L and V_MU), summed, and divided by the mass of the tissue sample (M_t) to obtain its specific radioactivity (eq 1). Approximately 1/10 of the injections yielded a dramatically high specific radioactivity in the hippocampus (more than twice the average); these abnormalities were attributed to inadvertent injection directly into the hippocampus and were excluded from the analysis. To correct for differences in the amount of radioactivity injected into each animal, the specific radioactivities in the cerebellum and hippocampus were divided by the specific radioactivity of the total brain to obtain relative specific radioactivities (eq 2).

Furman R., Murray I.V., Schall H.E., Liu Q., Ghiwot Y, & Axelsen P.H. (2016). Amyloid Plaque-Associated Oxidative Degradation of Uniformly Radiolabeled Arachidonic Acid. ACS chemical neuroscience, 7(3), 367-377.

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