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Microbeta trilux

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The MicroBeta TriLux is a high-performance liquid scintillation and luminescence counter designed for life science research applications. It offers a range of detection capabilities, including radioactive and luminescent assays.

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Lab products found in correlation

3h thymidine, by PerkinElmer (8 mentions) Whatman, by Cytiva (5 mentions) 3h thymidine, by Hartmann Analytic (5 mentions) Lumaplate, by PerkinElmer (4 mentions) Rotiszint eco plus, by PerkinElmer (4 mentions) Gf c 96 well plate, by Merck Group (4 mentions) Prism 5, by GraphPad (3 mentions) Bright glo reagent, by Promega (3 mentions) Triton x 100, by Merck Group (3 mentions) Filtermate harvester, by PerkinElmer (3 mentions) Net974001mc, by PerkinElmer (3 mentions) Multiscreen gf b 96 well plate, by Merck Group (3 mentions) Glosensor 22f, by Promega (2 mentions) Flipr, by Molecular Devices (2 mentions) Glosensor, by Promega (2 mentions) Glosensor 22f plasmid, by Promega (2 mentions) Nap 5 column, by GE Healthcare (2 mentions) Anti myc positive control antibody, by Cell Signaling Technology (2 mentions) Sephadex protein a g beads, by Merck Group (2 mentions) Concanavalin a (cona), by Merck Group (2 mentions)

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127 protocols using microbeta trilux

1

D1R GS-cAMP Accumulation Assay

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D1R GS-mediated GS-cAMP accumulation assays with HEK293T cells co-expressing human D1 and the cAMP biosensor GloSensor-22F (Promega) were performed. Cells were seeded (15 000 cells/40 μL/ well) into white 384 clear-bottom, tissue culture plates in DMEM containing 1% dialyzed fetal bovine serum (FBS). Next day, drug dilutions were diluted in HBSS, 20 mM N-(2-hydroxyethyl)piperazine-N′-ethanesulfonic acid (HEPES), 0.1% bovine serum albumin (BSA), 0.01% ascorbic acid, pH 7.4. Next, media was decanted from 384 well plates and 20 μL of drug buffer (HBSS, 20 mM HEPES, pH 7.4) containing GloSensor reagent was added per well and allowed to equilibrate for at least 15 min room temperature. To start the assay, cells were treated with 10 μL per well of 3× drug diluted in HBSS, 20 mM HEPES, 0.1% BSA, 0.01% ascorbic acid, pH 7.4 using a FLIPR (molecular devices). After 15 min, GS-cAMP accumulation was read on a TriLux Microbeta (PerkinElmer) plate counter. Data were normalized to maximum GS-cAMP accumulation by dopamine (100%). Data were analyzed using the sigmoidal dose−response function built into GraphPad Prism 5.0.
Martini M.L., Liu J., Ray C., Yu X., Huang X.P., Urs A., Urs N., McCorvy J.D., Caron M.G., Roth B.L, & Jin J. (2019). Defining Structure−Functional Selectivity Relationships (SFSR) for a Class of Non-Catechol Dopamine D1 Receptor Agonists. Journal of medicinal chemistry, 62(7), 3753-3772.
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2

Quantifying Gi/o-Mediated cAMP Inhibition

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To measure Gi/o-mediated cAMP inhibition, HEK293T cells were co-transfected in a 1:1 ratio with receptor and a split-luciferase-based cAMP biosensor (GloSensor; Promega) as described. After at least 24 hours, transfected cells were plated in poly-lysine coated 384-well white clear bottom cell culture plates with DMEM containing 1% dialyzed FBS at a density of 15,000 cells per 40 μL per well and incubated overnight. On the day of assay, drug dilutions were prepared in filtered fresh assay buffer (20 mM HEPES, 1X HBSS, 0.1% BSA, 0.01% ascorbic acid, pH 7.4) at 3X and 10 μL per well was added to cells containing 20 μL/well of assay buffer. Drug solutions used for G protein-mediated cAMP assays were exactly the same as used for Tango assays to allow relative within-experiment bias comparisons. After plates were allowed to incubate with drug for 15 minutes, 10 μL per well of 1 μM (final concentration) forskolin and GloSensor substrate was added. Luminescence counts per second (LCPS) were quantified after 15 minutes using a TriLux microbeta (Perkin Elmer) luminescence counter. LCPS were plotted as a function of drug concentration and normalized to % quinpirole with 100% as the quinpirole cAMP inhibition Emax and 0% as the forskolin-stimulate cAMP baseline. Data were analyzed using log (agonist) vs. response in GraphPad Prism 5.0 (Graphpad Software Inc., San Diego, CA).
McCorvy J.D., Butler K.V., Kelly B., Rechsteiner K., Karpiak J., Betz R.M., Kormos B.L., Shoichet B.K., Dror R.O., Jin J, & Roth B.L. (2017). Structure-inspired design of β-arrestin-biased ligands for aminergic GPCRs. Nature chemical biology, 14(2), 126-134.
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3

Quantifying Gi/o-Mediated cAMP Inhibition

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To measure Gi/o-mediated cAMP inhibition, HEK293T cells were co-transfected in a 1:1 ratio with receptor and a split-luciferase-based cAMP biosensor (GloSensor; Promega) as described. After at least 24 hours, transfected cells were plated in poly-lysine coated 384-well white clear bottom cell culture plates with DMEM containing 1% dialyzed FBS at a density of 15,000 cells per 40 μL per well and incubated overnight. On the day of assay, drug dilutions were prepared in filtered fresh assay buffer (20 mM HEPES, 1X HBSS, 0.1% BSA, 0.01% ascorbic acid, pH 7.4) at 3X and 10 μL per well was added to cells containing 20 μL/well of assay buffer. Drug solutions used for G protein-mediated cAMP assays were exactly the same as used for Tango assays to allow relative within-experiment bias comparisons. After plates were allowed to incubate with drug for 15 minutes, 10 μL per well of 1 μM (final concentration) forskolin and GloSensor substrate was added. Luminescence counts per second (LCPS) were quantified after 15 minutes using a TriLux microbeta (Perkin Elmer) luminescence counter. LCPS were plotted as a function of drug concentration and normalized to % quinpirole with 100% as the quinpirole cAMP inhibition Emax and 0% as the forskolin-stimulate cAMP baseline. Data were analyzed using log (agonist) vs. response in GraphPad Prism 5.0 (Graphpad Software Inc., San Diego, CA).
McCorvy J.D., Butler K.V., Kelly B., Rechsteiner K., Karpiak J., Betz R.M., Kormos B.L., Shoichet B.K., Dror R.O., Jin J, & Roth B.L. (2017). Structure-inspired design of β-arrestin-biased ligands for aminergic GPCRs. Nature chemical biology, 14(2), 126-134.
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4

D1R Gs-cAMP Accumulation Assay

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D1R GS-mediated GS-cAMP accumulation assays with HEK293T (ATCC CRL-11268) were performed using cells transiently expressing human D1R and the cAMP biosensor GloSensor-22F (Promega). Cells were seeded (20 000 cells/35 μL/well) into white 384 clear-bottom, tissue culture plates in DMEM containing 1% (v/v) dialyzed fetal bovine serum (FBS). Next day, 3x drug dilutions were diluted in HBSS, 20 mM N-(2-hydroxyethyl) piperazine-N′-ethanesulfonic acid (HEPES), 0.3% (w/v) bovine serum albumin (BSA), 0.03% (w/v) ascorbic acid, pH 7.4. Media was decanted from 384 well plates and 20 μL of drug buffer (HBSS, 20 mM HEPES, pH 7.4) containing GloSensor reagent was added per well and allowed to equilibrate for at least 15 min at room temperature. Cells were then treated with 10 μL per well of 3 × drug using a FLIPR (Molecular Devices). After 15 min, Gs-cAMP accumulation was read on a TriLux Microbeta (PerkinElmer) plate counter. Data were analyzed using the sigmoidal log(agonist) versus dose response function built into GraphPad Prism 8.4.
Zhuang Y., Xu P., Mao C., Wang L., Krumm B., Zhou X.E., Huang S., Liu H., Cheng X., Huang X.P., Shen D.D., Xu T., Liu Y.F., Wang Y., Guo J., Jiang Y., Jiang H., Melcher K., Roth B.L., Zhang Y., Zhang C, & Xu H.E. (2021). Structural insights into the human D1 and D2 dopamine receptor signaling complexes. Cell, 184(4), 931-942.e18.
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5

DRD1 Tango Assay Protocol for Arrestin Recruitment

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Human DRD1 Tango constructs were designed and assays were performed as previously described (Kroeze et al., 2015 (link); Liu et al., 2013 (link)). HTLA cells expressing TEV fused-β-Arrestin2 (kindly provided by Dr. Richard Axel, Columbia Univ.) were transfected with the 8 μg DRD1 Tango construct. After at least 16 h, cells were plated in DMEM supplemented with 1% (v/v) dialyzed FBS in poly-L-lysine coated 384-well white clear bottom cell culture plates at a density of 10,000–15,000 cells/well in a total of 40 μL. The cells were incubated for at least 6 h before receiving drug stimulation. Drug solutions were prepared in drug buffer (20 mM HEPES, 1 × HBSS, 0.3% BSA, pH 7.4) at 3 × and added to cells (20 μL per well) for overnight incubation. After at least 16 h, media and drug solutions were removed and 20 μL per well of diluted 1:20 BrightGlo reagent (Promega) was added. The plate was incubated for 20 min at room temperature in the dark before being counted using a TriLux Microbeta (PerkinElmer) plate counter. Results (relative luminescence units) were plotted as a function of drug concentration and analyzed using GraphPad Prism 8.4.
Zhuang Y., Xu P., Mao C., Wang L., Krumm B., Zhou X.E., Huang S., Liu H., Cheng X., Huang X.P., Shen D.D., Xu T., Liu Y.F., Wang Y., Guo J., Jiang Y., Jiang H., Melcher K., Roth B.L., Zhang Y., Zhang C, & Xu H.E. (2021). Structural insights into the human D1 and D2 dopamine receptor signaling complexes. Cell, 184(4), 931-942.e18.
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6

Glucose Uptake Assay for hASC-Adipocytes

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In vitro glucose uptake in hASC-adipocytes was modified from [32] (link). hASC-adipocytes were stimulated with insulin and/or FGF21 in 0.2%BSA w/v in DPBS (Life Technologies 14040133) for 30 min at 37°C. After stimulation, media was supplemented with 28 uM [14C]-2DG (PerkinElmer, NEC-495A), 800 uM 2DG (Sigma Cat# D3179) at final concentration for 30 min at 37°C. Cells were washed three times with cold PBS then lysed with 100 uL 1% Triton X-100 w/v in ddH2O for 30 min at room temp while shaking. Lysates were transferred to a 96-well LumaPlate (Perkin Elmer 6005630), dried overnight, and read for 14C on a Perkin Elmer Trilux MicroBeta for CPM. FGF21 neutralizing antibody (nAb) was custom generated and purified (clone# 9A2.H8.G4) by Green Mountain Antibodies using peptide, CGGPSQGRSPSYAS, for immunization. 100 ug/ml neutralizing antibody was used to neutralize 32 nM FGF21 in assay buffer 30 min prior to treating the cells.
Lee D.V., Li D., Yan Q., Zhu Y., Goodwin B., Calle R., Brenner M.B, & Talukdar S. (2014). Fibroblast Growth Factor 21 Improves Insulin Sensitivity and Synergizes with Insulin in Human Adipose Stem Cell-Derived (hASC) Adipocytes. PLoS ONE, 9(11), e111767.
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7

Assessing Antimalarial Drug Susceptibility

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In vitro susceptibility of the parasites to AQ-13 and dAQ was determined using the [3H]hypoxanthine uptake inhibition assay9 (link) against 38 P. falciparum isolates. AQ-13 [Ro 47-0543: N-(7-chloroquinolin-4-yl)-N′,N′-diethylpropane-1,3-diamine] was obtained from Medicine for Malaria Venture, monodesethylamodiaquine (dAQ) and DMSO (used as vehicle) were obtained from WWARN & Sigma Aldrich, Singapore, respectively. Parasites were synchronized at ring stage using two 5% d-sorbitol treatments (0–6 h post-invasion) and exposed to a concentration range of AQ-13 or dAQ (0.7 to 500 nM) for 48 h in presence of 0.5 μCi of [3H]hypoxanthine (Perkin-Elmer, Waltham, USA). Tritium incorporation was measured with a β-counter (Trilux microbeta; Perkin-Elmer Waltham, USA). Inhibitory concentrations values (IC50) were determined using IVART online software (https://www.wwarn.org/ivart).10 (link) Four P. falciparum laboratory reference strains were used as controls: 3D7, 7G8, W2 and Dd2. We chose an IC50 value >60 nM to define resistance to amodiaquine, according to previous studies.11 (link)
Nardella F., Mairet-Khedim M., Roesch C., Maher S.P., Ke S., Leang R., Leroy D, & Witkowski B. (2021). Cross-resistance of the chloroquine-derivative AQ-13 with amodiaquine in Cambodian Plasmodium falciparum isolates. Journal of Antimicrobial Chemotherapy, 76(10), 2565-2568.
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8

GTPγS Binding Assay for 5-HT5A Receptor

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GTPγ[35S] assays were performed in 96-well plates in assay buffer (20 mM HEPES, 100 mM NaCl, 10 mM MgCl2, 1 mM EDTA, 1 mM dithiothreitol (DTT); pH 7.4) containing 10 μM GDP, 10 μM GTPγS (only for nonspecific binding), 0.3 nM GTPγ[35S] (1250 Ci/mmol, PerkinElmer, Waltham, MA), and test or control ligands. In agonist mode, all ligands were screened at 32 μM. In antagonist mode, test ligands (100 μM) or control (10 μM SB-699551) were preincubated with a receptor for 15–30 min at RT before an EC80 of 5-HT (1.0 μM) was added. GTP loading was initiated by the addition of a premixture of cell membranes and WGA-SPA PVT beads (PerkinElmer, Waltham, MA) to a final concentration of 0.25 mg beads/well and 15 000 cpm 5-HT5AR-Gi1/well (as determined by [3H]-LSD binding). Plates were sealed and agitated at RT for 3 h (agonist mode) and 3–5 h (antagonist mode). Plates were counted in SPA mode in a PerkinElmer TriLux microbeta. Results (CPM) were normalized to 5-HT response in GraphPad Prism 5.0.
Kaplan A.L., Strachan R.T., Braz J.M., Craik V., Slocum S., Mangano T., Amabo V., O’Donnell H., Lak P., Basbaum A.I., Roth B.L, & Shoichet B.K. (2022). Structure-Based Design of a Chemical Probe Set for the 5-HT5A Serotonin Receptor. Journal of medicinal chemistry, 65(5), 4201-4217.
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9

Induction and Functional Assay of Regulatory T Cells

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Treg cells were induced in 24 well plates with coated anti-CD3 (5 ug/ml coated overnight at 4 degrees in PBS), soluble anti-CD28 (1 ug/ml), IL-2 (5 ng/ml) and TGF-β at 5 ng/ml or concentrations indicated. Control antibody or MH5A was added at 10 ug/ml where indicated. For Treg proliferation, Treg cells culture for 5 days as above were MACS isolated by CD25 positive selection and plated in 96-well plates pre-coated with anti-CD3 at indicated concentrations and IL-2 (5 ng/ml). 3H-thymidine (Perkin-Elmer) was added to wells during final 8 hours of culture and cells were analyzed for DNA-incorporation (proliferation) using a Trilux Microbeta (Perkin-Elmer). Treg suppressive function in the presence of MH5A was analyzed in an MLR assay using induced Treg cells as above. Treg cells were incubated with either control Ab or MH5A for one hour, then washed and added to 96-well round bottom plates containing B6 T cells (responders) and lethally irradiated BDF1 target splenocytes. Ratio indicates the Treg to responder ratio, with responder cells remaining consistent in all wells, and Treg cells decreasing along the x-axis of graph. Cells were cultured for 5 days. 3-H-thymidine was added during final hours of culture and analyzed as above.
Flies D.B., Higuchi T, & Chen L. (2015). Mechanistic Assessment of PD-1H Coinhibitory Receptor-Induced T-Cell Tolerance to Allogeneic Antigens. Journal of immunology (Baltimore, Md. : 1950), 194(11), 5294-5304.
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10

PRESTO-Tango Assay for 5-HT1e and 5-HT1F Receptor Recruitment

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For β-arrestin2 recruitment, we used the PRESTO-Tango assay, which was performed essentially as described (17 (link)). The 5-HT1eR and 5-HT1FR PRESTO-Tango constructs were obtained from Addgene. DNA was incubated with PEI in OptiMEM and then added to HEK293T cells in DMEM supplemented with 1% (v/v) dialyzed FBS. After transfection, cells were placed into the 37°C incubator overnight. The following day, cells were plated in DMEM supplemented with 1% (v/v) dialyzed FBS in wells of poly-lysine–coated white, transparent bottom 384-well plates as described above. The cell plates were placed into the 37°C incubator for approximately 4 hours or until cells adhered to the bottom of the plate. Drugs diluted in series to 3× concentration in assay buffer were then added directly to cell media, and the plates were incubated at 37°C overnight for approximately 16 hours. The next day, the drug solution and media were removed and replaced with 20 μl of BrightGlo Reagent (Promega). Cells were incubated in the dark at room temperature for 20 min before being read in a PerkinElmer Trilux Microbeta. LCPS were reported and then plotted as a function of drug concentration and analyzed in a nonlinear regression analysis of log(agonist) versus response in GraphPad Prism 8.0.
Zilberg G., Parpounas A.K., Warren A.L., Fiorillo B., Provasi D., Filizola M, & Wacker D. (2024). Structural insights into the unexpected agonism of tetracyclic antidepressants at serotonin receptors 5-HT1eR and 5-HT1FR. Science Advances, 10(16), eadk4855.
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