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96 well black microplates

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The 96-well black microplates are a versatile laboratory tool designed for a variety of applications. They feature a 96-well format with a black surface, which can be used for various fluorescence-based assays and experiments. The microplates are made of high-quality materials and are suitable for use with both manual and automated pipetting systems.

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Lab products found in correlation

Prism 4, by GraphPad (1 mentions) Victor x5, by PerkinElmer (1 mentions) Victor x5 plate reader, by PerkinElmer (1 mentions)

3 protocols using 96 well black microplates

1

Time-Resolved FRET Assay for ER-Coactivator Interaction

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SRC3 was titrated into a fixed amount of ERα-LBD-biotin mixed with SaTb (streptavidin-terbium, Invitrogen, Grand Island, NY), on 96-well black microplates (Molecular Devices, Sunnyvale, CA) following previously determined methods (Jeyakumar et al., 2011 (link)). The time-resolved Förster resonance energy transfer (tr-FRET) measurements were performed with a Victor X5 plate reader (Perkin Elmer, Shelton, CT) with an excitation filter at 340/10 nm and emission filters for terbium and fluorescein at 495/20 and 520/25 nm, respectively, with a 100 µs delay. Diffusion-enhanced FRET was determined by a parallel incubation without biotinylated ER-LBD and subtracted as a background signal. The final concentrations of reagents were: 1 nM ERα-417, 0.25 nM streptavidin-terbium, 1 µM ligand, SRC3-F1 coactivator titrated from 3.2×10-7 to 3.2×10–12M. The data, representing 2–3 replicate experiments, each with duplicate points, were analyzed using GraphPad Prism 4 and are expressed as the EC50 in nM.
Fanning S.W., Mayne C.G., Dharmarajan V., Carlson K.E., Martin T.A., Novick S.J., Toy W., Green B., Panchamukhi S., Katzenellenbogen B.S., Tajkhorshid E., Griffin P.R., Shen Y., Chandarlapaty S., Katzenellenbogen J.A, & Greene G.L. (2016). Estrogen receptor alpha somatic mutations Y537S and D538G confer breast cancer endocrine resistance by stabilizing the activating function-2 binding conformation. eLife, 5, e12792.
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2

Measuring ER-LBD Coactivator Binding

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SRC3 was titrated into a fixed amount of ER-LBD-biotin mixed with SaTb (streptavidin-terbium, Invitrogen, Grand Island, NY), on 96-well black microplates (Molecular Devices, Sunnyvale, CA), following previously determined methods.[16 , 20 (link)] The time-resolved Fluorescence Resonance Energy Transfer (tr-FRET) was measured with a Victor X5 plate reader (Perkin Elmer, Shelton, CT) with an excitation filter at 340/10 nm and emission filters for terbium and fluorescein at 495/20 and 520/25 nm, respectively, with a 100 μs delay. Diffusion-enhanced FRET was determined by a parallel incubation without biotinylated ER-LBD and subtracted as a background. The final concentrations of reagents were: 1 nM ER-LBD-biotin, 0.25 nM streptavidin-terbium, 1 μM ligand, SRC3 coactivator titrated from 3.2×10−7 to 3.2×10−12 M. The data, representing two to three replicate experiments, each with duplicate points, was analyzed using GraphPad Prism 4 and is expressed as the EC50 in nM.
Granchi C., Lapillo M., Spena C.R., Rizzolio F., Tuccinardi T., Martin T.A., Carlson K.E., Katzenellenbogen J.A, & Minutolo F. (2016). Cyclic-ketoximes as ER beta-selective agonists. ChemMedChem, 11(16), 1752-1761.
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3

Measurement of SRC-ER Interaction Kinetics

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SRC1 or SRC3 NR interaction domains (ca. 200 amino acids) were titrated into a fixed amount of ERα-LBD-biotin preparations of the six 375 genotypes (1 nM) and mixed with 25 nM streptavidin-terbium (Invitrogen, Grand Island, NY) and 25 μM of ligand, on 96-well black microplates (Molecular Devices, Sunnyvale, CA) following previously determined methods (23 (link), 53 (link)). The time-resolved FRET measurements were performed with a Victor X5 plate reader (Perkin Elmer, Shelton, CT). Diffusion-enhanced FRET was determined by a parallel incubation without biotinylated ER-LBD and subtracted as a background signal. The data, representing two to three replicate experiments, each with duplicate points, were analyzed using GraphPad Prism 4 and are expressed as Kd ± SD in nM.
Li Y., Coons L.A., Houtman R., Carlson K.E., Martin T.A., Mayne C.G., Melchers D., Jefferson T.B., Ramsey J.T., Katzenellenbogen J.A, & Korach K.S. (2020). A mutant form of ERα associated with estrogen insensitivity affects the coupling between ligand binding and coactivator recruitment. Science signaling, 13(650), eaaw4653.
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