Sealed 384 microwell plates

Manufactured by Greiner

Sealed 384-microwell plates are flat-bottom, high-throughput lab equipment used for a variety of applications such as sample storage, screening, and assays. They feature 384 individual wells in a 16x24 grid format and are sealed to prevent cross-contamination and evaporation.

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Lab products found in correlation

Varioskan flash spectral scanning multimode reader, by Thermo Fisher Scientific (3 mentions)

3 protocols using sealed 384 microwell plates

Kinetics of pTau/pK19 Fibrillation Assay

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ThT kinetics of pTau/pK19 in the absence and presence of Hsp27 and its variants were recorded using a Varioskan Flash Spectral Scanning Multimode Reader (Thermo Fisher Scientific) with sealed 384-microwell plates (Greiner Bio-One). The assay buffer is 30 mM PBS, 2 mM MgCl2, 1 mM DTT, 0.05% NaN₃, pH 7.4. 0.5% (v/v) of fibril seeds (the seeds were prepared by sonicating fibrils for 15 s) were added to promote the fibril formation of pTau/pK19. ThT fluorescence with a final ThT concentration of 30 µM in each sample was measured in triplicates with shaking at 600 rpm at 37 °C with excitation at 440 nm and emission at 485 nm.

Zhang S., Zhu Y., Lu J., Liu Z., Lobato A.G., Zeng W., Liu J., Qiang J., Zeng S., Zhang Y., Liu C., Liu J., He Z., Zhai R.G, & Li D. (2022). Specific binding of Hsp27 and phosphorylated Tau mitigates abnormal Tau aggregation-induced pathology. eLife, 11, e79898.

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Amyloid Fibril Formation Kinetics

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Amyloid fibril formation of pK19 and pTau23 were monitored using an in situ ThT-binding assay. The ThT kinetics for amyloid fibrils were recorded using a Varioskan Flash Spectral Scanning Multimode Reader (Thermo Fisher Scientific) with sealed 384-microwell plates (Greiner Bio-One). Client proteins were mixed in the absence or presence of NMNATs and variants in indicated molar ratios in a buffer of 50 mM Tris-HCl, 50 mM KCl, 5% glycerol, 0.05% NaN₃, pH 8.0, respectively. A final concentration of 50 µM ThT was added to each sample. To promote the formation of amyloid fibrils, 5% (v/v) of fibril seeds (the seeds were prepared by sonicating fibrils for 15 s) were added to pK19 and pTau23, respectively. ThT fluorescence was measured in triplicates with shaking at 600 rpm at 37 °C with excitation at 440 nm and emission at 485 nm.

Ma X., Zhu Y., Lu J., Xie J., Li C., Shin W.S., Qiang J., Liu J., Dou S., Xiao Y., Wang C., Jia C., Long H., Yang J., Fang Y., Jiang L., Zhang Y., Zhang S., Zhai R.G., Liu C, & Li D. (2020). Nicotinamide mononucleotide adenylyltransferase uses its NAD+ substrate-binding site to chaperone phosphorylated Tau. eLife, 9, e51859.

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Amyloid Aggregation Kinetics Assay

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The kinetics of α-syn, K19, Aβ₄₀, IAPP, and α-syn_1-100 fibril formation were monitored using ThT fluorescence assay. The mixture of amyloid client proteins and mN3 WT and variants were added into sealed 384-microwell plates (Greiner Bio-One), which were mixed at the indicated molar ratios in a buffer of 50 mM Tris–HCl, 150 mM NaCl, 0.05% NaN₃, pH 8.0. Then, the fluorescence was recorded by a Varioskan Flash Spectral Scanning Multimode Reader (Thermo Fisher Scientific) with shaking at 600 rpm at 37 °C using excitation at 440 nm and emission at 485 nm. To accelerate the fibrillation, 0.5% (v/v) of fibril seeds (the seeds were obtained by sonicating fibrils for 15 s) were added to K19, α-syn, and α-syn_1-100, respectively. The final concentration of ThT in each sample was 50 μM and three replicates were performed. The ThT results showing the influence of NaCl on the aggregation of α-syn was normalized by the strategy that at each salt concentration, the ThT fluorescence of α-syn with/without mN3 was normalized by using the average ThT value at the end time point (80 h) of the samples without mN3 as 100%.

Huang C., Lu J., Ma X., Qiang J., Wang C., Liu C., Fang Y., Zhang Y., Jiang L., Li D, & Zhang S. (2022). The mouse nicotinamide mononucleotide adenylyltransferase chaperones diverse pathological amyloid client proteins. The Journal of Biological Chemistry, 298(5), 101912.

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