Analyst ad

Manufactured by Molecular Devices

Sourced in United States

The Analyst AD is a high-performance microplate reader designed for researchers in life science and drug discovery applications. It provides precise and accurate absorbance measurements across a wide range of wavelengths, enabling a variety of assay types to be performed. The core function of the Analyst AD is to quantify and analyze samples in a microplate format.

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Lab products found in correlation

Black 96 well polystyrene plate, by Greiner (3 mentions) Celltiter glo luminescent cell viability assay kit, by Promega (2 mentions) Celltiter glo reagent, by Promega (1 mentions) Hepg2, by European Collection of Cell Cultures (1 mentions) Bovine gamma globulin, by Merck Group (1 mentions)

Close spelling variants of this product

Analyst AD platereader (2 citations)

8 protocols using analyst ad

In Vitro Amyloid Fibril Assay

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Samples of each filtered and ultracentrifuged protein were prepared, on ice, at a final concentration of 20 µM in 10 mM ABC buffer (pH 2.0) containing 150 mM NaCl, 10 µM thioflavin T (ThT), and 0.02% NaN₃, in 1.5 mL low-binding microcentrifuge tubes (total volume of 1.0 mL).
In vitro fibrillogenesis reactions were conducted by monitoring the fluorescence emission enhancement of thioflavin T (ThT) that occurs when ThT binds to amyloid fibrils. All fibril formation assays were performed in triplicate (260 µL per well) using black 96-well polystyrene plates (Greiner, Monroe, NC) sealed with plate sealers (Nunc, Roskilde, Denmark), covered with a black polystyrene cover, and sealed with tape to reduce evaporation. Samples were incubated at 37 °C while being continuously orbitally shaken (300 rpm) in a New Brunswick Scientific Innova40 incubator shaker. Fibril formation was monitored daily for 1 month (~750 h) following fluorescence on a plate reader (Analyst AD, Molecular Devices, Sunnyvale, CA). The excitation wavelength used was 440 nm, and the emission wavelength was 480 nm. The plate sealer and the tape sealing the cover were replaced daily.
We considered that a fibril formation reaction had occurred when we observed an at least 4-fold ThT fluorescence enhancement (~200000 AU in our system). The presence of amyloid fibrils was confirmed by electron microscopy.

Blancas-Mejía L.M, & Ramirez-Alvarado M. (2016). Recruitment of Light Chains by Homologous and Heterologous Fibrils Shows Distinctive Kinetic and Conformational Specificity. Biochemistry, 55(21), 2967-2978.

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Screening Hepatocyte Carcinoma Cell Viability

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Human Caucasian hepatocyte carcinoma cells (HepG2; European Collection of Cell Cultures, Salisbury, United Kingdom) were grown in accordance with their guidelines by using DMEM. Cells at a density of 30,000 cells/well in 96-well plates were incubated overnight (37°C, 5% CO₂ atmosphere). Medium was then removed and replaced with DMEM that contained control or compounds (1, 10, and 100 μM; n = 2 per concentration) for 24 h before addition of 100 μl/well of CellTiter-Glo Reagent (Promega, Madison, WI, USA) for ATP measurement and shaken to induce cell lysis. Luminescence was quantified on an AnalystAD plate-reader (Molecular Devices, Sunnyvale, CA, USA). Thioridizine (known HepG2 cytotoxicity) was used as positive control. Study was carried out by BioFocus DPI (Saffron Walden, United Kingdom).

Baker J.G., Gardiner S.M., Woolard J., Fromont C., Jadhav G.P., Mistry S.N., Thompson K.S., Kellam B., Hill S.J, & Fischer P.M. (2017). Novel selective β1-adrenoceptor antagonists for concomitant cardiovascular and respiratory disease. The FASEB Journal, 31(7), 3150-3166.

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Determining Drug-Induced Cell Proliferation Inhibition

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The effect of the drug on cell proliferation was determined using a CellTiter-Glo Luminescent Cell Viability Assay kit (Promega, Madison, WI), which is based on quantification of the cellular ATP level. Cells were plated in 96-well plates at a density of 2,000–5,000 cells (8 replicates per condition). The following day, cells were treated with a range of drug concentrations prepared by serial dilution. After 3–5 days of treatment, 100 ml of prepared reagent was added to each well. The contents of the wells were mixed on a plate shaker for 1 hour, and then luminescence was measured by an Analyst AD (Molecular Devices, Sunnyvale, CA). The relative growth was normalized to the untreated samples in each group. The growth or inhibition curves and IC50 values were calculated with Graph Pad Prism v.6.

Rodrik-Outmezguine V.S., Okaniwa M., Yao Z., Novotny C.J., McWhirter C., Banaji A., Won H., Wong W., Berger M., de Stanchina E., Barratt D.G., Cosulich S., Klinowska T., Rosen N, & Shokat K.M. (2016). Overcoming mTOR Resistance Mutations with a New Generation mTOR Inhibitor. Nature, 534(7606), 272-276.

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Monitoring Amyloid Fibril Formation

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ThT fluorescence from the aggregation mixture was monitored on a plate reader (Analyst AD; Molecular Devices, Sunnyvale, CA). An aliquot (~260 μL) of the fibril formation reaction (containing ThT) was placed in duplicate on a black 96 well polystyrene plate (Greiner, Monroe, NC) at specific time points (equivalent to the time points used for the sedimentation assay) to measure the fluorescence intensity. After the measurements, we placed back the reaction mixture into the microcentrifuge tube and resumed incubation at 37°C, 300 RPM in the orbital shaker till the end of the aggregation reaction. We repeat this process periodically to obtain the ThT intensity for all the time points presented in the figures. All the fluorescence measurements were done using an excitation wavelength of 440 nm and an emission wavelength of 480 nm.
For both the sedimentation and the Thioflavin T assay, we assumed the aggregation reaction had ended when the change in the minimum concentration of monomers or the Thioflavin T fluorescence intensity maximum remained constant over a period of at least 48 hrs.

Misra P., Blancas-Mejia L.M, & Ramirez-Alvarado M. (2019). Mechanistic insights into the early events in the aggregation of immunoglobulin light chains. Biochemistry, 58(29), 3155-3168.

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Monitoring Amyloid Aggregation Kinetics

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ThT fluorescence from the aggregation mixture was monitored on a plate reader (Analyst AD; Molecular Devices, Sunnyvale, CA) using an excitation wavelength of 440 nm and an emission wavelength of 480 nm as previously reported [21 (link)]. Two aliquots (~260 μL technical replicates) from the aggregation reaction (containing 20 μM ThT) were placed on a black 96-well polystyrene plate (Greiner, Monroe, NC) at specific time points to measure the fluorescence intensity. After the measurements, aliquots were placed back into the microcentrifuge tube to resume the incubation at 37°C with orbital shaking set at 300 RPM. The measurement process was repeated until the apparent change in fluorescence intensity plateaus over a period of at least 72 h.

Misra P, & Ramirez-Alvarado M. (2021). Early events in light chain aggregation at physiological pH reveal new insights on assembly, stability, and aggregate dissociation. Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis, 28(2), 113-124.

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Determining Drug-Induced Cell Proliferation Inhibition

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Fluorescence Polarization Assay Protocol

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Fluorescence polarization measurements were taken using an Analyst AD (Molecular Devices) with 530 nm excitation and 580 nm emission filters and 561 nm dichroic mirror. All experiments were conducted at room temperature in duplicate and used PBS supplemented with 0.5 mg/ml bovine gamma-globulin (Sigma) and 0.5 mM dithiothreitol, in a volume of 60 μl. Binding of TAMRA-labelled peptide is reported in millipolarisation units (mP) and is obtained from the equation, mP = 1000 × (S - G × P)/(S + G × P), where S and P are background-subtracted fluorescence count rates (S = polarised emission filter is parallel to the excitation filter; P = polarised emission filter is perpendicular to the excitation filter), and G (grating) is an instrument- and assay-dependent factor.

Hermann C., van Hateren A., Trautwein N., Neerincx A., Duriez P.J., Stevanović S., Trowsdale J., Deane J.E., Elliott T, & Boyle L.H. (2015). TAPBPR alters MHC class I peptide presentation by functioning as a peptide exchange catalyst. eLife, 4, e09617.

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SH2 Domain Binding Affinity Determination

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SH2 domains were dialyzed into binding buffer (50 mM HEPES, pH 7.25, 150 mM NaCl, 0.01% NP40, 5% glycerol) and 30 µl volume serially diluted into prechilled 384-well low-flange black, flat-bottom nonbinding microplate (Corning) while on ice. A 5-µl amount of 35 nM fluorescent peptide dissolved in binding buffer was added to each well (final concentration 5 nM) and mixed five times by pipetting, and plates were incubated at 4°C for 40 min. Fluorescence polarization experiments were performed with an Analyst AD (Molecular Devices, Sunnyvale, CA) spectrofluorimeter. Each well was excited using 485-nm light, and emission was read at 530 nm. Fluorescence polarization was measured 1 mm from the bottom of each well with an integration time of 560 ms. All experiments were conducted in triplicate. The change in fluorescence polarization was normalized such that maximum change for each condition was set at an arbitrary value of 100 for the ease of comparison. Normalized values were graphed and fit to a single-binding-site hyperbola using GraphPad Prism.

Rosenberg B.J., Gil-Henn H., Mader C.C., Halo T., Yin T., Condeelis J., Machida K., Wu Y.I, & Koleske A.J. (2017). Phosphorylated cortactin recruits Vav2 guanine nucleotide exchange factor to activate Rac3 and promote invadopodial function in invasive breast cancer cells. Molecular Biology of the Cell, 28(10), 1347-1360.

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