Typhoon trio scanner

Manufactured by GE Healthcare

Sourced in United States, Germany

The Typhoon Trio scanner is a versatile laboratory instrument designed for high-performance imaging and analysis of various biological samples. Its core function is to capture and analyze fluorescent and chemiluminescent signals from gels, blots, and microarrays with high sensitivity and resolution.

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Lab products found in correlation

Diamond nucleic acid dye, by Promega (4 mentions) Alexa fluor 647, by Thermo Fisher Scientific (4 mentions) Penta his antibody, by Qiagen (3 mentions) Instantblue coomassie, by Abcam (3 mentions) Storage phosphor screen, by GE Healthcare (3 mentions) Hybond n membrane, by GE Healthcare (3 mentions) Rediprime 2 kit, by GE Healthcare (3 mentions) Imagequant software, by GE Healthcare (3 mentions) Sybr gold, by Thermo Fisher Scientific (3 mentions) Molecular probes fluorescence based emsa kit, by Thermo Fisher Scientific (2 mentions) Nitrocellulose membrane, by GE Healthcare (2 mentions) T per buffer, by Thermo Fisher Scientific (2 mentions) Phenyl methyl sulfonyl fluoride (pmsf), by Merck Group (2 mentions) Bca assay, by Bio-Rad (2 mentions) Protease inhibitor cocktail, by Merck Group (2 mentions) Phosphorimager screen, by GE Healthcare (2 mentions) Pei cellulose f thin layer chromatography plate, by Merck Group (2 mentions) Decyder 2 d differential analysis software 6, by GE Healthcare (2 mentions) Nitrocellulose membrane, by Bio-Rad (2 mentions) Sypro ruby, by Thermo Fisher Scientific (2 mentions)

Spelling variants of this product

Typhoon Trio (260 citations) Typhoon scanner (254 citations) Typhoon-Trio laser scanner (5 citations) Typhoon TRIO fluorescence scanner (5 citations) Trio scanner (4 citations) Typhoon Trio multipurpose scanner (3 citations) Typhoon Trio gel scanner (3 citations) Scanners (2 citations) Typhoon Trio plus scanner (2 citations) Typhoon Trio high performance fluorescence scanner (2 citations)

84 protocols using typhoon trio scanner

Electrophoretic Mobility Shift Assay of MucR Protein Binding

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EMSA experiments were carried out as previously reported [59 (link)].
Briefly, several amounts of the recombinant MucR purified from E. coli Bl21 (DE3) and of the naturally expressed MucR from S. meliloti 1021 were mixed with the DNA target sites tested in binding buffer (25 mM HEPES pH 7.9, 50 mM KCl, 6.25 mM MgCl₂, 5% glycerol). Samples were incubated 10 min on ice and loaded in a 5% polyacrylamide gel. Electrophoresis was performed in 0.5× TBE and run at room temperature for 70 min at 200 V. Gels were stained for 20 min using Diamond™ Nucleic Acid Dye (Promega, Singapore) following the manufacturer’s instructions and imaged by Typhoon Trio+ scanner (GE Healthcare, Chicago, IL, USA).
For competition assays, competitors were added to the reaction mixture, prepared as described above, after proteins were incubated 10 min on ice with the FAM-labeled double-stranded oligonucleotides. After adding the competitors, samples were incubated for a further 10 min on ice and then loaded in a 5% polyacrylamide gel. Images were acquired by Typhoon Trio+ scanner (GE Healthcare) on the base of the FAM-labeled DNA fluorescence.
Protein amounts used, sequences, and amounts of double-stranded DNA targets are indicated in figures and figure legends.

Slapakova M., Sgambati D., Pirone L., Russo V., D’Abrosca G., Valletta M., Russo R., Chambery A., Malgieri G., Pedone E.M., Dame R.T., Pedone P.V, & Baglivo I. (2023). MucR from Sinorhizobium meliloti: New Insights into Its DNA Targets and Its Ability to Oligomerize. International Journal of Molecular Sciences, 24(19), 14702.

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Electrophoretic Mobility Shift Assay for Protein-DNA Binding

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The electrophoretic mobility shift assay (EMSA) experiments were carried out as previously described [28 (link)]. In detail, protein amounts from 0.2 up to 1.6 μg were incubated for 10 min on ice with 5 pmol of the double-stranded oligonucleotides in binding buffer (25 mM HEPES pH 7.9, 50 mM KCl, 6.25 mM MgCl2, 5% glycerol). The reaction mixture of 20 μL was loaded onto a 5% polyacrylamide gel in 0.5X TBE and run at room temperature for 75 min at 200 V. Gels were then stained for 20 min with Diamond™ Nucleic Acid Dye (Promega), rinsed with milliQ water and imaged by Typhoon Trio+ scanner (GE Healthcare). In particular, the amount of MucR used in the EMSAs with babR60 was 0.2, 0.4 and 0.8 μg. In the EMSAs with all the other double-stranded oligonucleotides tested, the amount of MucR used was 0.4, 0.8 and 1.6 μg.
For competition assays, 5 pmol of the FAM-labeled double-stranded babR60 was used as a probe incubated for 10 min on ice with 0.4 μg of MucR. Then, 10X, 20X or 40X of each competitor was added and the reaction mixtures were incubated on ice for another 10 min. The electrophoreses were carried out as already describe above and the fluorescent signals were imaged by Typhoon Trio+ scanner (GE Healthcare).

Borriello G., Russo V., Paradiso R., Riccardi M.G., Criscuolo D., Verde G., Marasco R., Pedone P.V., Galiero G, & Baglivo I. (2020). Different Impacts of MucR Binding to the babR and virB Promoters on Gene Expression in Brucella abortus 2308. Biomolecules, 10(5), 788.

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Chaperone Interaction Profiling with Peptide Microarrays

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Peptide microarrays containing FapC and CsgA sequences were used to probe the interaction of each chaperone with FapC/CsgA. The array contained immobilized 14-residue peptides^{75 (link)} from the FapC/CsgA sequence, each peptide spot displaced forward by 10 residues compared to the preceding peptide (i.e. 4 residues of overlap). Chaperones S100A9, CsgC, DnaJ (wt) and DnaJ-F91L were labeled with Alexa Fluor 546 (A546; Thermo-Fisher, Waltham, MA) and Bri2 monomer was labelled with Fluidiphore 503 dye according to the manufacturer's protocols (Fluidic Analytics, Cambridge UK). Free A546 was separated using PD-10 desalting column (GE Life Sciences), while free Fluidiphore 503 was removed by centrifugation (13 000 rpm, 10 min). The microarray was first blocked with TRIS saline buffer containing 0.1% Tween-20 (TSB-T) and 3% (w/v) whey protein at 4 °C overnight, washed three times with TSB-T and incubated with 0.05 mg ml⁻¹ of labelled chaperones for 4 hours at room temperature. After three times washing of the microarray with TSB-T, the arrays were air-dried in the dark and scanned using a Typhoon Trio scanner (GE Life Sciences, Pittsburgh, PA). Spot intensities were quantified using ImageJ.

Nagaraj M., Najarzadeh Z., Pansieri J., Biverstål H., Musteikyte G., Smirnovas V., Matthews S., Emanuelsson C., Johansson J., Buxbaum J.N., Morozova-Roche L, & Otzen D.E. (2021). Chaperones mainly suppress primary nucleation during formation of functional amyloid required for bacterial biofilm formation. Chemical Science, 13(2), 536-553.

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Non-denaturing Protein Isolation

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Total soluble protein was isolated under non-denaturing conditions using the standard extraction protocol described above with the following modifications. DTT was omitted from the lysis buffer, the final SDS concentration was decreased to 1% in the sample buffer, the protein samples were directly loaded onto the PAA gel without prior incubation at 95°C, and the electrophoretic separation was performed at 4 °C. The gels were scanned with a Typhoon^™ Trio⁺ scanner (GE Healthcare) using green laser light for excitation and the 526 SP emission filter.

Barahimipour R., Strenkert D., Neupert J., Schroda M., Merchant S.S, & Bock R. (2015). Dissecting the contributions of GC content and codon usage to gene expression in the model alga Chlamydomonas reinhardtii. The Plant journal : for cell and molecular biology, 84(4), 704-717.

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Annealing and Analysis of Fluorescent Conjugates

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The annealing was performed in annealing buffer (200 mM KOAc and 2 mM EDTA in nuclease-free H₂O). The conjugate solution (10 μL, 6.3 μM in nuclease-free H₂O, 63 pmol) was mixed with annealing buffer (20 μL) and heated in an Eppendorf tube to 55°C for 2 min. Concurrently, the complementary strand dissolved in nuclease-free water (10 μL, 6.3 μM in nuclease-free H₂O, 63 pmol) was heated for 2 min to 95°C and cooled down to 55°C. The complementary strand solution was transferred to the conjugate solution at 55°C and the heater was switched off and shaken in a thermoshaker with 650 rpm. After ∼60 min, the solutions were at RT and shaken overnight. The solutions were directly analyzed using urea gel electrophoresis. Directly after gel electrophoresis, the gels were scanned for the Atto488 fluorophore using a Typhoon Trio+ scanner (GE Healthcare Life Sciences) with a blue laser (488 nm) and a 526-nm band-pass filter. Afterward, the gel was stained using standard Coomassie staining. After destaining, the gel was washed with TBE buffer three times to remove acetic acid and methanol from the gel. SYBR gold staining was performed according to the manufacturer’s protocol. The Typhoon Trio+ scanner was used to scan for Coomassie staining without filter and excitation at 633 nm (red laser) as well as SYBR gold staining using a blue laser (488 nm) and a 555-nm band-pass filter.

Kuhlmann M., Hamming J.B., Voldum A., Tsakiridou G., Larsen M.T., Schmøkel J.S., Sohn E., Bienk K., Schaffert D., Sørensen E.S., Wengel J., Dupont D.M, & Howard K.A. (2017). An Albumin-Oligonucleotide Assembly for Potential Combinatorial Drug Delivery and Half-Life Extension Applications. Molecular Therapy. Nucleic Acids, 9, 284-293.

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DNA-Protein Binding Kinetics Assay

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Promoter regions of genes of interest were amplified with FAM-labeled primers (Table S1) and extracted from a 1% agarose gel to examine the specific binding with purified His₆-LrhA over a range of concentrations. Twenty µl reactions with purified His₆-LrhA, 5 nM FAM-DNA in 1X EMSA buffer (10% glycerol, 1 mM MgCl₂, 0.5 mM EDTA, 0.5 mM DTT, 50 mM NaCl, 10 mM Tris–HCl, 50 µg/ml poly (dI-dC) and 150 µg/ml BSA) were incubated at room temperature for 1 h before loading on to 1 × TBE (10.8 g/l Tris–HCl, 5.5 g/l boric acid, 2 mM EDTA, pH 8.0) 4%, 5%, or 6% acrylamide native gels followed by electrophoresis at 80 V for 2–3 h. Images were visualized on a Typhoon Trio Scanner (GE Healthcare). Experiments were done in duplicate.

Duong D.A, & Stevens A.M. (2017). Integrated downstream regulation by the quorum-sensing controlled transcription factors LrhA and RcsA impacts phenotypic outputs associated with virulence in the phytopathogen Pantoea stewartii subsp. stewartii. PeerJ, 5, e4145.

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Protein Separation and Identification by LC-MS/MS

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For LC–MS/MS analysis, protein samples were boiled for 5 min and resolved in 12.5% acrylamide gels, using a Mini-Protean II electrophoresis cell (Bio-Rad). A constant voltage of 150 V was applied for 45 min. Gels were fixed in a solution containing 10% acetic acid and 40% ethanol for 30 min and stained overnight in Sypro Ruby (Bio-Rad). Gels were then washed in a solution containing 10% ethanol and 7% acetic acid for 30 min, and the image was acquired using a Typhoon Trio scanner (GE Healthcare). Each lane was cut in slices and subjected to tryptic digestion, followed by LC–MS/MS analysis.

Hermanova I., Zúñiga-García P., Caro-Maldonado A., Fernandez-Ruiz S., Salvador F., Martín-Martín N., Zabala-Letona A., Nuñez-Olle M., Torrano V., Camacho L., Lizcano J.M., Talamillo A., Carreira S., Gurel B., Cortazar A.R., Guiu M., López J.I., Martinez-Romero A., Astobiza I., Valcarcel-Jimenez L., Lorente M., Arruabarrena-Aristorena A., Velasco G., Gomez-Muñoz A., Suárez-Cabrera C., Lodewijk I., Flores J.M., Sutherland J.D., Barrio R., de Bono J.S., Paramio J.M., Trka J., Graupera M., Gomis R.R, & Carracedo A. (2020). Genetic manipulation of LKB1 elicits lethal metastatic prostate cancer. The Journal of Experimental Medicine, 217(6), e20191787.

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Quantitative Protein Analysis via SYPRO Staining

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After electrophoresis, gels were fixed for 30 min in SYPRO fixer solution (40% (v/v) methanol, 10% (v/v) acetic acid in milliQ) followed by overnight staining with SYPRO Ruby fluorescent dye stain (ThermoFisher Scientific) on a shaker at room temperature. The following day, gels were destained (7.5% acetic acid, 20% methanol in milliQ) for 30 min and scanned using Typhoon Trio scanner (GE Healthcare). ImageQuant software (GE Healthcare) was used for the quantification of images by densitometry analysis using Benchmark ladder (ThermoFisher Scientific) as a protein standard.

Mackenzie K., Foot N.J., Anand S., Dalton H.E., Chaudhary N., Collins B.M., Mathivanan S, & Kumar S. (2016). Regulation of the divalent metal ion transporter via membrane budding. Cell Discovery, 2, 16011-.

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Analyzing DNA Structures via Agarose Gel

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Annealed DNA structures were directly loaded on 1.5% agarose gel (if not otherwise indicated) and allowed to migrate for 3 h at 4 °C (running buffer: 1X TBE, 10 mM MgCl₂; running voltage: 80 V). The gel was stained with SybrGold (Life Technologies) and visualised with Typhoon Trio scanner (GE Healthcare Life Sciences).

Grossi G., Dalgaard Ebbesen Jepsen M., Kjems J, & Andersen E.S. (2017). Control of enzyme reactions by a reconfigurable DNA nanovault. Nature Communications, 8, 992.

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Quantification of Protein Abundance via SYPRO Ruby Staining

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The SYPRO Ruby staining method was used to quantify protein amounts. Proteins were separated using SDS-PAGE, and Benchmark ladder (Life Technologies) was used as a protein standard for the following quantifications. The SDS-PAGE gels were immersed in fixation solution (40% (v/v) methanol, 10% (v/v) acetic acid) for 30 min with shaking. Gels were kept overnight in SYPRO Ruby fluorescent dye stain (Molecular Probes) and were then washed with destain solution (7.5% (v/v) acetic acid, 20% (v/v) methanol) for 30 min. Fluorescent signals were visualized using Typhoon Trio™ scanner (GE Healthcare) or Typhoon™ FLA 7000 scanner (GE Healthcare). Protein amounts were quantified by densitometric analysis with ImageQuant™ software (GE Healthcare).

Zhao K., Bleackley M., Chisanga D., Gangoda L., Fonseka P., Liem M., Kalra H., Al Saffar H., Keerthikumar S., Ang C.S., Adda C.G., Jiang L., Yap K., Poon I.K., Lock P., Bulone V., Anderson M, & Mathivanan S. (2019). Extracellular vesicles secreted by Saccharomyces cerevisiae are involved in cell wall remodelling. Communications Biology, 2, 305.

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