Typhoon trio

Manufactured by GE Healthcare

Sourced in United States, United Kingdom, Sweden

The Typhoon Trio is a versatile fluorescence and phosphor imaging system designed for a wide range of life science applications. It offers high-resolution imaging, multiple excitation sources, and flexible detection capabilities to support various experimental needs.

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Lab products found in correlation

Imagequant software, by GE Healthcare (20 mentions) γ 32p atp, by PerkinElmer (9 mentions) Decyder software, by GE Healthcare (8 mentions) Imagequant tl, by GE Healthcare (8 mentions) Imagequant tl software, by GE Healthcare (8 mentions) T4 polynucleotide kinase, by New England Biolabs (7 mentions) Imagequant, by GE Healthcare (6 mentions) Superscript 3 reverse transcriptase, by Thermo Fisher Scientific (4 mentions) Targetamp 1 round aminoallyl arna amplification kit, by Illumina (3 mentions) Kaleidagraph, by Synergy Software (3 mentions) High purity dimethyl sulphoxide, by GE Healthcare (3 mentions) Decyder software version 6, by GE Healthcare (3 mentions) Benchmark protein standard, by Thermo Fisher Scientific (3 mentions) Imagequant analysis toolbox software, by GE Healthcare (3 mentions) Sypro ruby, by Thermo Fisher Scientific (3 mentions) Image studio lite software, by LI COR (3 mentions) Supersignal west pico plus, by Thermo Fisher Scientific (3 mentions) Hybond xl membrane, by Cytiva (3 mentions) Hybond xl, by GE Healthcare (3 mentions) Hybond p membrane, by GE Healthcare (3 mentions)

Close spelling variants of this product

Typhoon TRIO Imager System Typhoon Trio Plus phosphoimager Typhoon Trio Biomolecular Imager Typhoon Trio plus scanner Typhoon Trio equipment Typhoon Trio phosphoimager Typhoon 9600 trio+ Typhoon Trio phosphorimager Typhoon Trio Plus Imager Typhoon Trio screen

260 protocols using typhoon trio

Quantitative Analysis of RNaseH2-Mediated DNA Nicks

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The protocol is based on the one previously published (25 (link)) with further modifications and optimization (Maffia and Sabbioneda, manuscript in preparation). Specifically, genomic DNA was extracted using NucleoSpin^® Tissue kit (Macherey-Nagel, Düren, Germany). Then, 1 μg of genomic DNA was digested with 1 U of E. coli RNaseH2 (BioLabs, Euroclone) or with 50 nM human recombinant RNaseH2 and the reaction was led in a dry heating block (Eppendorf^® Thermomixer^®) at 37°C with constant shaking at 550 rpm for 2.5 h. Reaction was stopped on ice for 30 min and nick translation reaction started trough the addition of 1 U of E. coli DNA pol I (Biolabs, Euroclone) and 2 μl of Atto647N-dUTP pH 7.5 NT Labelling Kit (Jena Biosciences, Löbstedter, Germany) at 16°C for 1 h.
Finally, the reaction was stopped by addition of standard gel loading buffer and loaded on a 1% agarose gel at 100 V for 2 h in TBE buffer. Ethidium bromide and Atto647N-dUTP signals were detected by laser scanning densitometry (Typhoon-TRIO, GE Healthcare) and quantified with ImageQuant TL (Typhoon-TRIO, GE Healthcare) normalizing Atto647N-dUTP signals with the Ethidium bromide ones. Quantitation of undigested genomic DNAs were subtracted from quantitation of digested genomic DNAs and P values were calculated using the Student's t-test.

Riva V., Garbelli A., Casiraghi F., Arena F., Trivisani C.I., Gagliardi A., Bini L., Schroeder M., Maffia A., Sabbioneda S, & Maga G. (2020). Novel alternative ribonucleotide excision repair pathways in human cells by DDX3X and specialized DNA polymerases. Nucleic Acids Research, 48(20), 11551-11565.

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Proteasome Activity Profiling using BODIPY-epoxomicin

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Proteasome subunits were labeled in the lysate with 0.5 μM activity-based probe BODIPY-epoxomicin for 1 h at 37 °C (BodipyFl-Ahx3L3VS, MV121, provided by H. Overkleeft, Institute of Chemistry, Leiden, The Netherlands) [60] (link) and sample buffer (350 mM Tris-HCl pH 6.8, 10% SDS, 30% glycerol, 6% β-mercaptoethanol, 0.02% bromophenol blue), added to 20 µg protein lysate. Samples were boiled for 5 min and loaded on a 12.5% SDS-PAGE gel. As a positive control, maximal proteasome activity was determined after treatment with IFNγ (50 U). After running the proteins on the gel, fluorescence imaging was performed on a Trio Typhoon (GE Medical Systems, Little Chalfont, UK) using the 580 bandpass filter to detect the probe directly on the gel. Proteasome total activity values were normalized according to the total proteasome content in cells as indicated by the levels of the α7 subunit of the 20S proteasome (1:1000; MCP72; Enzo Life Sciences, Zandhoven, Belgium). The experiment was performed in triplicate and repeated three times (N = 3).

Ramos de Carvalho J.E., Verwoert M.T., Vogels I.M., Reits E.A., Van Noorden C.J., Klaassen I, & Schlingemann R.O. (2018). Involvement of the ubiquitin-proteasome system in the expression of extracellular matrix genes in retinal pigment epithelial cells. Biochemistry and Biophysics Reports, 13, 83-92.

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Proteasome Modulation by Curcumin Compounds

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We investigated the potential role of nano-curcumin and curcumin as proteasome-modulating agents in RPE cells. Proteasome catalytic subunits β 2 , β 5i /β 1 , and β 5 /β 1i were labeled in lysates of ARPE-19 cells treated with nano-curcumin or curcumin (5, 50, or 100 μM) with a 0.5 μM activity-based probe BODIPY-epoxomicin for 1 h at 37 ° C (BodipyFl-Ahx3L3VS, MV121, provided by Prof. Dr. H. Overkleeft, Institute of Chemistry, Leiden, The Netherlands) [36] . Sample buffer (350 mM Tris-HCl pH 6.8, 10% SDS, 30% glycerol, 6% β-mercaptoethanol, 0.02% bromophenol blue) was added to 20 µg of protein lysate. The samples were boiled for 5 min and loaded on a 12.5% SDS-PAGE gel. After running the proteins on the gel, fluorescence imaging was performed using a Trio Typhoon (GE Medical Systems, Little Chalfont, UK) and a 580 bandpass filter to detect the probe directly on the gel. Proteasome total activity values were normalized on the basis of the total proteasome content in cells as indicated by the levels of the α 7 subunit of the 20S proteasome (1: 1,000; MCP72; Enzo Life Sciences).

Ramos de Carvalho J.E., Verwoert M.T., Vogels I.M.C., Schipper-Krom S., Van Noorden C.J.F., Reits E.A., Klaassen I, & Schlingemann R.O. (2018). Modulation of the Proteasome Pathway by Nano-Curcumin and Curcumin in Retinal Pigment Epithelial Cells. Ophthalmic research, 59(2).

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Lentiviral Transduction for DYRK1A Downregulation

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Lentiviral transduction of short hairpin (sh)RNAs was used to downregulate DYRK1A expression, and the generation of the lentiviral stocks and the infection conditions are detailed in the Supplementary Methods. The protocols to determine the cell cycle profile and cell volume are also included in the Supplementary Methods. To analyze global protein synthesis, T98G cells were incubated for 90 min in methionine-free Dulbecco’s modified Eagle’s medium (DMEM; GIBCO, Waltham, MA, USA) with 10% dialyzed fetal bovine serum (FBS; GIBCO), metabolically labeled for 20 min with ³⁵S-Met (50 μCi ³⁵S-Met, 1175 Ci/mmol, Perkin Elmer) and then lysed in SDS lysis buffer. The protein extracts were resolved by SDS-PAGE and the incorporation of ³⁵S-methionine was detected by the autoradiography of the dried gel using film or a Phosphoimager (Typhoon Trio, GE Healthcare, Chicago, IL, USA).

Di Vona C., Barba L., Ferrari R, & de la Luna S. (2023). Loss of the DYRK1A Protein Kinase Results in the Reduction in Ribosomal Protein Gene Expression, Ribosome Mass and Reduced Translation. Biomolecules, 14(1), 31.

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Protein Detection via SDS-PAGE and Western Blot

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Where described, protein samples were labeled with lightning red (Serva) diluted 1:50 in protein sample buffer and then separated on anyKD (Biorad) or 12.5% SDS-PAGE gels. Subsequently, total protein staining was analyzed using a Typhoon trio (GE Healthcare). After transfer to PVDF membranes (Carl Roth), membranes were blocked with 5% skimmed milk/TBST, incubated with primary antibodies overnight at 4 °C, followed by washing with TBST and incubation with HRP-conjugated second step antibodies for one hour. Luminescence was detected using ECL reagent and x-ray films (GE Healthcare). Films were scanned and where mentioned, densitometric quantification was performed using ImageJ.

Zingler P., Särchen V., Glatter T., Caning L., Saggau C., Kathayat R.S., Dickinson B.C., Adam D., Schneider-Brachert W., Schütze S, & Fritsch J. (2019). Palmitoylation is required for TNF-R1 signaling. Cell Communication and Signaling : CCS, 17, 90.

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RNA Expression Analysis by Northern Blot

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RNA was isolated using Trizol (Life Technologies) and resolved on formaldehyde/agarose gels. ³²P-labeled in vitro transcribed probes against β-globin or random-primed DNA probes against GFP were used for detection of mRNAs. Northern blots were imaged on Storm or Typhoon Trio scanners and quantification was performed using ImageQuant software (GE Healthcare, Pittsburgh, PA).

Ge Z., Quek B.L., Beemon K.L, & Hogg J.R. (2016). Polypyrimidine tract binding protein 1 protects mRNAs from recognition by the nonsense-mediated mRNA decay pathway. eLife, 5, e11155.

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Quantifying Cathepsin Activity in Neuroblastoma Cells

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SH-SY5Y and SK-N-BE2 neuroblastoma cells were seeded in equal density in 6-well plates. When cells reached 80% confluency, 0.1 μM BMV109 pan cathepsin activity-based probe [51 (link)] was added to the cell and incubated for 1 h. Following incubation cells were washed thrice with PBS. Cells were then harvested by scraping and lysed for analysis. Lysis buffer consisted of 50 mM citrate, pH 5.5, 0.5% CHAPS, 0.1% Triton X-100 and 4 mM DTT. The lysates were quantified using BCA assay and equal amount of sample (30 μg) was analysed on a gel. For cathepsin analysis, 30 μg of total protein from each secretome sample was taken and BMV109 probe (0.1 μM) was added to each sample and incubated at 37°C for 1 h. At the end of the incubation, SDS sample loading buffer was added to each sample and analysed on a gel. The Cy5 fluorescence of the probe was detected by scanning the gels under the Typhoon Trio (GE Healthcare) scanner. The gels was then transferred to a nitrocellulose membrane and probed with antibodies against Cathepsin isoforms B and L (R&D AF1515 and AF965 antibodies, respectively). The specificity of the probe was tested by growing cells in the presence of the cysteine cathepsin inhibitor JPM (100 μM) for 24 h and then incubating with the probe.

Gangoda L., Keerthikumar S., Fonseka P., Edgington L.E., Ang C.S., Ozcitti C., Bogyo M., Parker B.S, & Mathivanan S. (2015). Inhibition of cathepsin proteases attenuates migration and sensitizes aggressive N-Myc amplified human neuroblastoma cells to doxorubicin. Oncotarget, 6(13), 11175-11190.

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Radioactive Fatty Acid Labeling

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Cells were seeded in tissue culture dishes as described above. For labelling, the cells were starved using IM medium (Glasgow minimal essential medium buffered with 10 mM Hepes, pH 7.4). After 1 h, the medium was replaced by IM with 3H-palmitate at 200 µCi/mL (American Radiolabeled Chemicals, US) for 2 h at 37 °C. Cell lysis, immunoprecipitation and SDS-PAGE were performed as above. The gels were fixed for 30 min with 10% acetic acid, 25% isopropanol in water and the signal was amplified for 30 min with NAMP100 (GE Healthcare, US). The gels were then dried and applied to an Amersham Hyperfilm MP (GE Healthcare, US). The radioactivity was visualized and quantify using a Typhoon TRIO (GE Healthcare, US).

Sandoz P.A., Denhardt-Eriksson R.A., Abrami L., Abriata L.A., Spreemann G., Maclachlan C., Ho S., Kunz B., Hess K., Knott G., S. Mesquita F., Hatzimanikatis V, & van der Goot F.G. (2023). Dynamics of CLIMP-63 S-acylation control ER morphology. Nature Communications, 14, 264.

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SDS-PAGE Analysis of Conjugated Proteins

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Gel electrophoresis of the conjugated proteins was performed on a 4% stacking gel and 14% acrylamide/bisacrylamide (37.5:1) resolving gel. Gels were 1.5 mm thick and casted following a specific protocol (Table 2). The migration was done using the Mini-PROTEAN® system (Biorad, Hercules, CA, USA) and performed at a constant rate of 60 mA, 2 h in 1X running buffer (Table 2). Gel readings were done using a Typhoon Trio+ (GE Healthcare, Little Chalfont, Buckinghamshire, United Kingdom). The detection of CyDyes 3 and 5 was done at the optimal photomultiplier voltage (PMT) for each one of them, for each gel analyzed.

Paré B., Deschênes L.T., Pouliot R., Dupré N, & Gros-Louis F. (2016). An Optimized Approach to Recover Secreted Proteins from Fibroblast Conditioned-Media for Secretomic Analysis. Frontiers in Cellular Neuroscience, 10, 70.

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Quantitative Protein Expression Analysis

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Immediately after SDS-PAGE, gel images were scanned using Typhoon TRIO (GE Healthcare, Waukesha, WI). The images were analyzed by Image Quant software (version 6.0, GE Healthcare, Waukesha, WI), and quantitation analysis was done with DeCyder software (version 6.5, GE Healthcare, Waukesha, WI). In-gel DeCyder analysis was used to obtain the fold change of protein expression levels.

Qin E.Y., Cooper D.D., Abbott K.L., Lennon J., Nagaraja S., Mackay A., Jones C., Vogel H., Jackson P.K, & Monje M. (2017). Neural precursor-derived pleiotrophin mediates subventricular zone invasion by glioma. Cell, 170(5), 845-859.e19.

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