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Typhoon fla 9000 system

Manufactured by GE Healthcare
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The Typhoon FLA 9000 system is a multi-function fluorescence and chemiluminescence imaging system designed for high-performance imaging and analysis of various biological samples, including gels, blots, and microplates. The system utilizes a unique laser-based scanning technology to capture high-quality images with exceptional sensitivity and resolution.

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Lab products found in correlation

Urea loading dye, by Thermo Fisher Scientific (1 mentions) Protein kinase buffer, by Merck Group (1 mentions) Atpγ32p, by Hartmann Analytic (1 mentions) Storage phosphor screen, by GE Healthcare (1 mentions) Adenosine triphosphate (atp), by Merck Group (1 mentions) Cdk1 cyclin b1, by Sino Biological (1 mentions) Aurora b, by Sino Biological (1 mentions) Aurora a, by Sino Biological (1 mentions)

Spelling variants of this product

Typhoon FLA 9000 (180 citations) Typhoon system (16 citations) Typhoon 9000 (9 citations) Typhoon FLA 9000 imaging system (8 citations) Typhoon FLA 9000 PhosphorImaging system (4 citations) Molecular Dynamics Typhoon FLA 9000 system (2 citations)

4 protocols using typhoon fla 9000 system

1

Aortic Plaque Lipid Quantification

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Oil-Red-O staining depicted the distribution of plaques in ApoE−/− aortae that were subsequently photographed by a digital flatbed scanner and analysed by digital autoradiography. Aortae were exposed to a phosphor imager plate and read with a Typhoon FLA9000 system (GE Healthcare) 12 h later. To stain for lipid contents in atherosclerosis, aortae were briefly incubated in 60% 2-propanol and stained with 0.5% Oil-Red-O solution for 15 min at room temperature. After rinsing in 60% 2-propanol, aortae were washed repeatedly in PBS. Scanned autoradiography images were visualized using the ImageJ program (1.440).
Keliher E.J., Ye Y.X., Wojtkiewicz G.R., Aguirre A.D., Tricot B., Senders M.L., Groenen H., Fay F., Perez-Medina C., Calcagno C., Carlucci G., Reiner T., Sun Y., Courties G., Iwamoto Y., Kim H.Y., Wang C., Chen J.W., Swirski F.K., Wey H.Y., Hooker J., Fayad Z.A., Mulder W.J., Weissleder R, & Nahrendorf M. (2017). Polyglucose nanoparticles with renal elimination and macrophage avidity facilitate PET imaging in ischaemic heart disease. Nature Communications, 8, 14064.
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2

RNA Degradation by PNPase Variants

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For the RNA degradation experiments, PNPase proteins (10 nM)—including PNPase-CHis, PNPase-NHis, PNPase-Q387R and PNPase-E475G—were incubated with a 37-nt fluorescein-labeled ssRNA with a sequence of 5′-FAM-C7U30-3′ (10 nM, purchased from Dharmacon) at 37°C for 0–60 min in a reaction buffer containing 20 mM Tris–HCl (pH 7.5), 100 mM NaCl, 1 mM DTT, 2 mM NaH2PO4 and 0.25 mM MgCl2. The RNA degradation reactions were stopped by adding 2× urea loading dye (Thermo) at different time-points (0, 15, 30, 45 and 60 min) and heating at 90°C for 3 min. Samples were then loaded on a 20% TBE–urea polyacrylamide denaturing gel for electrophoresis, which was scanned with a Typhoon FLA 9000 system (GE Healthcare).
Golzarroshan B., Lin C.L., Li C.L., Yang W.Z., Chu L.Y., Agrawal S, & Yuan H.S. (2018). Crystal structure of dimeric human PNPase reveals why disease-linked mutants suffer from low RNA import and degradation activities. Nucleic Acids Research, 46(16), 8630-8640.
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3

Radiolabeling and Immunoprecipitation of Trypanosomes

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Pulse-chase radiolabeling of log-phase cultured BSF trypanosomes with [35S]methionine/cysteine, and subsequent immunoprecipitation of labeled polypeptides were performed as described previously (Tazeh et al., 2007 (link), Peck et al., 2008 (link)). Pulse and chase times are indicated in the figure legends. All immunoprecipitates were fractionated by 12% SDS-PAGE, and gels were analyzed by phosphorimaging using a Molecular Dynamics Typhoon FLA 9000 system with native ImageQuant Software (GE Healthcare, Piscataway, NJ).
Tiengwe C., Muratore K.A, & Bangs J.D. (2016). Variant Surface Glycoprotein, Transferrin Receptor, and ERAD in Trypanosoma brucei. Cellular microbiology, 18(11), 1673-1688.
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4

In Vitro Phosphorylation Assay

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Around 0.5 μg of recombinant FLAG‐CUL4A or FLAG‐CUL4B (in complex with DDB1 and RBX1) or 0.15 μg native swine myelin basic protein (MBP; SignalChem) were added to 1× protein kinase buffer (NEB) supplemented with 200 μM “cold” ATP (Sigma) and 500 μCi/μmol ATPγ32P (Hartmann Analytic). The reaction was initiated by the addition of 10 U (pmol/min) of recombinant CK1 (NEB), CDK1‐cyclin B1 (NEB), PLK1 (SignalChem), Aurora A (SignalChem) or Aurora B (SignalChem) kinases, incubated for 1 h at 30°C. Samples were boiled in 1× Laemmli buffer and subjected to SDS–PAGE. Gels were stained with InstantBlue Coomassie stain (Expedeon Protein Solutions), vacuum‐dried for 30 min, and exposed overnight to a storage phosphor screen (GE Healthcare). Screens were scanned in a Typhoon FLA 9000 system (GE Healthcare).
Stier A., Gilberto S., Mohamed W.I., Royall L.N., Helenius J., Mikicic I., Sajic T., Beli P., Müller D.J., Jessberger S, & Peter M. (2023). The CUL4B‐based E3 ubiquitin ligase regulates mitosis and brain development by recruiting phospho‐specific DCAFs. The EMBO Journal, 42(17), e112847.
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