Typhoon fla 7000 scanner

Manufactured by GE Healthcare

Sourced in United States

The Typhoon FLA 7000 scanner is a versatile laboratory equipment designed for the detection and analysis of fluorescent and chemiluminescent signals in various applications, such as protein and nucleic acid gels, Western blots, and microarrays. The scanner utilizes high-sensitivity photomultiplier tubes and advanced optics to provide accurate and reliable results.

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Lab products found in correlation

Imagequant tl software, by GE Healthcare (3 mentions) Nupage 4 12 bis tris protein gel, by Thermo Fisher Scientific (3 mentions) Rapid hyb buffer, by Cytiva (2 mentions) Hybond xl nylon membrane, by GE Healthcare (2 mentions) Biometra eco maxi system, by Analytik Jena (2 mentions) Endoglycosidase h, by Roche (2 mentions) 5 fam labeled single stranded dna ssdna oligonucleotides, by Integrated DNA Technologies (2 mentions) Emetine dihydrochloride hydrate, by Merck Group (2 mentions) Typhoon trio scanner, by GE Healthcare (1 mentions) Imagequant software, by GE Healthcare (1 mentions) Benchmark ladder, by Thermo Fisher Scientific (1 mentions) Td 20 20 luminometer, by Promega (1 mentions) Las 3000 device, by Fujifilm (1 mentions) Renilla luciferase assay system, by Promega (1 mentions) Mini protean tgx precast gel, by Bio-Rad (1 mentions) Tween 20 tbst, by Merck Group (1 mentions) Mirax slide scanner, by Zeiss (1 mentions) Oct medium, by Thermo Fisher Scientific (1 mentions) Pannoramic viewer, by 3DHISTECH (1 mentions) Nanodrop one, by Thermo Fisher Scientific (1 mentions)

41 protocols using typhoon fla 7000 scanner

Cellular Uptake Kinetics of Cy3-Labeled SPOT-ONs

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For U2OS cells, Cy3 3′-labeled SPOT-ONs were added respectively to DMEM media supplemented with 10% FBS and incubated at 37 °C at different time points (0, 0.5, 1, 2, 3, 6, and 24 h; unmodified Poly(A)₁₂-Cy3 samples at 0, 12, 24, 36, and 48 h) were run on 6% DNA retardation gel in 0.5X TBE buffer. The gel was imaged with a Typhoon FLA7000 scanner (GE Healthcare).

Barragán-Iglesias P., Lou T.F., Bhat V.D., Megat S., Burton M.D., Price T.J, & Campbell Z.T. (2018). Inhibition of Poly(A)-binding protein with a synthetic RNA mimic reduces pain sensitization in mice. Nature Communications, 9, 10.

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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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In Vitro [3H]VAT Brain Autoradiography

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To check the distribution of [³H]VAT in human and nonhuman primate brain tissues, in vitro autoradiography (ARG) study was performed using sections (12 μm) from frozen brain tissues. Brain sections were brought to room temperature for 30 min, and then pre-incubated with assay buffer (50 mM Tris-HCl buffer containing 150 mM NaCl and 1 mM EDTA at pH 7.4) for 15 min. Further, slides were incubated with 10 nM of [³H]VAT alone (for total binding), or with the addition of 10 μM of TZ6–59, a potent and selective VAChT ligand as a blocking agent (Liu et al., 2015 (link)) for 1 h at room temperature. Then these slides were washed with cold assay buffer for 2 min twice and finally rinsed in cold water. After these slides were dried overnight, they were exposed to X-ray film for 4 weeks before development, and then exposed to phosphor sensor plate for two weeks. Finally, the autoradiography signal was visualized on a Typhoon FLA 7000 scanner (GE), measured and quantified with Multi Gauge program.

Liang Q., Joshi S., Liu H., Yu Y., Zhao H., Benzinger T.L., Perlmutter J.S, & Tu Z. (2021). In vitro characterization of [3H]VAT in cells, animal and human brain tissues for vesicular acetylcholine transporter. European journal of pharmacology, 911, 174556.

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Protein Gel Electrophoresis and Viral RNA Analysis

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NuPAGE 4–12% Bis-Tris protein gel (Thermo Fisher Scientific, Waltham, MA, USA) was used for SDS-PAGE and Western blotting analyses. The chemiluminescence signals were detected using the LAS-3000 device (FUJIFILM, Tokyo, Japan). For detection of FLAG-tagged Met-IR and untagged full-length replication proteins of TMV, anti-DYKDDDDK antibody (clone 1E6; FUJIFILM Wako Pure Chemical, Osaka, Japan) and antisera against tomato mosaic virus replication proteins [8 (link)] were used, respectively. Luciferase activity was measured using the Renilla Luciferase Assay System (Promega) and the TD-20/20 luminometer (Promega). Radiolabeled RNA products were separated by 8 M urea–2.4% PAGE and detected using the Typhoon FLA 7000 scanner (GE Healthcare, Chicago, IL, USA). Band intensity of viral genomic RNA was quantified using ImageJ software (National Institutes of Health, Bethesda, MD, USA).

Yoshida T., Ishikawa M, & Ishibashi K. (2022). Inhibition of Cell-Free Translation and Replication of Tobacco Mosaic Virus RNA by Exogenously Added 5′-Proximal Fragments of the Genomic RNA. Viruses, 14(9), 1962.

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Western Blot Analysis of LPL in CHO Cells

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Extracellular CHO HCPs were precipitated with methanol as described previously (Valente et al., 2014 (link)) and resolubilized in phosphate buffered saline. Concentrations of resolubilized HCPs were measured using a Bradford assay. Two sets of 30 μg CHO HCPs were reduced by sodium dodecyl sulfate (SDS) and DTT before being separated on 4-20% Mini-PROTEAN TGX precast gel (Biorad Laboratories, Hercules, CA, USA). Proteins were then transferred to a 0.45 μm polyvinylidene difluoride membrane (Life Technologies). Membranes were blocked in 3% non-fat dry milk in Tris-buffered saline with TWEEN 20 (TBST, Sigma-Aldrich Chemical Co.) for 1 hour and probed overnight at 4 °C with LPL N-terminus primary antibody (1:500 dilution in 3% milk block), which recognizes LPL residues 27-79 (Santa Cruz Biotechnology, Dallas, TX, USA). A second membrane was probed overnight at 4 °C with LPL C-terminus primary antibody (1:250 dilution in 3% milk block), which recognizes LPL residues 297-326 (Abcam, Cambridge, UK). The membranes were then probed with alkaline phosphatase-conjugated mouse anti-rabbit IgG (1:5,000 dilution, Sigma-Aldrich Chemical Co.) for 45 minutes, detected using enhanced chemifluorescence (ECF, GE Healthcare Life Sciences) substrate following the manufacturer's instructions and imaged using a Typhoon FLA-7000 scanner (GE Healthcare Life Sciences).

Chiu J., Valente K.N., Levy N.E., Min L., Lenhoff A.M, & Lee K.H. (2016). Knockout of a difficult-to-remove CHO host cell protein, lipoprotein lipase, for improved polysorbate stability in monoclonal antibody formulations. Biotechnology and bioengineering, 114(5), 1006-1015.

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Soft Agar Colony Formation Assay

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To each well of a 6-well plate, 2 ml of 0.6% base low-melting point agarose was added. After the agarose was solidified, 1.0 × 10³ of HCT116 cells transduced with five different BZW2 shRNAs or a control shLuciferase were mixed with 0.3% low-melting point agarose and plated into a 6-well plate on top of the 0.6% base agarose layer. Then 150 μl of normal culture medium was added on top of the 0.3% low-melting point agarose. The medium was changed every 48 h. After 14 days of culture, colonies were stained with 200 μl of Nitro Blue Tetrazolium Chloride staining solution (2 mg/ml in water, filtered) overnight at 37 °C. Plates were imaged using a Typhoon FLA 7000 scanner (GE Healthcare).

Maio G., Smith M., Bhawal R., Zhang S., Baskin J.M., Li J, & Lin H. (2023). Interactome Analysis Identifies the Role of BZW2 in Promoting Endoplasmic Reticulum-Mitochondria Contact and Mitochondrial Metabolism. Molecular & Cellular Proteomics : MCP, 23(2), 100709.

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Brain Tissue Preparation and Imaging

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Mice were sacrificed immediately after imaging by CO₂ asphyxiation and cervical dislocation. Brains were dissected by removing the calvarium and gently dissecting the brain from the lower skull with the tip of a pair of forceps. Brains were embedded in OCT medium (Fisher Scientific, Houston, TX) on dry ice and sectioned at 10-μm thickness onto glass slides on a cryostatic microtome. Slides were placed into a cassette pressed against the pre-blanked storage phosphor plate, separated by a layer of plastic wrap, and the plate allowed to charge for ten half-lives at − 20 °C. The phosphor plate was read on a Typhoon FLA 7000 scanner (GE Healthcare, Port Washington, NY), and the slides were subjected to hematoxylin and eosin staining and scanned on a Mirax slide scanner (Carl Zeiss, Jena, Germany). Images were processed using Pannoramic Viewer (3DHISTECH Ltd., Budapest, Hungary) and the Fiji ImageJ distribution.

Donabedian P.L., Kossatz S., Engelbach J.A., Jannetti S.A., Carney B., Young R.J., Weber W.A., Garbow J.R, & Reiner T. (2018). Discriminating radiation injury from recurrent tumor with [18F]PARPi and amino acid PET in mouse models. EJNMMI Research, 8, 59.

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Northern Blotting for RNA Analysis

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Northern blotting was performed according to a previously published protocol (Miyakoshi et al., 2019 (link)). Briefly, total RNA was isolated using the TRIzol reagent (Invitrogen), treated with TURBO DNase (Invitrogen), and precipitated with cold ethanol. RNA was quantified using NanoDrop One (Invitrogen). Total RNA (5 µg) was separated by gel electrophoresis on 6% polyacrylamide/7 M urea gels in 1 × TBE buffer for 3 hr at 250 V using Biometra Eco‐Maxi system (Analytik‐Jena). DynaMarker RNA Low II ssRNA fragments (BioDynamics Laboratory) were used as a size marker. RNA was transferred from the gel onto Hybond‐XL nylon membrane (GE Healthcare) by electroblotting for 1 hr at 50 V using the same system. The membrane was crosslinked with transferred RNA by 120 mJ/cm² UV light, incubated for prehybridization in Rapid‐Hyb buffer (Amersham) at 42℃ for 1 hr, and then incubated for hybridization with a [³²P]‐labeled probe JVO‐0749 and JVO‐0322 at 42℃ overnight to detect GcvB and 5S rRNA, respectively. The membrane was washed in three 15‐min steps in 5× SSC/0.1% SDS, 1× SSC/0.1% SDS, and 0.5× SSC/0.1% SDS buffers at 42℃. Signals were visualized on Typhoon FLA7000 scanner (GE Healthcare) and quantified using Image Quant TL software (GE Healthcare).

Miyakoshi M., Okayama H., Lejars M., Kanda T., Tanaka Y., Itaya K., Okuno M., Itoh T., Iwai N, & Wachi M. (2021). Mining RNA‐seq data reveals the massive regulon of GcvB small RNA and its physiological significance in maintaining amino acid homeostasis in Escherichia coli. Molecular Microbiology, 117(1), 160-178.

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Northern Blot Analysis of Small RNAs

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2 µg of total RNA in RNA loading dye (NEB) was separated by gel electrophoresis on 6% polyacrylamide/7 M urea gels in 1xTBE buffer for 3 h at 250 V and was electroblotted onto Hybond-XL nylon membrane (GE Healthcare) for 1 h at 50 V using Biometra Eco-Maxi system (Analytik-Jena). The membrane was crosslinked by 120 mJ/cm² UV light. Oligonucleotides JVO-2624 and JVO-0485 to detect HPnc4160 and 5 S rRNA, respectively^{9 (link)}, were 5′-end-labeled with [³²P]-γ-ATP by T4 polynucleotide kinase (Nippon Gene) and purified over G25 columns (GE Healthcare). After prehybridization in Rapid-Hyb buffer (Amersham), the [³²P]-labeled probe was hybridized at 42 °C overnight. Membrane was washed in three steps in 5x SSC/0.1% SDS, 1x SSC/0.1% SDS and 0.5x SSC/0.1% SDS buffers for 15 min at 42 °C. Signals were visualized on Typhoon FLA7000 scanner (GE Healthcare).

Kinoshita-Daitoku R., Kiga K., Miyakoshi M., Otsubo R., Ogura Y., Sanada T., Bo Z., Phuoc T.V., Okano T., Iida T., Yokomori R., Kuroda E., Hirukawa S., Tanaka M., Sood A., Subsomwong P., Ashida H., Binh T.T., Nguyen L.T., Van K.V., Ho D.Q., Nakai K., Suzuki T., Yamaoka Y., Hayashi T, & Mimuro H. (2021). A bacterial small RNA regulates the adaptation of Helicobacter pylori to the host environment. Nature Communications, 12, 2085.

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Identifying gp160 Folding Intermediates

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To identify gp160 folding intermediates, glycans were removed from lysate-derived gp120 or gp160 with Endoglycosidase H (Roche) treatment of the immunoprecipitates as described before (Land et al., 2003 (link)). Samples were subjected to non-reducing and reducing (25 mM DTT) 7.5% SDS-PAGE. Gels were dried and exposed to super-resolution phosphor screens (FujiFilm) or Kodak MR films (Kodak). Phosphor screens were scanned with a Typhoon FLA-7000 scanner (GE Healthcare Life Sciences) and quantifications performed in ImageQuantTL (RRID:SCR_014246) and graphs prepared with Graphpad (RRID:SCR_000306).

Snapp E.L., McCaul N., Quandte M., Cabartova Z., Bontjer I., Källgren C., Nilsson I., Land A., von Heijne G., Sanders R.W, & Braakman I. (2017). Structure and topology around the cleavage site regulate post-translational cleavage of the HIV-1 gp160 signal peptide. eLife, 6, e26067.

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