Log In Sign up
The largest database of trusted experimental protocols

Typhoon imaging system

Manufactured by GE Healthcare
Visit Supplier
Sourced in United States, United Kingdom, Denmark

The Typhoon imaging system is a versatile lab equipment designed for high-resolution detection and analysis of various biomolecules. It utilizes a combination of fluorescence and chemiluminescence detection methods to capture and quantify signals from a wide range of sample types, including gels, blots, and microarrays.

Automatically generated - may contain errors

Lab products found in correlation

Storage phosphor screen, by GE Healthcare (6 mentions) Hybond, by Cytiva (5 mentions) Imagequant tl software, by GE Healthcare (4 mentions) Imagequant software, by GE Healthcare (4 mentions) Lambda dna, by New England Biolabs (3 mentions) γ 32p atp, by PerkinElmer (3 mentions) Kaleidagraph software, by Synergy Software (2 mentions) Trizol, by Thermo Fisher Scientific (2 mentions) Imagequant tl 8, by GE Healthcare (2 mentions) Imagequant tl, by GE Healthcare (2 mentions) Originpro 7, by Malvern Panalytical (2 mentions) Bis tris acrylamide gel, by Thermo Fisher Scientific (2 mentions) Whatman, by Cytiva (2 mentions) Trizol reagent, by Thermo Fisher Scientific (2 mentions) Amersham hybond n membrane, by GE Healthcare (2 mentions) Bis tris gel, by Thermo Fisher Scientific (2 mentions) Image studio lite software, by LI COR (1 mentions) Tamra azide, by Vector Laboratories (1 mentions) Optima max xp, by Beckman Coulter (1 mentions) Mouse anti α syn, by BD (1 mentions)

Close spelling variants of this product

Typhoon system (16 citations) Typhoon FLA 9500 imaging system (15 citations) Typhoon FLA 7000 imaging system (12 citations) Typhoon Trio Imaging System (11 citations) Amersham Typhoon imaging system (10 citations) Typhoon FLA 9000 imaging system (8 citations) Typhoon 9500 imaging system (2 citations) Typhoon FLA9400 imaging system (2 citations) Typhoon Gel Imaging System (2 citations) Typhoon FLA7000 Bio-Imaging System (2 citations)

70 protocols using typhoon imaging system

1

Quantitative Click Chemistry Labeling of Proteomes

Check if the same lab product or an alternative is used in the 5 most similar protocols
Click chemistry was performed by combining 42 μL of cell lysate with 8 μL of click chemistry cocktail, resulting in a final concentration of 1% SDS, 100 μM TAMRA-azide (Click Chemistry Tools #1245–5), 1 mM TCEP, 100 μM TBTA (from a 2 mM stock prepared in 1:4 DMSO:t-butyl alcohol), and 1 mM CuSO4. After incubation at room temperature for 90 min, the click reaction was quenched by adding 10 μL of 6X Laemmli sample buffer. Proteins were resolved by SDS-PAGE. Gels were washed with deionized water and scanned for TAMRA fluorescence (Typhoon Imaging System, Molecular Dynamics). Gels were then processed for western blotting or stained with Coomassie blue. All in-gel fluorescence images were processed by Windows ImageJ bundled with 64-bit Java 1.8.0_172 software (National Institute of Health), and contrast was adjusted appropriately. Western blots were analyzed with Image Studio Lite software (LI-COR Biosciences).
Yang T., Cuesta A., Wan X., Craven G.B., Hirakawa B., Khamphavong P., May J.R., Kath J.C., Lapek JD J.r., Niessen S., Burlingame A.L., Carelli J.D, & Taunton J. (2022). Reversible lysine-targeted probes reveal residence time-based kinase selectivity. Nature chemical biology, 18(9), 934-941.
+ Open protocol
+ Expand
2

SDS-PAGE Analysis of Click-Labeled Proteins

Check if the same lab product or an alternative is used in the 5 most similar protocols
After click conjugation with TAMRA-azide, samples were mixed with 6× Laemmli sample buffer and 15-μL aliquots were resolved by SDS-PAGE using 4 to 12% Bis-Tris, 1.0-mm gels (Life Technologies). Gels were washed briefly with 30% EtOH and water and then scanned for fluorescently labeled proteins and molecular weight markers (All Blue standards; Bio-Rad) using excitation wavelengths of 532 nm and 635 nm, respectively (Typhoon Imaging System; Molecular Dynamics), followed by staining with Coomassie blue reagent.
Phillips N.J., Vinaithirthan B.M., Oses-Prieto J.A., Chalkley R.J, & Burlingame A.L. (2023). Capture, Release, and Identification of Newly Synthesized Proteins for Improved Profiling of Functional Translatomes. Molecular & Cellular Proteomics : MCP, 22(3), 100497.
+ Open protocol
+ Expand
3

SDS-PAGE Analysis of TAMRA-Labeled Proteins

Check if the same lab product or an alternative is used in the 5 most similar protocols
After click conjugation with TAMRA-azide, 15 μL samples were treated with 4× Laemmli sample buffer and resolved by SDS/PAGE. Gels were scanned for fluorescently labeled proteins using excitation wavelength 532 nm, and also for the molecular weight marker, using excitation wavelength 647 nm (Typhoon Imaging System; Molecular Dynamics), then stained with Coomassie blue reagent.
Forester C.M., Zhao Q., Phillips N.J., Urisman A., Chalkley R.J., Oses-Prieto J.A., Zhang L., Ruggero D, & Burlingame A.L. (2018). Revealing nascent proteomics in signaling pathways and cell differentiation. Proceedings of the National Academy of Sciences of the United States of America, 115(10), 2353-2358.
+ Open protocol
+ Expand
4

Quantifying α-Synuclein Fibrils by SDS-PAGE

Check if the same lab product or an alternative is used in the 5 most similar protocols
A 150 μL aliquot of the fibrillation sample was centrifuged for 60min at 100,000 × g (Beckman Coulter Optima MAX-XP) to precipitate the fibrils. The supernatant was collected to analyze the residual monomeric content. The fibril pellet was dissolved in 150 μL PBS and vortexed gently and used for analysis. Appropriate amounts of the samples were mixed with Laemmli sample buffer and denatured proteins were separated via SDS-PAGE on a 12% (w/v) polyacrylamide gel and transferred to an Immobilon-FL PVDF membrane (pore size, 0.45 μm). The membrane was probed with mouse anti-αSyn (BD Biosciences; 1:1,500), and an anti- mouse AP-linked secondary antibody (Cell Signaling Technology, 1: 3,000). To visualize the bands, the membrane was exposed to ECF substrate and imaged using a Typhoon imaging system (GE Life Sciences, Pittsburgh, PA). Band intensities were quantified using ImageJ software (NIH, Bethesda, MD), and averages calculated by quantifying each band in triplicate.
Sanyal A., Dutta S., Camara A., Chandran A., Koller A., Watson B.G., Sengupta R., Ysselstein D., Montenegro P., Cannon J., Rochet J.C, & Mattoo S. (2019). Alpha-Synuclein is a Target of Fic-mediated Adenylylation/AMPylation: Possible Implications for Parkinson’s Disease. Journal of molecular biology, 431(12), 2266-2282.
+ Open protocol
+ Expand
5

Platelet Signaling Pathway Modulation

Check if the same lab product or an alternative is used in the 5 most similar protocols
WP (4 × 108 platelets/ml), were incubated with myricetin (7.5, 15, and 30 µM) or the nitric oxide donor PAPA-NONOate (100 µM), lysed in reducing Laemmli sample buffer [12% (w/v) Sodium Dodecyl Sulphate (SDS), 30% (v/v) glycerol, 0.15 M Tris-HCl (pH 6.8), 0.001% (w/v) Brilliant Blue R, 30% (v/v) β-mercaptoethanol] and heated for 5 min. Samples were loaded into a 10% Mini-PROTEAN TGX precast protein gel submerged in 1X Tris/Glycine/SDS buffer (25 mM Tris, 192 mM glycine, 0.1% SDS, pH 8.3), then submitted to vertical transfer in a tetra vertical electrophoresis cell (Bio-Rad, CA, USA) using constant voltage of 150V for 45 min. After protein separation, semi-dry transfer was performed at 15V for 2 h using a BioRad Trans-blot semidry blotter. Membranes were blocked with 5% bovine serum albumin (BSA) for 1 h and incubated with primary antibodies against VASP (Ser239) or GAPDH at 1:1,000 v/v dilution overnight. After washing the primary antibody off, Alexa-488 conjugated phalloidin secondary antibody was incubated for 1 h at room temperature at 1:4,000 v/v dilution. Membranes were visualized using a Typhoon imaging system (GE Healthcare, Hatfield, UK).
Gaspar R.S., da Silva S.A., Stapleton J., Fontelles J.L., Sousa H.R., Chagas V.T., Alsufyani S., Trostchansky A., Gibbins J.M, & Paes A.M. (2020). Myricetin, the Main Flavonoid in Syzygium cumini Leaf, Is a Novel Inhibitor of Platelet Thiol Isomerases PDI and ERp5. Frontiers in Pharmacology, 10, 1678.
+ Open protocol
+ Expand
6

Enzymatic tRNA Methylation Kinetics

Check if the same lab product or an alternative is used in the 5 most similar protocols
Reactions containing the indicated labeled tRNAs, 1.5 mM MgCl2, 50 mM Tris pH 8.0, 0.5 mM S-adenosyl methionine (SAM) were incubated with ≥2.5 µM enzyme (≥100-fold excess over tRNA concentration) at 40 °C (SctRNAs) or 50 °C (TktRNAs). Aliquots were taken at designated time points and quenched with phenol: chloroform: isoamyl alcohol (25:24:1), purified, digested with Nuclease P1 and analyzed by thin layer chromatography (TLC) in isobutyric acid:H2O:NH4OH (66:33:1) to resolve G/m1G9 and saturated ammonium sulfate:H2O:isopropanol (80:18:2) to resolve A/m1A9. Dried TLC plates were exposed to a phosphor screen and scanned using the Typhoon™ imaging system (GE Healthcare, Chicago, IL, USA) and quantified using ImageQuant™ TL software (GE Healthcare). The percent m1A9/m1G9 formed (%P) was plotted as a function of time (t), and kobs was determined by fitting to a single exponential equation (Equation (1)) using Kaleidagraph software (Synergy, Reading, PA, USA).

The rates were verified to be saturating for enzyme concentrations by measuring kobs with at least two different excess enzyme concentrations for WT, all alanine variants and the 3DE (D100N+D210N+D245N+E111Q) variant.
Krishnamohan A., Dodbele S, & Jackman J.E. (2019). Insights into Catalytic and tRNA Recognition Mechanism of the Dual-Specific tRNA Methyltransferase from Thermococcus kodakarensis. Genes, 10(2), 100.
+ Open protocol
+ Expand
7

RNA Extraction and Northern Blotting

Cited 1 time
Check if the same lab product or an alternative is used in the 5 most similar protocols
RNA extraction and Northern blotting analyses were performed as described previously (23 (link)). Briefly, total RNA was extracted using TRIzol (Thermo Fisher Scientific). 5–10 μg of RNA were separated on a denaturing formaldehyde 1% agarose gel for mRNAs and rRNAs or 10% polyacrylamide gel containing 7 m urea for tRNAs, transferred to a nylon membrane (GE Healthcare), and UV-crosslinked to the membrane. Membranes were hybridized with T7-transcribed [α-32P]UTP- radiolabeled riboprobes. Hybridization was performed at 60 °C in 50% formamide, 7% SDS, 0.2 m NaCl, 80 mm sodium phosphate, pH 7.4, and 100 μg/ml salmon sperm DNA. Imaging and quantification were performed with a phosphorimaging system (Bio-Rad) or Typhoon imaging system (GE Healthcare). A detailed list of primers used to transcribe the riboprobes is provided in supplemental Table S2.
Zaganelli S., Rebelo-Guiomar P., Maundrell K., Rozanska A., Pierredon S., Powell C.A., Jourdain A.A., Hulo N., Lightowlers R.N., Chrzanowska-Lightowlers Z.M., Minczuk M, & Martinou J.C. (2017). The Pseudouridine Synthase RPUSD4 Is an Essential Component of Mitochondrial RNA Granules. The Journal of Biological Chemistry, 292(11), 4519-4532.
+ Open protocol
+ Expand
8

Quantifying IGFBP-4 Cleavage by PAPP-A

Check if the same lab product or an alternative is used in the 5 most similar protocols
Specific proteolytic cleavage of 125I-labeled IGFBP-4 is described in detail elsewhere49 (link). Briefly, the PAPP-A:STC2 complex mixtures were diluted (1:190) to a concentration of 145 pM PAPP-A and mixed with preincubated 125I-IGFBP4 (10 nM) and IGF-1 (100 nM) in 50 mM Tris-HCl, 100 mM NaCl, 1 mM CaCl2. Following 1 h incubation at 37°C, reactions were terminated by the addition of SDS-PAGE sample buffer supplemented with 25 mM EDTA. Substrate and co-migrating cleavage products were separated by 12% nonreducing SDS-PAGE and visualized by autoradiography using a storage phosphor screen (GE Healthcare) and a Typhoon imaging system (GE Healthcare). Band intensities were quantified using ImageQuant TL 8.1 software (GE Healthcare).
Marouli E., Graff M., Medina-Gomez C., Lo K.S., Wood A.R., Kjaer T.R., Fine R.S., Lu Y., Schurmann C., Highland H.M., Rüeger S., Thorleifsson G., Justice A.E., Lamparter D., Stirrups K.E., Turcot V., Young K.L., Winkler T.W., Esko T., Karaderi T., Locke A.E., Masca N.G., Ng M.C., Mudgal P., Rivas M.A., Vedantam S., Mahajan A., Guo X., Abecasis G., Aben K.K., Adair L.S., Alam D.S., Albrecht E., Allin K.H., Allison M., Amouyel P., Appel E.V., Arveiler D., Asselbergs F.W., Auer P.L., Balkau B., Banas B., Bang L.E., Benn M., Bergmann S., Bielak L.F., Blüher M., Boeing H., Boerwinkle E., Böger C.A., Bonnycastle L.L., Bork-Jensen J., Bots M.L., Bottinger E.P., Bowden D.W., Brandslund I., Breen G., Brilliant M.H., Broer L., Burt A.A., Butterworth A.S., Carey D.J., Caulfield M.J., Chambers J.C., Chasman D.I., Chen Y.D., Chowdhury R., Christensen C., Chu A.Y., Cocca M., Collins F.S., Cook J.P., Corley J., Galbany J.C., Cox A.J., Cuellar-Partida G., Danesh J., Davies G., de Bakker P.I., de Borst G.J., de Denus S., de Groot M.C., de Mutsert R., Deary I.J., Dedoussis G., Demerath E.W., den Hollander A.I., Dennis J.G., Di Angelantonio E., Drenos F., Du M., Dunning A.M., Easton D.F., Ebeling T., Edwards T.L., Ellinor P.T., Elliott P., Evangelou E., Farmaki A.E., Faul J.D., Feitosa M.F., Feng S., Ferrannini E., Ferrario M.M., Ferrieres J., Florez J.C., Ford I., Fornage M., Franks P.W., Frikke-Schmidt R., Galesloot T.E., Gan W., Gandin I., Gasparini P., Giedraitis V., Giri A., Girotto G., Gordon S.D., Gordon-Larsen P., Gorski M., Grarup N., Grove M.L., Gudnason V., Gustafsson S., Hansen T., Harris K.M., Harris T.B., Hattersley A.T., Hayward C., He L., Heid I.M., Heikkilä K., Helgeland Ø., Hernesniemi J., Hewitt A.W., Hocking L.J., Hollensted M., Holmen O.L., Hovingh G.K., Howson J.M., Hoyng C.B., Huang P.L., Hveem K., Ikram M.A., Ingelsson E., Jackson A.U., Jansson J.H., Jarvik G.P., Jensen G.B., Jhun M.A., Jia Y., Jiang X., Johansson S., Jørgensen M.E., Jørgensen T., Jousilahti P., Jukema J.W., Kahali B., Kahn R.S., Kähönen M., Kamstrup P.R., Kanoni S., Kaprio J., Karaleftheri M., Kardia S.L., Karpe F., Kee F., Keeman R., Kiemeney L.A., Kitajima H., Kluivers K.B., Kocher T., Komulainen P., Kontto J., Kooner J.S., Kooperberg C., Kovacs P., Kriebel J., Kuivaniemi H., Küry S., Kuusisto J., La Bianca M., Laakso M., Lakka T.A., Lange E.M., Lange L.A., Langefeld C.D., Langenberg C., Larson E.B., Lee I.T., Lehtimäki T., Lewis C.E., Li H., Li J., Li-Gao R., Lin H., Lin L.A., Lin X., Lind L., Lindström J., Linneberg A., Liu Y., Liu Y., Lophatananon A., Luan J., Lubitz S.A., Lyytikäinen L.P., Mackey D.A., Madden P.A., Manning A.K., Männistö S., Marenne G., Marten J., Martin N.G., Mazul A.L., Meidtner K., Metspalu A., Mitchell P., Mohlke K.L., Mook-Kanamori D.O., Morgan A., Morris A.D., Morris A.P., Müller-Nurasyid M., Munroe P.B., Nalls M.A., Nauck M., Nelson C.P., Neville M., Nielsen S.F., Nikus K., Njølstad P.R., Nordestgaard B.G., Ntalla I., O'Connel J.R., Oksa H., Loohuis L.M., Ophoff R.A., Owen K.R., Packard C.J., Padmanabhan S., Palmer C.N., Pasterkamp G., Patel A.P., Pattie A., Pedersen O., Peissig P.L., Peloso G.M., Pennell C.E., Perola M., Perry J.A., Perry J.R., Person T.N., Pirie A., Polasek O., Posthuma D., Raitakari O.T., Rasheed A., Rauramaa R., Reilly D.F., Reiner A.P., Renström F., Ridker P.M., Rioux J.D., Robertson N., Robino A., Rolandsson O., Rudan I., Ruth K.S., Saleheen D., Salomaa V., Samani N.J., Sandow K., Sapkota Y., Sattar N., Schmidt M.K., Schreiner P.J., Schulze M.B., Scott R.A., Segura-Lepe M.P., Shah S., Sim X., Sivapalaratnam S., Small K.S., Smith A.V., Smith J.A., Southam L., Spector T.D., Speliotes E.K., Starr J.M., Steinthorsdottir V., Stringham H.M., Stumvoll M., Surendran P., Hart L.M., Tansey K.E., Tardif J.C., Taylor K.D., Teumer A., Thompson D.J., Thorsteinsdottir U., Thuesen B.H., Tönjes A., Tromp G., Trompet S., Tsafantakis E., Tuomilehto J., Tybjaerg-Hansen A., Tyrer J.P., Uher R., Uitterlinden A.G., Ulivi S., van der Laan S.W., Van Der Leij A.R., van Duijn C.M., van Schoor N.M., van Setten J., Varbo A., Varga T.V., Varma R., Edwards D.R., Vermeulen S.H., Vestergaard H., Vitart V., Vogt T.F., Vozzi D., Walker M., Wang F., Wang C.A., Wang S., Wang Y., Wareham N.J., Warren H.R., Wessel J., Willems S.M., Wilson J.G., Witte D.R., Woods M.O., Wu Y., Yaghootkar H., Yao J., Yao P., Yerges-Armstrong L.M., Young R., Zeggini E., Zhan X., Zhang W., Zhao J.H., Zhao W., Zhao W., Zheng H., Zhou W., Rotter J.I., Boehnke M., Kathiresan S., McCarthy M.I., Willer C.J., Stefansson K., Borecki I.B., Liu D.J., North K.E., Heard-Costa N.L., Pers T.H., Lindgren C.M., Oxvig C., Kutalik Z., Rivadeneira F., Loos R.J., Frayling T.M., Hirschhorn J.N., Deloukas P, & Lettre G. (2017). Rare and low-frequency coding variants alter human adult height. Nature, 542(7640), 186-190.
+ Open protocol
+ Expand
9

Enzymatic Ligation Reaction Kinetics

Check if the same lab product or an alternative is used in the 5 most similar protocols
Ligation reactions were performed at 37°C in standard reaction buffer (50 mM NaMOPS, pH 7.5, 10% glycerol, 1 mM ATP, 1 mM DTT, 100 μg/μl BSA) at 150 mM ionic strength, unless otherwise stated. Ionic strength was controlled using the Debye–Hückel theory of electrolytes. Mg(OAc)2 and NaOAc concentrations were adjusted to achieve the desired reaction conditions. Reactions were stopped by mixing reaction aliquots with an appropriate volume of 1.2× quench solution (90% formamide, 50 mM EDTA, 0.006% bromophenol blue, 0.006% xylene cyanol) at predetermined times. Quenched samples were loaded directly onto running DNA denaturing gels (15% (w/v) polyacrylamide, 8 M urea, 1 × TBE). Gels were scanned using a Typhoon imaging system (GE) set to monitor emission at 525 (BP20) with excitation set to 488 nm. The fluorescence values of all DNA species were within the linear range of the instrument and were quantified using ImageQuant TL (GE). After quantification, the fractions of all observable species were plotted and analyzed using GraphPad Prism.
McNally J.R., Ames A.M., Admiraal S.J, & O’Brien P.J. (2023). Human DNA ligases I and III have stand-alone end-joining capability, but differ in ligation efficiency and specificity. Nucleic Acids Research, 51(2), 796-805.
+ Open protocol
+ Expand
10

Primer Extension Kinetics Assay

Check if the same lab product or an alternative is used in the 5 most similar protocols
A 12-mer oligomer (FAM-5´-GGTGGTCCATAA-3´, for full primer extension in the presence of four dNTPs) and a 14-mer oligomer (FAM-5´-GGTGGTCCATAAAC-3´, for single base primer extension and steady-state kinetics in the presence of single dNTPs) were annealed to the 19-mer oligomer template (5´-TCTCXGTTTATGGACCACC-3´, where X is dA or S-[2-(N6-deoxyadenosinyl)ethyl]GSH). Primer extension was performed with 120 nM oligonucleotide complex in 50 mM Tris-HCl buffer (pH 7.5) containing 50 mM NaCl, 5 mM MgCl2, 500 µM dNTPs, 2% (v/v) glycerol, 50 µg/mL bovine serum albumin (BSA), and 20 nM polymerase (with the exception of hPol ι, 40 nM) at 37 °C. Steady-state kinetics were performed under the same conditions except using polymerase concentrations from 1–40 nM, varying dNTP concentrations (0.1–500 µM), and incubation times from 5–30 min so that the maximum incorporation was < 20% of the substrate concentration. Reactions were quenched with 7 µL of 20 mM EDTA (pH 9.0) in 95% (v/v) formamide. Products were separated using 18% (w/v) polyacrylamide gel electrophoresis and visualized using a Typhoon imaging system (GE Healthcare).
Sedgeman C.A., Su Y, & Guengerich F.P. (2017). Formation of S-[2-(N6-Deoxyadenosinyl)ethyl]glutathione in DNA and Replication Past the Adduct by Translesion DNA Polymerases. Chemical research in toxicology, 30(5), 1188-1196.
+ Open protocol
+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Sign up for free.
Registration takes 20 seconds.
Available from any computer
No download required

Sign up now

Revolutionizing how scientists
search and build protocols!