Storm imaging system

Manufactured by GE Healthcare

Sourced in United Kingdom

The Storm imaging system is a laboratory equipment product from GE Healthcare. It is designed to capture and analyze images for research purposes. The core function of the Storm imaging system is to provide high-quality image acquisition and data analysis capabilities to support scientific research and investigation.

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Lab products found in correlation

Nupage, by Thermo Fisher Scientific (2 mentions) Lds sample buffer, by Thermo Fisher Scientific (2 mentions) Imagequant software, by GE Healthcare (2 mentions) Polyvinylidene difluoride membrane, by Merck Group (1 mentions) Roti quant reagent, by Carl Roth (1 mentions) Phospho bcl 2, by Cell Signaling Technology (1 mentions) Hybond p membrane, by GE Healthcare (1 mentions) Ripa lysis buffer, by Merck Group (1 mentions) Caspase 3, by Cell Signaling Technology (1 mentions) Gapdh, by Cell Signaling Technology (1 mentions) Nupage bis tris gel, by Thermo Fisher Scientific (1 mentions) Bradford reagent, by Merck Group (1 mentions) Bradford protein assay, by Thermo Fisher Scientific (1 mentions) Odyssey infrared imaging system, by LI COR (1 mentions) Primuline, by Merck Group (1 mentions) Imagequant tl software, by GE Healthcare (1 mentions) Bamhi, by Thermo Fisher Scientific (1 mentions) Polyvinylidene fluoride membrane, by Merck Group (1 mentions) Imagequant las 4000 system, by GE Healthcare (1 mentions) Typhoon trio variable mode imager, by GE Healthcare (1 mentions)

Close spelling variants of this product

Storm 860 Imaging System Storm 860 Gel and Blot Imaging System STORM-840 imaging system Storm Gel and Blot Imaging System

8 protocols using storm imaging system

In Vitro BY-Kinase Assays for Substrate Identification

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In vitro BY-kinase assays were carried out in a total volume of 10 µl containing either 0.5 µg of CapA and CapB, or 2 µg of a CapAB protein fusion construct. For identification of protein substrates, 2 µg of a recombinant target protein were added. The proteins were incubated in the presence of 10 μCi γ-labeled [³³P]ATP (~300 nM; Hartmann Analytic) in 50 mM Tris-HCl, 10 mM MgCl₂, pH 7.5 supplemented with 0.5 mM DTT, 0.5 mM EDTA and 10 µM ATP. Assays with CapAB protein variants were carried out as described for the wild-type proteins.
For identification of PknB protein substrates, purified PknB (0.5 µg) was incubated in presence of 3 mM MnCl₂ in the reaction mixture described above. Cross-phosphorylation of CapAB by PknB was assessed analogously.
After 30 min of incubation at 30 °C, reactions were stopped by addition of 4x LDS sample buffer (Invitrogen), and analyzed by SDS-PAGE (NuPAGE, Invitrogen). Radioactive protein bands were visualized using a storage phosphor screen in a Storm imaging system (GE Healthcare). A detailed description of the identification of phosphorylation sites by nanoLC-MS/MS is given in the Supplementary Methods.

Rausch M., Deisinger J.P., Ulm H., Müller A., Li W., Hardt P., Wang X., Li X., Sylvester M., Engeser M., Vollmer W., Müller C.E., Sahl H.G., Lee J.C, & Schneider T. (2019). Coordination of capsule assembly and cell wall biosynthesis in Staphylococcus aureus. Nature Communications, 10, 1404.

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Protein Separation and Detection

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SDS-PAGE was performed using standard procedures. Proteins were separated on 15% polyacrylamide gels. Polyvinylidene difluoride membranes (Millipore) were used for Western blotting. An enhanced chemiluminescence detection system was used, and chemiluminescence was detected with X-ray films (Foton-Bis). Radioactively labeled proteins were visualized by digital autoradiography (Storm imaging system; GE Healthcare), followed by image processing with ImageQuant software (GE Healthcare). The protein concentration was determined by the Bradford method using the Roti-Quant reagent (Carl Roth GmbH) and bovine serum albumin as the protein standard.

Sakowska P., Jans D.C., Mohanraj K., Riedel D., Jakobs S, & Chacinska A. (2015). The Oxidation Status of Mic19 Regulates MICOS Assembly. Molecular and Cellular Biology, 35(24), 4222-4237.

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Compound Treatment Induces Apoptosis

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Cells were seeded in T-25 flasks at ∼2.5 × 10⁵ cells per flasks in 4 ml of cell-specific media and exposed to compounds at 0.5 μM for 24 h, 48 h or 72 h. Protein was prepared from treated cells using RIPA lysis buffer (Sigma) and quantified using the Bradford protein assay with Bradford reagent (Sigma). Equal amounts of protein were loaded in all wells (15 μg). Proteins were separated by electrophoresis through a 4–12% NuPAGE Bis-Tris gel (Invitrogen) and subsequently transferred to Hybond-P membrane (GE Healthcare, Buckinghamshire, UK).
Detection was carried out using anti-human cyclin B1 (ref. H433; Santa Cruz Biotechnology, Inc., Santa Cruz, CA, USA), phospho-Bcl2 (ref. 2827S; Cell Signaling Technology, Boston, MA, USA), caspase-3 (ref. 9665; Cell Signaling), GAPDH (ref. 2118; Cell Signaling) and p53 (ref. ab28-100; Abcam, Cambridge, UK) primary antibodies. Secondary alkaline phosphatase-conjugated anti-rabbit IgG (ref. 7054; Cell Signaling) or anti-mouse IgG (ref 7056; Cell Signaling) antibodies were used for detection in conjunction with a chemifluorescent substrate (ECF substrate, ref. RPN5785; GE Healthcare). Bands were visualised and quantified using a Storm imaging system (GE Healthcare).

Stengel C., Newman S.P., Day J.M., Chander S.K., Jourdan F.L., Leese M.P., Ferrandis E., Regis-Lydi S., Potter B.V., Reed M.J., Purohit A, & Foster P.A. (2014). In vivo and in vitro properties of STX2484: a novel non-steroidal anti-cancer compound active in taxane-resistant breast cancer. British Journal of Cancer, 111(2), 300-308.

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Immunoblotting of Whole Cell Lysates

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Immunoblots were performed on whole cell lysates in radioimmunoprecipitation assay (RIPA) buffer. Cells were lysed in RIPA buffer for 20 minutes at 4°C. Protein concentration was determined via Bradford protein assay (Life Technologies). 10–30 µg of protein were loaded onto a 4–20% gradient SDS-polyacrylamide gel (SDS-PAGE) (BioRad). Immuoblotting was either performed using the Odyssey Infrared Imaging System (Li-Cor) or STORM imaging system (GE Healthcare) and analyzed using ImageJ.

Wolf Horrell E.M., Jarrett S.G., Carter K.M, & D’Orazio J.A. (2017). Divergence of cAMP signaling pathways mediating augmented nucleotide excision repair and pigment induction in melanocytes. Experimental dermatology, 26(7), 577-584.

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Quantitative Lipid Profiling via TLC

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The dried extract residue was re-dissolved in 0.5 ml of chloroform/methanol (9:1) solution. After a further 1:5 dilution in the same solution, 10 μl of the lipid extract was loaded onto a thin layer chromatography plate (silica gel 60A, 250 μm thickness, 20×20 cm, Watman, England) along with L-α-lysophosphatidylcholine standards (from egg yolk, Sigma L4129, St. Louis, MO). The lipids on the plate were first separated in a polar solvent (65:25:4 chloroform:methanol:water) for 12 min. After drying, the lipids on the plate were separated in a non-polar solvent (75:35:1 hexane/diethyl ether/acetic acid) for 30 min. The plate was thinly sprayed with 0.05% primuline (Sigma, St. Louis, MO) in 80% acetone. The band detection was performed under fluorescence mode in a Storm imaging system (GE Healthcare, CT). The band analysis and quantification was based on integration of band density using ImageQuant TL software (GE Healthcare, CT). The amount of LPC in each sample group was extrapolated from the standards and reported as a percentage of the total tissue weight.

Wiltz D.C., Han R.I., Wilson R.L., Kumar A., Morrisett J.D, & Grande-Allen K.J. (2014). Differential Aortic and Mitral Valve Interstitial Cell Mineralization and the Induction of Mineralization by Lysophosphatidylcholine In Vitro. Cardiovascular engineering and technology, 5(4), 371-383.

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CapC Phosphatase Activity Assay

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CapC phosphatase activity was examined in vitro by the addition of CapC1 or CapC2 (2 µg each) with 2 mM MnCl₂ to the CapAB in vitro kinase assays (see above) and subsequent heat-inactivation. After incubation for 1 h at 30 °C, phosphatase reaction was stopped by the by addition of 4x LDS sample buffer (Invitrogen), and analyzed by SDS-PAGE (NuPAGE, Invitrogen). Radioactive protein bands were visualized using a storage phosphor screen in a Storm imaging system (GE Healthcare).

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Quantifying Mitochondrial DNA Levels

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DNA samples were digested with BamHI (Fermentas) at 37 °C for 20 min at 1 μg per 20 mL reaction and resolved on a 10 cm pathlength 0.6% agarose gel. Gels were nicked, denatured, neutralized, and transferred on to positively charged Hybond (GE Healthcare) overnight. Next, membrane was pre-hybridized in Church and Gilbert buffer for 2 h then hybridized with randomly labeled human 185 probe overnight. Following this, the membrane was washed three times in 20 min intervals in SSC buffer. The membrane was subsequently exposed to a phosphorimager screen for two days and scanned on a Storm Imaging System (GE Healthcare). The membrane was then re-probed with human mitochondrial DNA probes and similarly processed. The ratio of mitochondrial DNA to nuclear DNA was calculated and normalized to the average of the three control samples.

Nath S., Caron N.S., May L., Gluscencova O.B., Kolesar J., Brady L., Kaufman B.A., Boulianne G.L., Rodriguez A.R., Tarnopolsky M.A, & Truant R. (2022). Functional characterization of variants of unknown significance in a spinocerebellar ataxia patient using an unsupervised machine learning pipeline. Human Genome Variation, 9, 10.

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Mitochondrial Protein Analysis: SDS-PAGE, BN-PAGE, and Western Blot

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SDS–PAGE was performed according to standard procedures. Protein extracts were examined on 15% acrylamide gels. BN-PAGE was performed as described previously (Chacinska et al., 2004 (link)). Digital autoradiography was used for gel analysis (Storm Imaging System and Variable Mode Imager Typhoon Trio; GE Healthcare, Little Chalfont, United Kingdom), followed by use of ImageQuant software (GE Healthcare). Western blot was performed using polyvinylidene fluoride membranes (Millipore, Billerica, MA) and an ECL detection system. The chemiluminescent signals were detected with x-ray film (Foton-Bis, Bydgoszcz, Poland) or the digital ImageQuant LAS4000 system (GE Healthcare). The protein concentrations were estimated according to the Bradford method with Roti-Quant (Carl Roth, Karlsruhe, Germany) and BSA as the protein standard. The chemical modification of mitochondria was performed with mPEG reagent (Sigma-Aldrich).

Gornicka A., Bragoszewski P., Chroscicki P., Wenz L.S., Schulz C., Rehling P, & Chacinska A. (2014). A discrete pathway for the transfer of intermembrane space proteins across the outer membrane of mitochondria. Molecular Biology of the Cell, 25(25), 3999-4009.

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