Fusion fx7 detection system

Manufactured by Avantor

Sourced in Germany

The FUSION-FX7 detection system is a laboratory instrument designed for the detection and quantification of various analytes. It utilizes advanced spectroscopic techniques to perform sensitive and accurate analyses. The core function of this system is to provide reliable data measurements for research and diagnostic applications.

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Lab products found in correlation

Bio1d software, by Vilber (2 mentions) Protran nitrocellulose membrane, by Cytiva (1 mentions) Pierce ecl western blotting substrate, by Thermo Fisher Scientific (1 mentions) Donkey anti mouse 488, by Thermo Fisher Scientific (1 mentions) Mca409s, by Bio-Rad (1 mentions) Donkey anti rat 488, by Thermo Fisher Scientific (1 mentions) Donkey anti mouse 647, by Thermo Fisher Scientific (1 mentions) α gfp, by Roche (1 mentions) α myc, by Merck Group (1 mentions) Pvdf membrane, by Merck Group (1 mentions) Mouse anti β actin, by Merck Group (1 mentions) Bc assay protein quantitation kit, by Interchim (1 mentions) Phosstop, by Roche (1 mentions) Complete mini, by Roche (1 mentions) Myimageanalysis software, by Thermo Fisher Scientific (1 mentions) Lowry assay, by Bio-Rad (1 mentions)

Spelling variants of this product

Fusion FX7 (16 citations) Fusion FX7 system (11 citations)

5 protocols using fusion fx7 detection system

Immunoblot Analysis of HA-Tagged Proteins

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The strains of interest were grown to an OD_750nm of 0.9–1 in 20 mL TAP medium and then cells were harvested by centrifugation (3000 x g for 3 min). After that, proteins were extracted by resuspending pelleted cells in 200 μl of lysis buffer (60 mM Tris pH 6.8, 2% (w/v) SDS, 10 % (v/v) glycerol, 100 mM DTT). Protein concentrations were quantified using the amido black assay [24 (link)]. Samples containing 10 μg of total protein fractions were denatured at 95 °C for 5 min, separated via Tris-glycine-SDS-PAGE in 8% (w/v) polyacrylamide gels and transferred to 0.45 μm Protran Nitrocellulose membranes (Amersham) using transfer buffer (25 mM Tris-HCl, 192 mM glycine and 20 % (v/v) methanol). Immunochemical protein detection was performed with HA-tag polyclonal antibody (Thermo Fisher Scientific) using the Thermo Scientific Pierce ECL Western blotting substrate. Signals were visualized using the FUSION-FX7 detection system (Peqlab, Germany).

Dementyeva P., Freudenberg R.A., Baier T., Rojek K., Wobbe L., Weisshaar B, & Kruse O. (2021). A novel, robust and mating-competent Chlamydomonas reinhardtii strain with an enhanced transgene expression capacity for algal biotechnology. Biotechnology Reports, 31, e00644.

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SDS-PAGE Analysis of Cellular Protein Expression

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For sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) cell lysates of CG4, CG4_venus, and CG4_wt-α-syn cells (n = 3 each) were extracted using RIPA buffer and 15 μg of proteins were loaded on a 4-12 % Novex® NuPAGE Bis-Tris-Mini gels (Invitrogen) and afterwards transferred on a polyvinylidene fluoride membrane (Immobilon PVDF-FL, 0.45 μm; Millipore). Membranes were blocked (PBS containing 0.1 % Tween-20 and 1 % BSA) for 1 h at RT and incubated in primary antibodies diluted in 0.1 % sodium azide, 0.1 % Tween 20, and 1 % BSA in PBS overnight at 4°C: monoclonal rat anti-MBP (1:200; MCA409S; AbD Serotec), monoclonal mouse anti-GAPDH (1:100.000; clone GB-69; Sigma), and monoclonal anti-CNPase (1:1000; clone 11-5B; Millipore) were detected with respective secondary antibodies diluted in blocking buffer (1 h at RT): donkey anti-mouse 488 (1:3000), donkey anti-rat 488 (1:3000), and donkey anti-mouse 647 (1:1000; all Invitrogen). Fluorescent signals were captured using a Fusion FX7 detection system (Peqlab). Results were quantified using Bio1D software (Vilber Lourmat) and normalized to GAPDH.

May V.E., Ettle B., Poehler A.M., Nuber S., Ubhi K., Rockenstein E., Winner B., Wegner M., Masliah E, & Winkler J. (2014). α-Synuclein impairs oligodendrocyte progenitor maturation in multiple system atrophy. Neurobiology of aging, 35(10), 2357-2368.

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Protein Detection and Immunoblotting

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Proteins were separated on SDS-PAGE, transferred to the PVDF membrane (Millipore) and detected using one of the following antibodies: α-GFP (mouse, 1:1,000, Roche), α-RFP (rat, 1:1,000, Chromotek), α-Myc (1:1,000, Sigma), α-ARF1 (rabbit, 1:2,000, Agrisera), α-GN-SEC7 (rabbit, 1:2,500) [37 (link)], and POD-conjugated secondary antibodies. Chemiluminescence signal was acquired using Fusion Fx7 detection system (PEQlab, Erlangen, Germany).

Singh M.K., Richter S., Beckmann H., Kientz M., Stierhof Y.D., Anders N., Fäßler F., Nielsen M., Knöll C., Thomann A., Franz-Wachtel M., Macek B., Skriver K., Pimpl P, & Jürgens G. (2018). A single class of ARF GTPase activated by several pathway-specific ARF-GEFs regulates essential membrane traffic in Arabidopsis. PLoS Genetics, 14(11), e1007795.

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Quantifying Astrocyte Glutamate Transporters

Cited 1 time

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Cultured astrocytes were harvested in 1xRipa lysis buffer [10xRipa: 150 mM NaCl, 38.5mM SDS, 50mM Tris, 134mM SDOX, 0.5 mM EDTA, 1% NP40, complete protease inhibitor cocktail Complete Mini and phosphatase inhibitor cocktail PhosStop (Roche Diagnostic GmbH, Mannheim, Germany)] and centrifuged at 10,000 rpm for 10 min. Protein concentration was determined with BC Assay Protein Quantitation Kit (Interchim) and equal amounts of proteins were analyzed by Western blotting. SLC1A2 protein was detected by using rabbit anti-SLC1A2 (Thermo Fisher Scientific, 1:500) and SLC1A3 by using rabbit anti SLC1A3 (Abcam; 1:300). Mouse anti-β-actin (1:1000, Millipore clone C4) or anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH) was blotted as loading control. All blots were at least performed three times. Signal capture was conducted using a Fusion FX7 detection system (PeqLab). Densitometric quantifications were performed using the Bio1D software (Vilber Lourmat) by normalizing signals to beta actin or GAPDH expression (for further details on blotting and quantification see also [19 (link)]).

Lee D.H., Seubert S., Huhn K., Brecht L., Rötger C., Waschbisch A., Schlachetzki J., Klausmeyer A., Melms A., Wiese S., Winkler J, & Linker R.A. (2017). Fingolimod effects in neuroinflammation: Regulation of astroglial glutamate transporters?. PLoS ONE, 12(3), e0171552.

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Quantitative Immunoblotting of IFR1 Protein

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Cells were pelleted (3000 × g, 3 min) and suspended in lysis buffer (60 mM Tris pH 6.8, 2% SDS, 10% glycerol and freshly added 1 mM Pefabloc). Total proteins were extracted via freeze-thaw cycle in liquid N₂ and quantified by Lowry assay (BioRAD). The proteins were separated by a 12% Tris-glycine SDS-PAGE and blotted on to a nitrocellulose membrane. After overnight blocking (5% Milk powder in TBST with 0.1% Tween), the membrane was incubated at room temperature for 1.5 h with IFR1-specific antiserum (1:2500), washed and then incubated for 1 h with a peroxidase-conjugated anti-rabbit antibody (Agrisera, Sweden) for chemiluminescence detection (ECL: GE Healthcare). Signals were visualized using the FUSION-FX7 detection system (Peqlab, Germany). Protein bands were quantified with MyImageAnalysis software (ThermoFisher Scientific).

Venkanna D., Südfeld C., Baier T., Homburg S.V., Patel A.V., Wobbe L, & Kruse O. (2017). Knock-Down of the IFR1 Protein Perturbs the Homeostasis of Reactive Electrophile Species and Boosts Photosynthetic Hydrogen Production in Chlamydomonas reinhardtii. Frontiers in Plant Science, 8, 1347.

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