Shotgun proteomics was performed on an LTQ-Orbitrap Elite mass spectrometer (Thermo Fisher Scientific) connected to a Dionex UltiMate RS 3000 nano-LC (Thermo Fisher Scientific). Peptides were loaded onto a C18 trap column (Acclaim PepMap, 100 A 5 μm particle size) (Thermo Fisher Scientific) at a flow rate of 5 μL/min in solvent A (0.1% formic acid in water) and desalted for 10 minutes. Tryptic peptides were then separated by a reversed-phase C18 analytical column (25-cm long, packed with Magic AQ C18 resin) (Michrom Bioresources, Auburn, CA). Peptides were eluted by changing the concentration of solvent B (0.1% formic acid in acetonitrile) from 2% (first 10 min), to 35% (over 100 min), and 85% (next 2 min followed by 5 min hold at 85%). Eluted peptides were subjected to MS1 and MS/MS on the mass spectrometer. The MS1 mass resolution was set to 60,000 with a scan range of 400 to 1800 m/z. The top 10 most abundant ions in each MS1 scan were selected for collision-induced dissociation. Dynamic exclusion was set for 30 seconds.
Magic aq c18 resin
Manufactured by Bruker
The Magic AQ C18 resin is a high-performance liquid chromatography (HPLC) material designed for the separation and purification of a wide range of compounds. It features a chemically bonded C18 stationary phase that provides efficient retention and separation of both polar and non-polar analytes. The resin is compatible with various HPLC applications and solvents, making it a versatile tool for analytical and preparative chromatography.
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2 protocols using magic aq c18 resin
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Shotgun Proteomics on LTQ-Orbitrap Elite
2
Shotgun Proteomics on LTQ-Orbitrap Elite
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Shotgun proteomics was performed on an LTQ-Orbitrap Elite mass spectrometer (Thermo Fisher Scientific) connected to a Dionex UltiMate RS 3000 nano-LC (Thermo Fisher Scientific). Peptides were loaded onto a C18 trap column (Acclaim PepMap, 100 A 5 μm particle size) (Thermo Fisher Scientific) at a flow rate of 5 μL/min in solvent A (0.1% formic acid in water) and desalted for 10 minutes. Tryptic peptides were then separated by a reversed-phase C18 analytical column (25-cm long, packed with Magic AQ C18 resin) (Michrom Bioresources, Auburn, CA). Peptides were eluted by changing the concentration of solvent B (0.1% formic acid in acetonitrile) from 2% (first 10 min), to 35% (over 100 min), and 85% (next 2 min followed by 5 min hold at 85%). Eluted peptides were subjected to MS1 and MS/MS on the mass spectrometer. The MS1 mass resolution was set to 60,000 with a scan range of 400 to 1800 m/z. The top 10 most abundant ions in each MS1 scan were selected for collision-induced dissociation. Dynamic exclusion was set for 30 seconds.
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