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Symmetry c18 preparative column

Manufactured by Waters Corporation
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The Symmetry C18 preparative column is a high-performance liquid chromatography (HPLC) column designed for preparative-scale separations. The column features a C18 reversed-phase stationary phase, which is suitable for the purification of a wide range of organic compounds. The column dimensions and packing material are optimized for preparative-scale applications, allowing for efficient separation and high sample loading capacity.

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Lab products found in correlation

Nanoacquity ultraperformance lc system, by Waters Corporation (3 mentions) Orbitrap elite mass spectrometer, by Thermo Fisher Scientific (3 mentions) Ltq velos mass spectrometer, by Thermo Fisher Scientific (3 mentions) Ultimate 3000 rapid separation lc system, by Thermo Fisher Scientific (3 mentions) Ethyl hybrid c18 analytical column, by Waters Corporation (3 mentions) Nanoacquity ultra performance liquid chromatography system, by Waters Corporation (1 mentions) Bridged ethyl hybrid c18 analytical column, by Waters Corporation (1 mentions) Ltq velos, by Thermo Fisher Scientific (1 mentions)

4 protocols using symmetry c18 preparative column

1

Proteomic Analysis via SDS-PAGE and LC-MS/MS

Cited 1 time
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Following SDS-PAGE, gel lanes were sliced and subjected to in-gel digestion with trypsin58 (link) with modifications11 (link). Peptide samples were analysed by liquid chromatography (LC)-tandem MS using a nanoACQUITY UltraPerformance LC system (Waters) coupled online to an LTQ Velos mass spectrometer (Thermo Fisher Scientific) or using an UltiMate 3000 Rapid Separation LC system (Thermo Fisher Scientific) coupled online to an Orbitrap Elite mass spectrometer (Thermo Fisher Scientific). Peptides were concentrated and desalted on a Symmetry C18 preparative column (20 mm × 180 μm, 5-μm particle size; Waters) and separated on a bridged ethyl hybrid C18 analytical column (250 mm × 75 μm, 1.7-μm particle size; Waters) using a 45-min linear gradient from 1% to 25% or 8% to 33% (v/v) acetonitrile in 0.1% (v/v) formic acid at a flow rate of 200 nl/min. Peptides were selected for fragmentation automatically by data-dependent analysis.
Horton E.R., Byron A., Askari J.A., Ng D.H., Millon-Frémillon A., Robertson J., Koper E.J., Paul N.R., Warwood S., Knight D., Humphries J.D, & Humphries M.J. (2015). Definition of a consensus integrin adhesome and its dynamics during adhesion complex assembly and disassembly. Nature cell biology, 17(12), 1577-1587.
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2

Proteomic Analysis via SDS-PAGE and LC-MS/MS

Cited 1 time
Check if the same lab product or an alternative is used in the 5 most similar protocols
Following SDS-PAGE, gel lanes were sliced and subjected to in-gel digestion with trypsin58 (link) with modifications11 (link). Peptide samples were analysed by liquid chromatography (LC)-tandem MS using a nanoACQUITY UltraPerformance LC system (Waters) coupled online to an LTQ Velos mass spectrometer (Thermo Fisher Scientific) or using an UltiMate 3000 Rapid Separation LC system (Thermo Fisher Scientific) coupled online to an Orbitrap Elite mass spectrometer (Thermo Fisher Scientific). Peptides were concentrated and desalted on a Symmetry C18 preparative column (20 mm × 180 μm, 5-μm particle size; Waters) and separated on a bridged ethyl hybrid C18 analytical column (250 mm × 75 μm, 1.7-μm particle size; Waters) using a 45-min linear gradient from 1% to 25% or 8% to 33% (v/v) acetonitrile in 0.1% (v/v) formic acid at a flow rate of 200 nl/min. Peptides were selected for fragmentation automatically by data-dependent analysis.
Horton E.R., Byron A., Askari J.A., Ng D.H., Millon-Frémillon A., Robertson J., Koper E.J., Paul N.R., Warwood S., Knight D., Humphries J.D, & Humphries M.J. (2015). Definition of a consensus integrin adhesome and its dynamics during adhesion complex assembly and disassembly. Nature cell biology, 17(12), 1577-1587.
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3

In-Gel Trypsin Digestion and LC-MS/MS Analysis

Cited 1 time
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Following SDS–PAGE, entire gel lanes were sliced into 30 pieces per lane and subjected to in-gel digestion with trypsin as described7 (link). Peptide samples were analysed by liquid chromatography-tandem MS using a nanoACQUITY UltraPerformance liquid chromatography system (Waters) coupled online to an LTQ Velos (Thermo Fisher Scientific). Peptides were concentrated and desalted on a Symmetry C18 preparative column (20 mm × 180 μm inner diameter, 5-μm particle size; Waters) and separated on a bridged ethyl hybrid C18 analytical column (250 mm × 75 μm inner diameter, 1.7-μm particle size; Waters) using a 45-min linear gradient from 1 to 25% (v/v) acetonitrile in 0.1% (v/v) formic acid at a flow rate of 200 nl min−1. Peptides were selected for fragmentation automatically by data-dependent analysis.
Byron A., Askari J.A., Humphries J.D., Jacquemet G., Koper E.J., Warwood S., Choi C.K., Stroud M.J., Chen C.S., Knight D, & Humphries M.J. (2015). A proteomic approach reveals integrin activation state-dependent control of microtubule cortical targeting. Nature Communications, 6, 6135.
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4

Proteomics Workflow: SDS-PAGE to MS/MS

Cited 1 time
Check if the same lab product or an alternative is used in the 5 most similar protocols
Following SDS–PAGE, gel lanes were sliced and subjected to in-gel digestion with trypsin42 (link) with modifications43 (link). Peptide samples were analysed by liquid chromatography (LC)-tandem MS using a nanoACQUITY UltraPerformance LC system (Waters) coupled online to an LTQ Velos mass spectrometer (Thermo Fisher Scientific) or using an UltiMate 3000 Rapid Separation LC system (Thermo Fisher Scientific) coupled online to an Orbitrap Elite mass spectrometer (Thermo Fisher Scientific). Peptides were concentrated and desalted on a Symmetry C18 preparative column (20 mm × 180 μm, 5-μm particle size; Waters) and separated on a bridged ethyl hybrid C18 analytical column (250 mm × 75 μm, 1.7-μm particle size; Waters) using a 45-min linear gradient from 1% to 25% or 8% to 33% (v/v) acetonitrile in 0.1% (v/v) formic acid at a flow rate of 200 nl min−1. Peptides were selected for fragmentation automatically by data-dependent analysis. The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium via the PRIDE44 (link) partner repository with the dataset identifier PXD017913 (pending publication).
Randles M.J., Lausecker F., Humphries J.D., Byron A., Clark S.J., Miner J.H., Zent R., Humphries M.J, & Lennon R. (2020). Basement membrane ligands initiate distinct signalling networks to direct cell shape. Matrix Biology, 90, 61-78.
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