Samples were analyzed using a Maxis II QTOF instrument (Bruker Daltonik GmbH, Bremen, Germany) equipped with CaptiveSpray nanoBooster ion source coupled to a Dionex UltiMate 3000 RSLCnano system (Sunnyvale, CA, USA). Peptides were separated on an Acquity M-Class BEH130 C18 analytical column using gradient elution (isocratic hold at 4% for 11 min, then elevating B solvent content to 25% in 75 min, and to 40% in 15 min) following trapping on an Acclaim PepMap100C18 trap column. Solvent A consisted of water + 0.1% formic acid, Solvent B was acetonitrile + 0.1% formic acid, and the sample loading buffer was 0.1% TFA and 0.01% HFBA in water.
The MS/MS measurements were carried out in DDA mode. The cycle time was set at 2.5 sec, with a dynamic MS/MS exclusion of the same precursor ion for 2 minutes, or if the intensity is at least 3 times larger. Preferred charge states were set between +2 and +5. MS spectra were acquired at 3 Hz in the 150-2200 m/z range, while MS/MS spectra at 4 or 16 Hz depending on the intensity of the precursor. For single stage MS measurements spectra were recorded over the mass range of 300-3000 m/z at 1 Hz.
[doi:10.25345/C5NZ36]
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: prostate ; prostate cancer ; cancer ; tissue ; tissue microarray ; proteomics ; glycoproteomics ; N-glycosylation
Principal Investigators: (in alphabetical order) |
Lilla Turiak, MS Proteomics Research Group, Research Centre for Natural Sciences, Eotvos Lorand Research Network, Hungary |
Submitting User: | rozmarakiraly |
Simon Sugár, Gábor Tóth, Fanni Bugyi, Károly Vékey, Katalin Karászi, László Drahos, Lilla Turiák.
Alterations in protein expression and site-specific N-glycosylation of prostate cancer tissues.
Sci Rep. 2021 Aug;11(1), 1-12. doi: 10.1038/s41598-021-95417-5.
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