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Join us at the 5th International Congress on Analytical Proteomics | 3-6 July, Costa de Caparica, Portugal
Meet our scientists and representatives at booth #2 to learn more and discuss how we can partner with you to identify proteins faster and more accurately, so you can go beyond the limit of what was ever thought possible.
Register today to attend our lunch seminar on Tuesday, July 4th | 01:00 – 02:00 PM
In-depth and reproducible protein measurement especially with many biological/individual replicates is critical for pharmaceutical/clinical proteomics, but remains highly challenging owing to suboptimal accuracy, reproducibility and false-positive-biomarker-discovery, and high levels of missing data. MS2-based Data-Independent-Acquisition(MS2-DIA) approaches were developed to lower missing values but often with limited depth. To address these challenges, we developed an “IonStar” workflow consisting of experimental components based on the use of an Ultra-high-field Orbitrap and a data processing pipeline to take full advantage of high-resolution MS1 ion-current-based quantification, which achieves accurate, precise and in-depth protein quantification with low-missing-values in large cohorts. This pipeline was thoroughly compared to popular methods including spectral counting, OpenMS and Maxquant, using a 5-group, 20-replicates benchmark sampleset. IonStar showed by far the most in-depth analysis, best accuracy, lowest intra-group-variation(~5%CV vs.11-18% by others), missing data(<0.2% vs.18-44%) and false-positive-biomarker-discovery-rate(<4% vs.7-31%), with quantified protein abundances spanning ~5.8 orders of magnitudes(vs.3.2-4.4). As applications, we quantified >6000 protein groups, >99% without missing data, in large biological cohorts (50-100 samples).
Speaker: Jun Qu, University at Buffalo, Buffalo, NY, USA
Chemical cross-linking combined with mass spectrometry (CX-MS) is a powerful method to probe the structure of proteins, complexes and interactions. The high resolution and mass accuracy of Orbitrap technology, in combination with enhanced fragmentation modes (e.g., HCD, ETD, EtHCD) and MSn modalities, allow completely unique and effective methods to probe protein structure. New reagents and software facilitate sample preparation and data interpretation to make these capabilities available to all labs.
Speaker: Sega Ndiaye, Thermo Fisher Scientific, France
Lunch will be provided. Event is free but registration is mandatory.