Waters Corporation Brings High Definition to Proteomics at HUPO 2007
Product News Oct 10, 2007
At the Human Proteome Organization’s 6th Annual World Congress, Waters Corporation is showcasing several technologies expected to give proteomics researchers new insights into the workings of the human proteome.
• Waters Synapt™ High Definition Mass Spectometry™ System – Differentiating Ions by Size, Shape, and Charge as Well as Mass
The Waters® Synapt HDMS™ System is intended for researchers working at the limits of conventional mass spectrometry (MS) and who need to further characterize and define their samples.
The Synapt HDMS system is the first mass spectrometer of its kind to employ high efficiency ion-mobility based measurements and separations and specialized software to enable the analysis of sample ions differentiated by size, shape and charge as well as mass. This additional dimension of separations fidelity leads to improved specificity and sample definition, meaning scientists can extract more information about their samples including the detection of previously unseen constituents.
• Waters IdentityE High Definition Proteomics System for Label-Free Protein Identification
The Waters® IdentityE High Definition Proteomics™ System is an UltraPerformance LC® (UPLC)/High-Bandwidth Mass Spectrometry (MSE) system solution designed for protein identification and to meet stringent requirements as outlined by leading scientific journals.
The Waters IdentityE High Definition Proteomics System catalogs complex protein digest mixtures containing tens of thousands of peptides. The system features a Waters nanoACQUITY® UltraPerformance LC(UPLC®) System for high chromatographic peak capacity and retention time reproducibility, together with an electrospray tandem mass spectrometer - Waters Q-Tof Premier™ or Waters Synapt HDMS - for high dynamic mass resolution and consistent over-sampling of complex protein digests – two hallmarks of high definition proteomics.
• HUPO Dinner Forum to Feature Presentations from World Class Scientists
Waters is hosting a dinner forum where invited speakers will present on novel techniques for protein identification. The agenda features scientists from European and Korean institutions in the area of protein research.
• Identification, Quantification and Annotation of Heart Membrane Proteins Using IdentityE, Prof. Mike Dunn, UCD, Dublin, Ireland
• Analysis of Post-Translational Modifications by Ion Mobility and Mass Spectrometry, Prof. Ole N. Jensen, University of Southern Denmark
• A Strategy for Comprehensive Identification of Post-translational Modifications in Cellular Proteins Including Low Abundant Modifications, Prof. Kong-Joo Lee, Ewha Womans University, Korea
• Waters Poster Presentations
Waters scientists are presenting several posters at HUPO. Copies of the posters will be available for downloading from Waters web site shortly after HUPO concludes.
• Separation and Detection of Protein Post-Translational Modifications by Liquid Chromatography Coupled With a Novel Ion Mobility Mass Spectrometer, Mark Ritchie; Chris Hughes; Therese Mckenna, James Langridge, Waters Corp. MS Technologies Centre, Manchester, United Kingdom
• Top Down Sequence Analysis of Intact Proteins Using Ion Mobility Coupled With Time-of-Flight Mass Spectrometry, Therese McKenna, James Langridge, Christopher J Hughes, Waters Corp. MS Technologies Centre, Manchester, United Kingdom
• High Speed Nanoscale UPLC Separations Combined With Off-line MALDI MS/MS for Peptide Analysis, James I Langridge; Marten Snel, Emmanuelle Claude, Roy Martin, Therese McKenna, Waters Corp. MS Technologies Centre, Manchester, United Kingdom
• Identification, Quantification and Annotation of Heart Membrane Proteins Using Label-Free Nanoscale LC-MS, Pamela M. Donoghue1, Johannes P.C. Vissers2, James I. Langridge2, Michael J. Dunn3;1 Immune Regulation Research, Trinity College Dublin, 2 Waters Corporation, MS Technologies Center, Manchester, UK, 3 Proteome Research Centre, UCD Conway Institute, University College Dublin
• Sequencing and Characterization of Human Histones by Ion Mobility Tandem Mass Spectrometry, Ms. Hye Ryung Jung1, Chris Hughes2, Therese McKenna2, James Langridge2, Prof. Ole N Jensen1, 1University of Southern Denmark; 2Waters Corporation.