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Waters Corporation. (2/11/06). "Press Release: Waters Introduces new Capabilities for Proteomic Research. Company Enhances Bioanalysis Software for Quantitative and Qualitative Research". Long Beach, CA.
|Region||United States (USA)|
|Organisation||Waters Corporation (NYSE: WAT)|
|Organisation 2||ABRF (Association of Biomolecular Resource Facilities)|
|Product||proteomic software tools|
|Product 2||Q-TOF mass spectrometer (Micromass/Waters)|
Waters Corporation is announcing a new version of its ProteinLynx Global SERVER™ software, including enhancements to Waters® Protein Expression System, at the annual meeting of the Association of Biomolecular Resource Facilities (ABRF), February 11 - 14. Waters ProteinLynx Global SERVER (PLGS) 2.2.5 software features new tools allowing researchers to identify and quantify proteins and biomarkers more efficiently.
Waters Protein Expression System, featuring PLGS, was the first commercial product for cost-effective and practical quantitative proteomics without the use of isotope labeling technologies. PLGS 2.2.5 extends this breakthrough technology with improved algorithms for efficient protein quantification and identification across large patient/sample sets or time-course studies.
A new quantification module in PLGS allows quantitative data to be generated at the protein or peptide level using any of the commercially available or user-defined labeling technologies such as SILAC™, AQUA™, ICAT® or iTRAQ™. The ability to perform both 'label free' and 'isotopic labeling' approaches now means that PLGS provides unparalleled flexibility to analyze proteomics samples of varying type and complexity.
PLGS 2.2.5 provides a 'step change' in the ability to identify proteins efficiently in complex samples by incorporating a new algorithm, which enables identification of proteins from MS E data (E - elevated collision energy) acquired from a Q-Tof™ type mass spectrometer. In an LC/MS experiment, a proprietary and patented* 'parallel' peptide fragmentation protocol is employed to provide a 100% duty cycle on all detectable peptides in a protein digest. This new approach results in significantly higher sequence coverage and confidence in protein identification than traditional 'Data Dependent Acquisition' (DDA™) MS/MS methods.
Other enhancements for PLGS 2.2.5 include new data visualization tools that visually depict what happens to the protein concentration over a large number of samples or conditions. These new tools are especially important for researchers performing time-scale studies during which changes in the protein profile are carefully monitored at intervals, e.g. drug time course studies.
Finally, for researchers publishing their scientific findings in peer-reviewed scientific journals, PLGS 2.2.5 will have access to a number of popular formats including peaklist, eXtensible Markup Language (XML) and the mzData Format as required by the Human Protein Organization (HUPO) Proteomics Standards Initiative for Mass Spectrometry.
These and other enhancements being introduced at ABRF 2006 will be discussed in Booth #311 and in several posters during the scientific session available after the conference at www.waters.com/posters.
Increased Proteomic Throughput and Productivity Using a Simple LC/MS Platform
C. A. Dorschel, J. C. Silva, G. Li, M. V. Gorenstein, S. J. Geromanos; Waters Corporation, Milford, MA, United States
The Effect of Cold Shock on A.thaliana: A Proteomics Study from Gel Separated Rosette Leaf Homogenates using Label Free Quantitative LC/MS
M. Ritchie 1 , H. Mock 2, S. Amme 2, J. Langridge 1, T. McKenna 1; 1 Waters MS Technology centre, Manchester, United Kingdom, 2 Institute of Plant Genetics and Crop Plant Research, Gatersleben, Germany
A Combined Proteomic and Metabonomic Approach to Biomarker Discovery for Schizophrenia Using Accurate Mass LC/MS
Therese McKenna, Hilary Major, Christopher Hughes, Jeffrey T.-J. Huang, Sabine Bahn, and James Langridge; Institute of Biotechnology, University of Cambridge, Cambridge, UK Waters Corporation, Manchester, UK
Comparative LC/MS for Quantitative Proteomics Analysis of Tomato-Fungus Interaction
A.H.P. America 1, J.H.G. Cordewener 1, J.P.C. Vissers 2, J.L. Langridge 2, I.J.E. Stulemeijer 3, M.H.A.J. Joosten 3; 1 Plant Research International, Wageningen, The Netherlands, 2 Waters Corporation - MS Technologies Centre, Manchester, United Kingdom, 3 Laboratory of Phytopathology, Wageningen University, Wageningen, The Netherlands
Ischemia-Induced Changes in Protein Expression in Rat and Mouse Brains
M.D. Stapels 1, J.W. Finch 1, J.C. Gebler 1, M. Minami 2, A. Zhou 2; 1 Waters Corporation, Milford, MA, 2 Legacy Research, Portland, OR
A Quantitative Analysis of Complex Peptide Mixtures Derived from Mouse Serum Using Liquid Chromatography Coupled with MALDI MS and MS/MS
G. S. Cavey 1, E. Claude 2, P. Davidson 1, J. I. Langridge 2, T. McKenna 2, D. Monsma 1, M. Snel 2, R. Tyldesley 2,-Worster 2, C. Webb 1; 1 Van Andel Research Institute, Grand Rapids, MI, United States, 2 Waters Corporation, Manchester, United Kingdom
Increased Sequence Coverage of Photosystem II Complex of Barley Using Combined ESI/MALDI Analysis
M. Snel 1, D. Uria 1, E. Claude 1, T. McKenna 1, J. Langridge 1, B. Granvogl 2, V. Reisinger 2, L. A. Eichacker 2; 1 Waters Corporation, Manchester, United Kingdom, 2 Ludwig-Maximillians-Universitaet, Munich, Germany
Quantification of Diagnostic Protein Signatures of Polygenic Diseases Characterized by Mass Spectrometric Proteome Analysis: A Study on Mammalian Carcinoma
J.P.C. Vissers 1, M. Kipping 2, T. Reimer 3, A. Kasten 3, C. Koy 3, J.L. Langridge 1, M.O. Glocker 3; 1 Waters Corporation - MS Technologies Centre, Manchester, United Kingdom, 2 Waters GmbH, Eschborn, Germany, 3 Proteome Center Rostock, Department for Proteome Research, Institute of Immunology, Medical Faculty and Natural Science Faculty, University of Rostock, Germany
The object of proteomics is to quantify as many proteins - whether in small or large concentrations - in a single analysis as possible from a biological sample with the goal of better understanding the effect of drug candidates on the protein "fingerprint" of a dosed subject. By being able to measure which proteins increase or decrease in concentration after the dosing of a subject in early stages of research, scientists know whether or not a drug is having the intended effect. Accurate protein quantification is still the focus among many researchers, with protein identification a secondary goal.
About Waters Corporation
Waters Corporation holds worldwide leading positions in three complementary analytical technologies - liquid chromatography, mass spectrometry and thermal analysis. These markets account for $4.5 - $5.0 billion of the overall $20 + billion analytical instrument market.
* Patents US6717130, GB2363249, US6982414
Waters is a registered trademark and ProteinLynx Global SERVER and Q-Tof are trademarks of Waters Corporation. Progenesis is trademark of Nonlinear Dynamics Ltd. ICAT is a trademark of the University of Washington, U.S. iTRAQ is a trademark of Applied Biosystems. SILAC is a trademark of Invitrogen Corporation. AQUA is a trademark of Harvard University.
Certain statements contained herein are forward looking. Many factors could cause actual results to differ from these statements, including delays in product introductions, loss of market share through competition, introduction of competing products by other companies, pressures on prices from competitors and/or customers, regulatory obstacles to new product introductions, lack of acceptance of new products, changes in the healthcare market and the pharmaceutical industry, changes in distribution of the Company's products, and foreign exchange fluctuations. Such factors are discussed in detail in the Company's filings with the Securities and Exchange Commission and, in particular, the Company's Annual Report on Form 10-K
Record changed: 2016-03-19
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