Product category:
Spectroscopy software
News Release from: Waters | Subject: PLGS 2.2.5
Edited by the Laboratorytalk Editorial
Team on 14 February 2006
Identify and quantify proteins and
biomarkers
New version of Waters's ProteinLynx Global Server, with enhancements to protein expression system, launched at annual meeting of Association of Biomolecular Resource Facilities, 11-14 February 2006
Waters ProteinLynx Global Server (PLGS) 2.2.5 software features new tools which will allow 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 labelling technologies
This article was originally published on Laboratorytalk on 2 Aug 2004 at 8.00am (UK)
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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, iTraq, etc.
The ability to perform both 'label free' and 'isotopic labeling' approaches now means that PLGS provides unparalleled flexibility to analyse proteomics samples of varying type and complexity, says Waters.
Further reading
Taking liquid chromatography a stage further
Claiming to be the first end-to-end ultra performance liquid chromatography system offering specially designed column chemistries, hardware, software, and documentation
Expanded chromatography control with this software
Acquires data and controls the operation of and processes data from Waters brand instrumentation as well as Agilent photodiode array detectors, liquid chromatographs, and gas chromatographs
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 MSE 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 visualisation 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 and discussed in several posters during the scientific session which will be available online after the conference.
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