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Bruker Daltonics Introduces Several Important and Novel Proteomics Capabilities and Solutions at HUPO 2007.


SEOUL, South Korea -- At the Human Proteome Organisation's (HUPO HUPO Human Proteome Organisation ) 6th Annual World Congress, Bruker Daltonics is announcing several novel capabilities and solutions for proteomics mass spectrometry at two Bruker luncheon seminars on Monday and Wednesday, as well as in more than 40 scientific oral and poster contributions.

Bruker Daltonics was the first company to introduce ETD ETD
abbr.
estimated time of departure

Noun 1. ETD - a system for screening luggage in airports; an agent passes a swab around or inside luggage and then runs the swab through a machine that can detect trace amounts of
 (Electron Transfer Dissociation Electron transfer dissociation (ETD) is a method to fragment ions in a mass spectrometer.[1][2] Similar to electron capture dissociation, ETD induces fragmentation of cations (e.g. peptides or proteins) by transferring electrons to them. ) on its commercial high-capacity trap, and has by far the largest number of successful ETD customer installations. With the release of its new Compass[TM] 1.3 ion trap software, Bruker's high-capacity trap HCTultra PTM PTM Post-Translational Modifications
PTM Porsche Traction Management
PTM Point-To-Multipoint
PTM Please Tell Me
PTM Packet Transfer Mode
PTM Pulse-Time Modulation
PTM Portugal The Man (band)
PTM Predictive Technology Model
 Discovery System[TM] becomes the first commercial mass spectrometer fully equipped with both ETD and PTR PTR Pointer (as used in DNS records; an address points to a name)
PTR Partner
PTR Painter
PTR Proton Transfer Reaction
PTR Pupil/Teacher Ratio
PTR Public Test Realm (gaming, World of Warcraft) 
 (Proton Transfer Reaction). Using a unique and innovative ion optics design and chemistry setup for ETD/PTR allows rapid, routine top-down characterization of large peptides and mid-size proteins in the high-capacity ion trap with superior sensitivity.

The usefulness of ETD/PTR is demonstrated impressively by the unambiguous characterization of post-translational modifications. Compass 1.3 also introduces a novel CID Cid or Cid Campeador (sĭd, Span. thēth kämpāäthōr`) [Span.,=lord conqueror], d. 1099, Spanish soldier and national hero, whose real name was Rodrigo (or Ruy) Díaz de Vivar.  fragmentation mode, called PAN[TM], which eliminates the low mass cut-off of ion traps in MS/MS MS/MS Tandem Mass Spectroscopy
MS/MS Multistage Mass Spectrometry
. It enables multiplexed quantitative proteome analyses by, e.g. iTRAQ[TM] labelling chemistry, on Bruker's high-capacity ion trap systems. Moreover, a new AutoMSn mode in Compass 1.3, called "ActiveEjection", automatically eliminates the most abundant ions in order to further enhance dynamic range.

Finally, "Scheduled Target Lists" in Compass 1.3 extend the number of possible MRM MRM Marketing Resource Management
MRM Mobile Resource Management
MRM Metabolic Response Modifiers
MRM Multiple Reaction Monitoring (mass spectrometry)
MRM Mormonism Research Ministry
MRM Mechanically Recovered Meat
 transitions per run. This new dynamic scheduling allows monitoring hundreds of target compounds in parallel for large scale biomarker validation studies or for pesticide, drug and doping screening.

With its new ProteinScape[TM] 2 software, Bruker Daltonics introduces a next-generation bioinformatics platform addressing scientists' current needs in biomarker profiling, quantification and validation. As a comprehensive solution for qualitative and quantitative LC-MS/MS protein analysis, ProteinScape 2 supports all current label chemistries including multiplexed labels, as well as label-free quantification. Interactive validation of protein quantification based on raw LC/MS LC/MS Liquid Chromatography/Mass Spectrometry  data is simple and straight forward. It streamlines the discovery process through decoy auto-validation algorithms and the ProteinExtractor[TM] algorithm that produces non-redundant protein result lists across entire proteomics projects.

ProteinScape 2 has a number of dedicated data viewers that permit the evaluation and validation on each level of proteomics experiments, such as the LC/MS survey viewer, the gel viewer and sequence-annotated MS/MS spectra. All these views are linked and permit simple browsing through scientists' proteomics data, supported by extensive queries. It also allows the retrieval of data generated years ago, allowing their joint re-analysis with novel analytic capabilities and mining tools.

The ProteinScape 2 processing pipeline adopts the "HUPO Brain Proteomics Project processing guidelines" (forum.hbpp.org) and eventually will facilitate the direct submission process of project data adhering to HUPO/PSI publishing guidelines.

Recent data on biomarker discovery, obtained with the Bruker Daltonics MALDI MALDI Matrix-Assisted Laser Desorption/Ionization  Molecular Imager[TM] system, demonstrates the power of direct tissue analysis by MALDI-TOF MALDI-TOF Matrix Assisted Laser Desorption Ionization - Time of Flight  and MALDI-TOF/TOF, such as the ultraFlex[TM] III TOF/TOF shown here. The complete Bruker solution comprises the new ImagePrep[TM] device for automated high-resolution matrix application on tissue, the unique SmartBeam[TM] laser technology and the proprietary ClassImaging[TM] algorithm for tissue classification and biomarker detection, molecular histology as well as imaging of drug and metabolite distributions in drug development.

Dr. Arnd Ingendoh, Assistant Vice President for Proteomics, commented: "Our introductions at this year's HUPO Congress show the major commitment of Bruker Daltonics to innovative, far reaching proteomic applications. We are focusing on some of the most important areas to proteomics scientists like high-sensitivity PTM discovery, as well as biomarker discovery, quantification and rigorous validation."

Clive Seymour, Bruker Daltonics' Vice President for Asia and the Pacific, added: "ETD on our Paul high-capacity trap is revolutionizing proteomics mass spectrometry, as demonstrated by the very substantial success our HCT-Ultra has in the proteomics market. We believe that the simplicity and vastly improved sensitivity of doing ETD in a Paul 3D high-capacity trap, which by its very nature traps positive and negative ions at the center of the our unique ion trap configuration, makes our ETD implementation by far the most robust, most sensitive, fastest and most useful ETD implementation on the market. I cannot imagine any future cutting-edge proteomics laboratory without the dramatic new capabilities for de novo sequencing, greater sequence coverage, and most importantly, facile, sensitive, and fully automated PTM discovery and localization. ETD on a high-capacity Paul 3D trap is a nearly ideal combination for modern proteomics research."

The Bruker Daltonics' Luncheon Seminars will be held on Monday, October 8th at 1:10-2:20 pm, and on Wednesday, October 10th, at 1:10-2:20 pm, in Jangbogo Hall 332, Level 3, COEX. Invited speakers include Helmut Meyer from the Medical Proteome Center of Bochum University/Germany, Pierre Chaurand from Vanderbilt University, Nashville, TN/USA, and Thomas Franz from the EMBL EMBL European Molecular Biology Laboratory
EMBL Eniwetok Marine Biological Laboratory
 Heidelberg in Germany. For more information, please visit www.bdal.com/hupo.

ABOUT BRUKER BIOSCIENCES (NASDAQ NASDAQ
 in full National Association of Securities Dealers Automated Quotations

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: BRKR BRKR Breaker )

Bruker BioSciences Corporation Bruker Biosciences Corporation is a Massachusetts-based company formed in 2003 which develops and manufactures scientific instrumentation for academic research and industrial use.  in Billerica, Massachusetts, is the publicly traded parent company of Bruker AXS Inc., Bruker Daltonics Inc. and Bruker Optics. Bruker Daltonics is a leading developer and provider of innovative life science tools based on mass spectrometry. For more information, please visit www.bdal.com or www.bruker-biosciences.com

Trademarks: iTRAQ is a trademark of Applera Corporation
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Date:Oct 7, 2007
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