Vendor Seminare

Mittwoch, 1. Juli 2015

Seminarraum 1

12:00 – 13:30 h

 

 

 

           

 

"PeptiQuant: Multiplex Protein Quantitation by MRM"

Christoph Borchers Ph.D,

Director of University of Victoria Genome British Columbia Proteomics Centre, CSO MRM Proteomics Inc.

 

 

 

Das Agilent IMS QTOF – „Funktionweise und eine ganze Liste von Vorteilen“

Dr. Volker Gnau

Product Specialist Mass Spectrometry, Agilent Technologies

 

 

 

 

 

 

Dienstag, 30. Juni 2015   

Seminarraum 1

12.45 - 14.15 h

 

 

Not just a label: application of Isotope-Coded Protein Label (ICPL) in radiation proteomics

Dr. Omid Azimzadeh, Hemholtz Institut, München,

Comprehensive proteomics analysis provides a hypothesis-generating means to identify undiscovered biological pathways involved in the radiation response. Progress made in quantitative proteomics enables the investigation of transcriptional and translational regulators and detection of posttranslational modifications.
The aim of this presentation is to introduce the recent developments in the field of radiation proteomics focussing on the application of Isotope-Coded Protein Label (ICPL) in tissue proteomics with the advantages and challenges of this method.

 

 

Quantitative Bestimmung von Harnproteinen zur frühen Erkennung der Präeklampise

Dr.  Goran Mitulović, Medizinische Universität Wien

Präeklampsie ist eine der gefährlichsten hypertensiven Erkrankungen, die  während der Schwangerschaft auftreten kann. Die aktuelle Studie an der Medizinischen Universität Wien beschäftigt sich mit der Entdeckung und Quantifizierung von möglichen Biomarkern für Präeklampsie im Harn. Klassische Proteomics Methoden und ICPL-Quantifizierung wurden angewandt. Insgesamt wurden 584 Proteine im Harn nachgewiesen. Zur Quantifizierung wurden nur die Proteine ausgewählt, welche mehr als drei quantifizierbare Peptide beinhaltet. Unter diesen Proteinen waren 34 Proteine, welche signifikant höhere Expression zeigten und 57 Proteine, welche signifikant weniger exprimiert wurden. Unsere Ergebnisse bestätigten die bereits bekannten Ergebnisse, zeigen aber auch neue Proteine. Diese Proteine könnten sowohl in der Akutphase und in der Immunantwort während der Präeklampsie involviert sein. Was auch sehr wichtig ist, ist die Anwesenheit vieler Plasmaproteine, was auf eine massive Schädigung der Glomerulomembran deutet.

 

 

Identifizierung und Charakterisierung von SSX2IP, einem wichtigen Faktor für Zentrosom-Reifung

Dr. Thomas Ruppert, ZMBH, Heidelberg

Die Meisose in Xenopus ist ein exzellentes Modell, um die Reorganisation von Mikrotubuli während der Spindelbildung zu untersuchen. Wir untersuchten die Änderung des Panels Mikrotubuli bindender Proteine während der Reifeteilung. Stabile Isotopenmarkierung der an Mikrotubuli angereicherten Proteine mit ICPL und quantitative Massenspektrometrie führte zur Identifikation von synovial sarcoma X breakpoint protein (SSX2IP) als neuem Spindelprotein. Funktionelle Studien zeigten, dass SSX2IP in Dynein abhängiger Weise an den Spindelpolen akkumuliert und mit dem Gamma-Tubulin-Ring-Komplex und dem perizentrosomalen Satellitenprotein PCM1 interagiert.  SSX2IP ist notwendig für Zentrosomenintegrität und kontrollierte Mitose.

 

 

Neue Möglichkeiten der Fluoreszenz-Markierung und gelbasierten Detektion von Proteinen

Günter Theßeling, SERVA Electrophoresis GmbH, Heidelberg

Günter Theßeling stellt in seinem Vortrag neue Möglichkeiten der Fluoreszenz-Färbung und Markierung zur Detektion von Proteinen bei der Gelelektrophorese vor. SERVA präsentiert neue Farbstoffe und ein neues bildgebendes Gerät für die Auswertung von Fluoreszenz-basierenden Proteinelektrophoresen bei verschiedenen Wellenlängen. Das neue System bietet diese Möglichkeiten in einem vorher nicht bestehenden preislichen Rahmen – damit wird Fluoreszenz-Empfindlichkeit und -Linearität für jede Arbeitsgruppe zugänglich.

 

Mittwoch, 1. Juli 2015

grosser Saal

12.00 - 13.30 h

 

 

 

 

Identification of protein-protein crosslinks in macromolecular assemblies

Olexandr Dybkov

Max Planck Institute for Biophysical Chemistry, Göttingen, Germany

Chemical crosslinking combined with mass spectrometry (XL-MS) is a very potent technique to study molecular interactions. Crosslinkers can covalently bind proximal residues “freezing” the contact sites and enabling the detailed analysis of interactions within multimeric complexes. Recent advances in MS instrumentation have made it possible to efficiently identify protein-protein crosslinks formed in large and dynamic macromolecular complexes. Combining the results of XL-MS with low resolution structures of the molecular machines as well as high resolution structures of their components contributes significantly to our understanding of structures, functions and mechanisms of their actions.

 

Getting the most of the TMT Tool Box

Dr. Christopher Lößner

Proteome Sciences

Bereits 2003 wurde mit Tandem Mass Tags eine neue Quantifizierungsstrategie entwickelt, die seitdem ständig weiterentwickelt und verbessert wird. In diesem Vortrag werden Ihnen die vielfältigen Reaktivitäten von TMT Reagentien, die parallele Quantifizierung von bis zu zehn Proben sowie neueste Optimierungen bei der Datenakquisition und Auswertung präsentiert.

 

Orbitrap Fusion Lumos Tribrid Mass Spectrometer: the latest developments and applications

Dr. Patrick Pankert

Thermo Fisher Scientific

 

Dienstag, 30. Juni 2015

grosser Saal

12.45 - 14.15 h 

 

 

 

 

Higher-order structure characterization of protein G´-derivatives** by ion mobility mass spectrometry

Prof. Dr. Michael O. Glocker

Director, Proteome Center Rostock

Department for Proteome Research

Institute of Immunology

University Rostock Medical Center and Natural Science Faculty

University of Rostock

 

 

Application Benefits of the Contribution if Ion Mobility to DIA, DDA and MRM LC-MS Schema and Assays

Dr. Marc Kipping, Waters GmbH

 

 

 

 

Montag, 29. Juni 2015

grosser Saal

12:30 – 14:00 h

 

 

 

 

Robust, powerful and easy to implement analytical solutions for Protein research

 

Glycoproteomics: getting ready for the next analytical challenge in Life Science

Pierre-Olivier Schmit, Bruker Daltonique, France

Protein glycosylation is a process involved in many major biological events, like cell recognition, cell adhesion, immune and inflammatory reactions and many others. It can be influenced by various factors like sex, age, and tissue type or health status. This makes glycoproteins highly relevant compounds to focus on when it comes to the search for candidate biomarkers or candidate therapeutic targets.

Mass spectrometry, on the other hand, is one of the most sensitive and powerful approach to detect, identify and characterize glycoproteins. However, the limited ionization efficiency, and the combinatorial nature of glycoconjugates, makes it difficult to get a fully informative fragmentation pattern and complicates its analysis. These challenges have to be addressed in order to target glycoproteins as potential candidate biomarkers.

In this talk we will describe how we deal with these obstacles when using the latest proteomics analysis solution based on the Impact II UHR-Q-TOF. A special focus will be made on glycopeptide analysis and on the solutions which have been developed to increase their ionization efficiency, to obtain meaningful MS/MS in an LC timescale and to facilitate their analysis while using dedicated bioinformatics tools. These features will be illustrated with application examples.

 

rapifleX MALDI Tissuetyper™ - A New instrument for Megapixel Tissue Imaging at High Speed

Michael Becker, Bruker Daltonik GmbH, Germany

Currently, acquisition speed and spatial resolution are major limitations of MALDI imaging experiments. We have addressed these limitations with a new instrument which allows acquisition speeds up to 50 pixels/second at 10 µm resolution.

The rapifleX, is based on the newly developed smartbeam 3D laser. This 10 kHz laser employs an aspherical lens to project a Gaussian laser spot of less than 5 µm diameter. A pair of rotating mirrors allows fast and precise positioning of the laser spot on the sample. These capabilities are used to acquire imaging data from quasi-square, non-overlapping pixels, increasing overall data quality and pixel-to-pixel reproducibility.

Combined with re-designed acquisition and analysis software, the rapifleX allows acquisition of large sample sets, 3D MALDI Imaging and true Megapixel images in a reasonable timeframe.

We present results using the new instrument for the common application fields of mass spectrometric imaging, among them the analysis lipids, tryptic peptide, and intact protein distributions.

 

Evaluation of quadrupole time-of-flight mass spectrometry platform for qualitative and quantitative proteomics

Pierre-Olivier Schmit, Bruker Daltonique, France

Recent technological advances, both at the hardware and software levels, have redefined last generation Qtofs performance levels and have given them access to an extremely wide range of applicative fields. Their ability to deal with high concentration of ions enable them to reach impressive levels of intra-spectral dynamic range. Their capacity to offer a speed-independent high resolution in MS and MS/MS ensures compatibility with fast separation devices and has enables the development of new acquisition strategies like DIA.

The impact II is the synthesis of these latest advances in a benchtop format, capable of delivering o resolution of 50000 @ 1200 m/z without compromising sensitivity or acquisition speed, or of preserving an accurate isotopic profile while measuring a complex mixture of intact proteins. The robustness of the system makes them compatible with large scale-omics analysis.

These analytical features, combined to the use of last generation software, are supporting a wide panel of complementary biologically relevant applications. In this presentation, we will illustrate how these technological advances are permitting to reach an extremely high ratio determination accuracy while digging deep into the proteome complexity, and how they are opening new applications that are complementary to the traditional bottom-up approaches.

 

Bitte registrieren Sie sich hier für das Lunch Seminar:

https://www.bruker.com/events/2015/mikromethoden-proteinchemie-lunch-seminar.html

Montag, 29. Juni 2015 

Seminarraum 1 

12:30 – 14:00 h

 

 

 

Combined Targeted Analysis of Proteins and Metabolites in Biosamples

Dr. Sascha Dammeier

Medical Proteome Center, Centre for Ophthalmology

University of Tübingen

 

 

 

Next-Generation Proteomics and the OneOmics™ Project:

From MS Data Acquisition to Biological Answers

Dr. Marcus Macht

Sciex Deutschland

Darmstadt