PRIME™, Proteomics via Integrated MALDI and ESI

5 Sept 2011
bridget bridget
Laboratory Director

Bruker has introduced PRIME™ (PRoteomics via Integrated MALDI and ESI), a new integrated solution for proteomics, which was showcased at the 10th HUPO World Congress in Geneva.

The Proteome has turned out to be far more complex than expected at the beginning of the proteomics revolution. Complex protein dynamics in time, localization and concentration, as well as extreme structural variability due to modifications and mutations require novel, complementary and integrated approaches to generate the most useful, reliable and complete proteomics information. Bruker’s PRIME solution enables integrated approaches for modern proteomics and harnesses the strengths of MALDI and ESI mass spectrometry technologies, as well as state of the art bioinformatics. This results in enhanced protein identification, structural information, distribution and quantitative information, for data rich interpretation of the proteome.

For MALDI imaging, now emerging as an important applied proteomics tool, PRIME provides a complete top-down based workflow for biomarker discovery and identification from sample preparation to localization, data analysis and interpretation. Intact protein analysis for the elucidation of post-translational modifications is also fully integrated within the PRIME solution with stable and reliable second-generation Electron Transfer Dissociation (ETD) methodologies available. The core technology of PRIME is ProteinScape™, Bruker’s proteomics database system, enabling data analysis at a high level of efficiency for protein identification, quantitation and PTM characterization. This constantly evolving bioinformatics suite manages and merges data from MALDI and ESI workflows and has now been further enhanced with the powerful new GlycoQuest™ database search for glycan structure identification. This complements the conventional peptide database search tools and provides complete glycopeptide identification within the evolving field of glycomics.

“Bruker has been at the leading edge of mass spectrometry based proteomics since the outset and continues innovating to match this rapidly evolving field,” commented Dr. Detlev Suckau, Head of MALDI-Applications Development and Proteomics at Bruker. “Our integrated ESI and MALDI instruments together today identify around 2,500 non-redundant proteins in the bottom-up analysis of cell lysates in merged data sets with a FDR <1%. Combining this highest performance with tools including complementary top-down intact protein measurements generates valuable knowledge about the complete protein, including sequence, splicing or proteolytic processing variants and post-translational modifications (PTMs).”

Bruker’s PRIME solution delivers instruments and workflows for bottom-up, top down and PTM studies, quantitation and imaging, integrating a range of technologies including MALDI-TDS, Ion Trap ETD and high resolution UHR-ESI-QTOF, all anchored to the bioinformatics core, Proteinscape.

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