Bruker introduces PRIME multidimensional solution for
unravelling the proteome
20 September 2011
Bruker has announced PRIME (proteomics via integrated MALDI
and ESI), a novel integrated solution for proteomics.
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.
There is no “one size fits all” in unraveling the proteome.
Bruker’s unique PRIME solution leads the way to integrated
approaches for modern proteomics and harnesses the strengths of
MALDI and ESI mass spectrometry technologies, as well as state of
the art bioinformatics, without compromises. This results in
enhanced protein identification, structural information,
distribution and quantitative information, for data rich
interpretation of the proteome.
In the innovative PRIME solution, bottom-up, top-down analyses as
well as in-depth protein characterization merge to illuminate the
true picture of the proteome, complete with biological context and
confidence in data quality and extracted information. Novel
approaches including glycomics, general PTM analysis and MALDI
molecular imaging are fully embedded within workflows attuned to the
evolving sub-fields within the overall proteomics arena.
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 the most stable and reliable second-generation Electron
Transfer Dissociation (ETD) methodologies available.
The core technology of PRIME is ProteinScape, Bruker’s
market-leading proteomics database system, enabling data analysis at
an unsurpassed level of efficiency for protein identification,
quantitation and PTM characterization. This well accepted and
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).”