Go beyond with Orbitrap Tribrid MS for large and small molecule analysis
Built on revolutionary Thermo Scientific Tribrid architecture that combines the best of quadrupole, Orbitrap, and linear ion trap mass analyzers, Orbitrap Tribrid mass spectrometers enable high throughput analyses of challenging samples.
These include accurate and precise quantitation of low-abundance peptides in complex matrices, characterization of structural isomers, from drug metabolites to intact proteins, resolution of isobaric species, and native protein complexes structure characterization.
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Look inside an Orbitrap Tribrid Mass Spectrometer
The architecture inside of an Orbitrap Tribrid mass spectrometer enables a broad range of experimental applications from discovery to profiling and quantification, expediting scientific advancements while offering experimental flexibility, all on a single instrument.
Explore our Orbitrap Tribrid instruments
Orbitrap Eclipse Tribrid MS
Thermo Scientific Orbitrap Eclipse Tribrid Mass Spectrometer is our flagship Orbitrap Tribrid instrument, designed for the highest performance across a wide range of applications. It was developed to produce the best results in quantitative proteomics, protein characterization and small molecule analysis. It features the latest, most innovative hardware, intelligent instrument control with the possibility of real-time database search, and an impressive set of optional functionalities, including the most recent high mass range MSn (HMRn) for native protein complex characterization and proton transfer charge reduction (PTCR) for complex spectra simplification through charge manipulation.
One of the most impressive recent advancements in cell biology research is a single cell analysis. Comprehensive characterization of single-cell proteomes has a promise to provide a wealth of novel information about cellular development in the context of disease progression and response to treatment as a function of cell type. Recently Professor Ryan Kelly, at Brigham Young University, in collaboration with our company, developed an integrated workflow for single cell analysis, allowing for high throughput accurate quantitation of thousands of proteins in a single cell.
“A revolution in single-cell proteomics is just beginning. The combination of nanoPOTS with the Orbitrap Eclipse Tribrid mass spectrometer, TMT reagents, and SPS MS3 with Real-Time Search provide the depth of coverage, quantitative accuracy, and throughput needed to propel this nascent field forward.”
Professor Ryan Kelly, Brigham Young University, UT
Dr. Erwin Schoof, Head of Proteomics Facility,
Technical University of Denmark Postdoctorial Fellow, Copenhagen University
Dr. Ryan Kelly, Associate professor
Chemistry and Biochemistry, Brigham Young University
Dr. Erwin Schoof, Head of Proteomics Facility,
Technical University of Denmark Postdoctorial Fellow, Copenhagen University
Dr. Ryan Kelly, Associate professor
Chemistry and Biochemistry, Brigham Young University
Orbitrap ID-X Tribrid MS
Thermo Scientific Orbitrap ID-X Tribrid Mass Spectrometer is our premier Orbitrap Tribrid MS dedicated to the analysis of small molecules. Utilizing multiple modes of fragmentation, intelligent data acquisition with AcquireX, HRAM Orbitrap spectra at MSn levels, and annotation of unknowns with the mzLogic algorithm, it facilitates comprehensive structural characterization of unknowns in a wide variety of applications ranging from forensics to metabolomics.
Recently, the Orbitrap ID-X Tribrid MS was used to detect flavonoids in the freshwater algae Penium margaritaceum. Chen Jiao and coworkers were able to show the presence of these UV-absorbing compounds, which are typically found only in land plants, and provide potential insight on the development of the first terrestrial plant life.
Dr. Sheng Zhang, Director
Proteomics Facility and Metabolomics Facility, Cornell University
Dr. Sheng Zhang, Director
Proteomics Facility and Metabolomics Facility, Cornell University
Orbitrap Fusion Lumos Tribrid MS
Thermo Scientific Orbitrap Fusion Lumos Tribrid mass spectrometer delivers unprecedented sensitivity, selectivity and versatility to enable life scientists to obtain high quality data. It is designed to pursue difficult analyses, including multiplexed quantitation of low-abundance peptides in complex matrices, characterization of positional isoforms of intact proteins, resolution of isobaric metabolites, protein structure characterization using chemical crosslinking and deep mining of challenging post-translational modifications.
Recently, the Orbitrap Fusion Lumos mass spectrometer was used to characterize DNA-protein crosslinking in Escherichia coli engineered to use methanol as a source of carbon. Researchers from UCLA showed that cultures inoculated from the stationary phase exhibited exceedingly long lag phases. Identification and quantification of DNA-crosslinked proteins provided insight on the possible causes of cell death and potential disruption to the transcription and translation processes that would explain this observation.
Orbitrap Fusion Tribrid MS
Thermo Scientific Orbitrap Fusion Tribrid MS is easy to use, yet sophisticated. The Tribrid architecture combined with multiple fragmentation methods (HCD/CID/ETD) and intuitive instrument control allow for a wide range of experiments, which have been successfully carried out to test hypotheses in many areas of biomedical research including protein turnover, PTM analysis, enzymatic activity, subcellular localization, protein-protein interactomics, growth factor signaling activation, and profiling cellular differentiation.
The Orbitrap Fusion MS was recently deployed to investigate the role of phosphorylation in the regulation of lipid metabolism. Martinez-Montanes and co-workers performed a series of proteomic and lipidomic experiments on the yeast Saccharomyces Cerevisiae during different phases of its lifecycle. In doing so, they were able to show significant links between protein phosphorylation and multiple pathways in the lipid metabolic network.
Dr. Pierre Thibault, Professor
Department of Chemistry, Faculty of Arts and Sciences, University of Montreal
Dr. Pierre Thibault, Professor
Department of Chemistry, Faculty of Arts and Sciences, University of Montreal
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High-Field Asymmetric waveform Ion Mobility Spectrometry (FAIMS) can be used to optimize ion selectivity and reduce chemical backgrounds during mass spectrometry assays. FAIMS successfully prevents interferences from co-eluting compounds and increases signal to noise ratios by 100-fold or higher.
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