Catalog Number | Description |
---|---|
0726090 | Thermo Scientific™ Q Exactive™ UHMR Hybrid Quadrupole-Orbitrap™ Mass Spectrometer |
BRE0032840 | Direct Mass Technology™ mode for Thermo Scientific™ Q Exactive™ UHMR Hybrid Quadrupole-Orbitrap™ Mass Spectrometer - Field Upgrade |
BRE0032850 | Direct Mass Technology™ mode for Thermo Scientific™ Q Exactive™ UHMR Hybrid Quadrupole-Orbitrap™ Mass Spectrometer - Factory |
Perform the highest-quality native, intact mass, and top-down analysis in structural biology and biopharma research. The Thermo Scientific™ Q Exactive™ UHMR (Ultra-High Mass Range) Hybrid Quadrupole-Orbitrap™ Mass Spectrometer (MS) is the first UHMR MS to combine substantially increased sensitivity and mass resolution at high m/z, MS2, and psuedo-MS3 capabilities in a single platform. Thermo Scientific™ Direct Mass Technology™ mode resolves complexity and provides insights into complex macromolecules by adding charge detection capabilities.
Decipher complexity with clarity
Add on Direct Mass Technology mode for simultaneous charge detection to address samples too complex to resolve by ensemble measurements. Define small changes to larger molecules with exquisite detail to unlock new insights into the identification and characterization of proteoforms, biotherapeutics, and next generation drug modalities.
Confidently resolve small mass differences
Analyze intact megaDalton assemblies and resolve small differences in masses that reveal key ligands, modifications, and interactions for better understanding of biological processes.
Conserve precious sample
Samples are often precious and only available in limited amounts. With orders of magnitude enhanced sensitivity at high m/z, you can make high-confidence measurements, even if you have very little sample to work with.
Rapidly perform top-down MS analysis of native proteins
Ultra-high mass quadrupole selection up to 25k m/z and higher fragmentation efficiency in the injection flat pole and HCD cell region allow native top-down analysis.
Characterize intact native protein assemblies, including membrane proteins
By varying the in-source trapping energy, the instrument can release protein subunits for top-down sequencing or, with gentle activation, retain membrane proteins bound to multiple ligands allowing whole complex analysis.