ECD Fragmentation for the Workhorse Mass Spectrometer
The ExD cell produces ECD fragmentation similar to FTICR-ECD, but on workhorse mass spectrometers like Q-TOFs and Orbitrap QEs. The ability to perform simple electron-based fragmentation enables valuable new types of data and time-saving workflows. The Example Data on this page illustrates the value the ExD cell can add to your laboratory.
Click the toggles below to see detailed figures and captions describing some ExD example data.
Our ExD filament design features a plug-in cassette with exchangeable filament insert for quick and easy replacement.
Install the ExD cell in your current instrument to maximize your investment, or add ExD to an instrument purchase order to capitalize on the increased sensitivity and resolution of newer technology.
The ExD cell attaches to the entrance of a shortened collision cell, replacing the original collision cell during installation. This way, ExD occurs after isolation by the quadrupole mass filter without affecting collision cell operation.
The ExD cell is available for the entire Agilent Q-TOF family, including 6530, 6545, 6545XT, 6546, 6550, and 6560 Q-TOFs.
ECD is a “gentle” fragmentation method that preserves labile PTMs – phosphorylation, glycosylation – on fragment ions. With the ExD cell installed, use ECD to map their precise location on peptides and proteins.
Selective dissociation of disulfide bonds by ECD enables their localization without prior sample reduction.
The ExD cell can operate in either ECD or transmission-only mode.
Now, the ExD Software enables automatic switching between selected ExD modes in sync with changes in instrument scan type during data acquisition.
Use the ExD Software autotune feature to simplify operation of the ExD cell.
The ExD AQ-25x Option for Agilent LC/Q-TOF makes electron-based fragmentation methods accessible and highly affordable for pharmaceutical, clinical, consumer product, and life science protein research laboratories.
Increase sequence coverage of larger peptides and intact proteins beyond the limits of CID alone.
Since ECD and CID produce complementary sequence information, the combination of both methods increases confidence in results.
ECD fragmentation products unique to isoaspartate clearly differentiate it from the non-isomerized form. Isoaspartate is implicated in age-related protein inactivation and aggregation, and reduced efficacy of protein therapeutics.
Side chain fragments (w-ions) produced by ECD can be used to distinguish isobaric amino acids.