6340 Ion Trap MS makes the fragmentation power of electron transfer dissociation (ETD) - formerly attainable only with Fourier-transform MS - affordable for the average laboratory
Agilent Technologies has announced the availability of the Agilent 6340 ion trap liquid chromatograph/mass spectrometer (LC/MS), which allows scientists to study proteins in a manner that was previously achievable only on a million-dollar floor-standing instrument that requires a dedicated operator.
The 6340, a new instrument in Agilent's 6000 Series portfolio of LC/MS systems, fits on a bench top and is equipped with an electron transfer dissociation (ETD) unit - a new tool for the study of proteins and post-translational modifications.
"The 6340 Ion Trap MS makes the fragmentation power of ETD - formerly attainable only with Fourier-transform MS - affordable for the average laboratory and accessible to all scientists," said Linda Lopez, product manager.
"Our complete solution, which includes innovative separation technologies, the 6340 and data processing software designed expressly for ETD data, will bring unsurpassed performance, reliability and productivity to proteomics research." Proteins regulate most biological processes, and their activity is often controlled by the attachment of molecules such as phosphate groups, also known as post-translational modifications.
Scientists use various approaches to identify and characterize proteins - and chemical modifications - that may be involved in normal biological functions or diseases such as cancer.
Although ion trap mass spectrometers are a popular choice for protein studies, analysis of post-translational modifications can be challenging because standard ion fragmentation methods often cause labile phosphates, glycans and other chemical modifications to dissociate from peptides.
This makes it difficult to determine the attachment point of these modifications and affords minimal peptide sequence information.
Agilent's new ETD provides a 'softer' mode of fragmentation that preserves these labile modifications.
When operated in ETD mode, the 6340 Ion Trap provides extensive and easy-to-interpret amino acid sequence information in the form of complementary C- and Z-series ions.
Other features that make the 6340 an ideal tool for the study of post-translational modifications include the ability to alternate between ETD and collision induced dissociation (CID) modes of fragmentation from scan to scan, which helps to pinpoint the precise identity and location of a chemical modification.
In addition, neutral-loss triggered auto-MS3 and pseudo-MSn modes can be used to target specific families of modifications.
Unlike FT-MS devices, the 6340 supports rapid nano-scale chromatography, which facilitates 'shot-gun' proteomics studies involving the analysis of all the proteins extracted from whole cell lysates (contents released during the decomposition of a cell).
When used in concert with Agilent's revolutionary HPLC-Chip, the 6340 will enhance researchers' ability to identify and characterize protein modifications in extremely complex samples.
The Agilent Spectrum Mill for MassHunter Workstation completes the full solution for post-translational modification studies.
Other new features and advances of the 6340 include a high-speed data acquisition system that provides unsurpassed scan collection and transfer rates; ETD reagent anion monitoring; selective or automatic charge state data collection; and reproducible ETD spectra.
Agilent offers an entire line of ion traps (6310, 6320 and 6330) to accommodate a wide range of budget and performance requirements.
