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Bruker Introduces PTMscan™ on its High-Capacity Ion Trap PTM Discovery System™
Product News

Bruker Introduces PTMscan™ on its High-Capacity Ion Trap PTM Discovery System™

Bruker Introduces PTMscan™ on its High-Capacity Ion Trap PTM Discovery System™
Product News

Bruker Introduces PTMscan™ on its High-Capacity Ion Trap PTM Discovery System™


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Bruker Daltonics has announced the release of PTMscan™ on its PTM Discovery System™ at Pittcon 2006.

The PTM Discovery System incorporates electron transfer dissociation (ETD) in Bruker Daltonics' HCTultra™ high-capacity ion trap mass spectrometer.

ETD fragmentation breaks the peptide backbone non-ergodically and preserves functionally important post-translational modifications (PTMs), such as phosphorylation and glycosylation.

Bruker claims that, the PTMscan can now detect PTMs by first screening for specific neutral losses during collision-induced dissociation (CID), and then triggering automatic, data-dependent ETD experiments on the fly.

A particularly important PTMscan, called Phospho-PTMscan™ is designed to enable the automated detection and localization of phosphorylations of peptides and small proteins. Similar Glyco-PTMscan™ methods are supported as well.

Dr. Michael Schubert, Executive Vice President of Bruker Daltonics, commented, "Last year, we introduced the world's first high-capacity ion trap with ETD capability. This year, the PTMscan methods further extend our customers' ability for automated, intelligent phosphorylation and glycosylation characterization."

"While similar PTM-analysis capabilities have been available on our apex® -Qe FTMS systems, PTMscan now also enables this important branch of proteomics on our robust, ultra-high sensitivity ion traps."

"This further establishes Bruker Daltonics as the leader in PTM and proteomics research by mass spectrometry."

Bruker Daltonics will exhibit at booth #3155 at Pittcon 2006.

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