Thermo Scientific Forms Technology Alliance Partnership with Barnett Institute
News Jan 28, 2013
Thermo Fisher Scientific Inc. has entered into a Technology Alliance Partnership agreement with scientists at the Barnett Institute, Northeastern University, Boston, MA.
This partnership establishes a formal collaboration to accelerate research in high-resolution accurate mass liquid chromatography-mass spectrometry (LC-MS) applications.
The agreement, a broad collaboration between Thermo Fisher scientists and Northeastern scientists will include: performing research and sharing samples and data that could lead to development of improved techniques, exchanging ideas and opinions about improving instrument and software performance, discourse about current technology issues and publishing new methodologies and scientific advances.
The alliance, with the Barnett Institute’s Director Barry Karger and team, will focus on three research areas:
• Comprehensive characterization of complex proteins
• Ultra-trace analysis methodologies of proteomic samples
• New LCMS based methods for analysis of biosimilars
“Academic research labs are tremendous sources of innovation, which is why we’re so pleased to collaborate with Northeastern scientists who have particular expertise in combining the strengths of separation science and high resolution MS analysis of proteins,” said Iain Mylchreest, vice president, Research and Development, Thermo Fisher.
“This agreement formalizes our commitment to actively expedite the development and application of important new technologies,” said Professor Karger.
Professor Karger continued, “We are very pleased to strengthen the ongoing collaboration of our laboratory with Thermo Fisher in LC-MS protein analysis for biomedical and biotechnology applications.”
Chinese researchers have developed interfacially polymerized porous polymer particles for low- abundance glycopeptide separation. These polymer particles - with hydrophilic-hydrophobic heterostructured nanopores - can separate low-abundance glycopeptides from complex biological samples with high-abundance background molecules efficiently.