Michael Merriman Applied Biosystems/Sciex, Foster City, CA Office: 800-248-0281 x7228 FAX: E-mail: Job Title: Field Application Scientist M.S. in Organic Synthesis from Northwestern University

Speaker: Michael Merriman, Applied Biosystems/Sciex, Foster City, CA

Topic: iTRAQ Reagents: Amine-Specific Labeling For Multiplexed Relative and Absolute Protein Quantitation

Place: Building 549, Auditorium, NCI at Frederick, Frederick, MD

Time: Thursday, January 20, 2005, at 10:00 AM

Abstract: Proteomics research includes the characterization of protein mixtures in order to understand complex biological systems and determine relationships between proteins, their function, and protein-protein interactions. Often, the goal is to monitor changes in protein mixture composition under different physiologically relevant conditions, a type of study referred to as differential profiling. While monitoring these qualitative changes is valuable, there is a need to develop quantitative tools that can provide more insight into these experiments. Recent approaches to some of these challenges in protein quantitation involve the combination of chemistry with 2D gel electrophoresis (DIGE) or liquid chromatography (ICAT® reagents). As these techniques become established and gain acceptance in protein expression analysis there is a requirement to expand the scope of these technologies and address some of the remaining issues in quantitative proteomics such as: 1) improve overall protein and proteome coverage while retaining important post translational modification (PTM) information, 2) simultaneously compare multiple samples, e.g. normal versus diseased versus drug treated samples or time course studies, in the same experiment, 3) quantify, in absolute terms, specific proteins of interest, such as biomarkers, or to screen drug targets, such as kinase inhibitors, and 4) increase statistical relevance needed for quantitative experiments by expanding multiplexing, up to four, to include duplicates or triplicates in the design. These requirements for broad proteome coverage, multiplexing, absolute quantitation, and more statistically significant information has led to the development of the isobaric tags for related and absolute quantitation.