|12. Development of Human Serum N-Glycan Library for Rapid Identification in Disease Biomarker Discovery Using nanoLC-MS
|Mon 4:30 PM - PosterSplash Track 2
University of California, Davis
|View Long Abstract
|It has been estimated that over 70% of human proteins are glycosylated. Glycosylation, one of the most common post-translational modifications, has been shown to change with various pathological states including cancer. Global glycan profiling of human serum based on mass spectrometry has led to several promising markers for disease. These changes in glycan structure can alter monosaccharide composition as well as linkages. Due to the lack of a glycan template, high-throughput analysis of N-glycans is not possible. In an effort towards rapid profiling and identification, the glycome has been characterized and compiled into a structure library, enabling rapid analysis.