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Shimadzu Review 82[3・4] (2026)
Abstract
Glycans, along with proteins and nucleic acids, are one of the three major biopolymers and the subject of a large body of research. However, due to their structural complexity and analytical limitations, characterization of the entire complement of glycans (the glycome) trails that of the genome, transcriptome, and proteome. Thanks to technological advancements in the 2000s, mass spectrometry has developed into a powerful technique for glycan analysis. This led to the development of numerous related MS-based products, including Shimadzu’s Accurate Glycan Analyzer (AGA) system and Erexim Application Suite. More recently, Shimadzu has been pursuing new glycan modification technologies through industry-academia collaboration. Sialic acid linkage-specific alkylamidation (SALSA), which was developed by Shimadzu, resolves important issues faced by the MS analysis of sialylated glycans. SALSA neutralizes and stabilizes sialic acid groups based on linkage-dependent derivatization, thereby allowing α2,3- and α2,6-linkage isomers of sialylated glycans to be differentiated using MS alone. Through industry-academia partnerships that have led to significant technological advances, SALSA has grown to achieve widespread adoption and now serves as one of the core technologies for glycomics research in a major research project in Japan. This article reviews SALSA and its reagent kit, the SialoCapper-ID Kit, and industry-academia initiatives surrounding these technologies.
1Healthcare Solution Unit, Solutions COE, Analytical & Measuring Instruments Division, Shimadzu Corporation, Kyoto, Japan
2Koichi Tanaka Mass Spectrometry Research Laboratory, Shimadzu Corporation, Kyoto, Japan
3Proteome Research, Research Team for Mechanism of Aging, Tokyo Metropolitan Institute for Geriatrics and Gerontology, Tokyo, Japan
4Institute for Glyco-Core Research (iGCORE), Nagoya University, Aichi, Japan
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