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2/3 of human proteins can be phosphorylated. The signal network of phosphorylation sites provides information to determine physiological status of cells, identify disease markers, and discover drug targets. Achieving higher specific enrichment of phosphoproteins or phosphopeptides would reduce sample complexity, suitable for applications such as MS-based phosphoproteome analysis. For this purpose, IMAC is one of the most effective methods for phosphopeptide enrichment, commonly used on phosophoproteome research.
Dr. Mingliang Ye has developed the new phosphopeptide enrichment material Ti4+-IMAC.
Ti-IMAC’s structure and mechanism of binding with phosphopeptide
- Higher identification ability of conventional immobilized metal affinity chromatography: 3 times of Fe3+-IMAC, 1.3 times of TiO2
- Enrichment specificity up to 95%
- Better selectivity and enrichment efficiency than Zr-IMAC, ZrO2, etc. 
- Bian Y, et al. J. Proteomics. 2014, 96, 253-262.
- Zhou H, Ye M, Dong J, Han G, Jiang X, Wu R, Han F. Journal of Proteome Research. 2008, 7, 3957-3967.
- Yao Y, Dong J, Dong M, Liu F, Wang Y, Mao J, Ye M, Zou H. J. Chromatogr. A. 2017, 1498, 22–28.
- Zhou, H., Ye, M., Dong, J. et al. Nat Protoc.2013, 461–480.
- Zhou, Houjiang,Low, Teck Y.,Hennrich, Marco L.,et al. Molecular & Cellular Proteomics. 2011,10(10):1.
Dr. Ye’s Profile
He has developed several new approaches for highly sensitive detection and large-scale analysis of protein post-translational modifications. He has published more than 180 Science papers with more than 6,000 citations in high-impact journals.
2749380 CAE-Ti-IMAC, 100%