According to statistics, more than two-thirds of human proteins can be phosphorylated. The huge signaling network composed of these phosphorylation sites provides important information for people to evaluate the physiological status of cells, identify disease markers, and discover drug targets. Therefore, phosphoproteomics is a very important direction in current protein research.

However, since phosphorylated proteins have low abundance and high dynamics compared to ordinary proteins, highly specific enrichment of phosphoproteomics samples is an important step to reduce sample complexity and increase the number of identified phosphorylation sites. An important step. Among them, immobilized metal ion affinity chromatography (IMAC) is one of the commonly used phosphorylated peptide enrichment techniques in phosphoproteomics research.

Researcher Ye Mingliang of Dalian Institute of Chemical Physics, Chinese Academy of Sciences, developed a new generation of phosphopeptide enrichment material - Ti-IMAC [2] (Figure 1).

Figure 1 Schematic diagram of the structure of Ti-IMAC material and the mechanism of binding phosphopeptides [1]

In 2014, after Ti-IMAC materials were applied to large-scale analysis of the human liver phosphoproteome, the human liver tissue phosphorylation site data set was nearly 100 times larger than in 2008 (Figure 2) [2]. Due to the excellent enrichment performance of Ti-IMAC materials, it has received widespread attention and has been recognized by well-known universities, scientific research institutes and bio-tech companies at home and abroad.

The protein phosphorylation identification ability is strong, which is more than three times that of conventional immobilized metal ion affinity chromatography (Fe3+-IMAC). Compared with TiO2, it can be improved by about 30%, and the enrichment specificity can reach 95% [3];
Compared with conventional phosphopeptide enrichment materials such as TiO2, phosphopeptide enrichment efficiency is higher [4].

Figure 2 Ti-IMAC was applied to the large-scale analysis of human liver phosphoproteome, resulting in the largest phosphorylation site data set in human liver tissue [5]

Bailingwei sells the scientific research results of researcher Ye Mingliang - Ti-IMAC.

Researcher Ye Mingliang has developed a number of original technologies in highly sensitive detection and large-scale analysis of protein post-translational modifications. He has published more than 180 SCI papers in Nat. Methods, Nat. Chem. Biol. and other journals, with more than 6,000 citations. . He has successively presided over projects such as the NSFC Outstanding Youth Fund, key projects of the National Key Research and Development Plan, and major national scientific research plan projects. He has won awards such as the Special Scholarship Award of the President of the Chinese Academy of Sciences, the Natural Science Award of Liaoning Province, and the Second Prize of the National Natural Science Award.

2749380
Monodisperse immobilized affinity chromatography microspheres
CAE-Ti-IMAC, 100%
Particle size: ~10μm
Enrichment method: solution method

2749381
Solid phase extraction immobilized affinity chromatography microspheres
SPE-Ti-IMAC, 100%
Particle size: 40-100μm
Enrichment method: solution method/Tip column method

References

1. Zhou, H., Ye, M., Dong, J. et al. Nat Protoc.2013, 461–480.
2. Zhou H, Ye M, Dong J, Han G, Jiang X, Wu R, Han F. Journal of Proteome Research. 2008, 7, 3957-3967.
3. Yao Y, Dong J, Dong M, Liu F, Wang Y, Mao J, Ye M, Zou H. J. Chromatogr. A. 2017, 1498, 22–28.
4. Zhou, Houjiang,Low, Teck Y.,Hennrich, Marco L.,et al. Molecular & Cellular Proteomics. 2011,10(10):1.
5. Bian Y, et al. J. Proteomics. 2014, 96, 253-262.