New phosphoproteome enrichment materials Ti4+-IMAC
J&K new phosphoproteome enrichment materials Ti4+-IMAC with excellent identification ability and enrichment performance
Phosphorylation is one of the most important and widely studied forms of post-translational modification of proteins. More than two-thirds of human proteins can be phosphorylated, and the large signal network of these phosphorylation sites provides important information to judge the physiological state of cells, identify disease markers, and discover drug targets. Phosphorylated proteins are characterized by low abundance and high dynamics relative to common proteins; it is a crucial step, therefore, for phosphorylated proteins to achieve high specific enrichment which can reduce sample complexity and increase the number of identified phosphorylation sites. Immobilized metal ion affinity chromatography (IMAC) is one of the most commonly used phosphorylation peptide enrichment techniques in phosphoproteome research.
J&K’s new phosphoproteome enrichment materials ——Ti4+-IMAC offer an identification ability that is three times that of conventional immobilized metal affinity chromatography (Fe3+-IMAC) and provide a 30% increase compared with TiO2. Furthermore, they offer enrichment specificity up to 95%. At the same time, compared with Zr-IMAC, ZrO2, etc., they also have better selectivity and enrichment efficiency -. These new products are now available online through the J&K website.
-  J. Proteome Res., 2008, 7, 3957
-  J. Chromatogr. A, 2017, 1498, 22-28.
-  Nature Protocols, 2013, 8, 3, 461-480
-  Molecular & Cellular Proteomics, 2011, 10:10.1074/mcp.M110.006452, 1-14
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