Protein phosphorylation plays a pivotal role in most cellular processes, with 30% of the proteome transiently phosphorylated. It is therefore a widely studied post-translational modification. However, the low-abundant nature of phosphopeptides, the low stoichiometry of the modification, and the physico-chemical properties of phosphorylated peptides make proteome-wide characterization of phosphorylation a significant challenge to proteomics researchers.
Consequently, technologies than can specifically enrich phosphopeptides, and are compatible with mass spectrometric analyses, are highly desirable. MagReSyn® TiO2 microparticles allow highly specific, reproducible enrichment of phosphopeptides from complex biological samples such as protein digests. Titanium dioxide enrichment shows selective affinity for phosphoserine (pSer), phosphothreonine (pThr) and phosphotyrosine (pTyr) residues. MagReSyn® TiO2 microparticles have been engineered to achieve the ultimate specificity, outperforming competitor products, with excellent phosphopeptide recovery.
MagReSyn® TiO2 microparticles may be used alone or in combination with MagReSyn® ZrO2, MagReSyn® Zr-IMAC and/or MagReSyn® Ti-IMAC microparticles to enrich diverse types of phosphopeptides for comprehensive phosphoproteomics analyses
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