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MagResyn TiO2

TiO2-functional microspheres for highly-specific phosphopeptide enrichment

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 microspheres 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 microspheres have been engineered to achieve the ultimate specificity, outperforming competitor products, with excellent phosphopeptide recovery.  MagReSyn® TiO2 microspheres may be used alone or in combination with MagReSyn® ZrO2 and/or MagReSyn® Ti-IMAC microspheres to enrich diverse types of phosphopeptides for comprehensive phosphoproteomics analyses.


Support : Proprietary polymer microspheres containing iron oxide (magnetite)

Binding capacity : > 10 µg phosphopeptide per mg support

Bead size : 5-10 µm average

Formulation : 25 suspension in 20% ethanol

2 mL : 440 $

5 mL : 880 $

10 mL : 1405 $