MagReSyn Ti-IMAC - Ultra-capacity high performance magnetic microparticles

Protein phosphorylation is one of the most important post-translational modifications and is a critical process in cellular signaling and regulation of cellular networks. Comprehensive analysis of the phosphoproteome is a challenging task due to the transient and sub-stoichiometric nature of phosphorylation sites. High-throughput phosphoproteome analysis by mass spectrometry requires compatible technologies than can specifically enrich phosphopeptides. MagReSyn Ti-IMAC?microparticle have a flexible linker (to reduce steric hindrance) activated with phosphonate groups for Ti4 chelation. The unique properties of the proprietary ReSyn microparticle technology allows extremely specific, reproducible enrichment of phosphopeptides from complex biological samples/protein digests. The microparticles can be used either alone, or in combination with MagReSyn TiO2, MagReSyn Zr-IMAC and/or MagReSyn ZrO2 to increase phosphoproteome coverage.

The new High Performance (HP) version of our popular titanium IMAC for phosphopeptide enrichment, was externally validated by the Olsen Lab, and the use first published in Nature Communications, by Dorte B Bekker Jensen et al., 2020. The product offers potentially increased recovery and sample coverage, with application to low-quantity peptide input.

Each batch of product for phosphopeptide enrichment is validated for the application using our stringent mass spectrometry based QC procedures to ensure maximum reproducibility.

MagReSyn Ti-IMAC

Magnetic microparticles with chelated Ti4 metal ions for highly-specific phosphopeptide enrichment

Our classic and highly published research tool for phosphopeptide enrichment, consisting of phosphonate groups chelated with Ti4.