MagResyn Ti-IMAC

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

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.

This product is available in Standard or High Performance.

  • Support: Proprietary polymer microparticles containing iron oxide (magnetite)
  • Bead size: ~5-10 µm
  • Formulation: 20 mg.ml-1 suspension in 20% ethanol

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*PhenoSwitch Bioscience only distributes MagResyn products in Canada. If you are not located in Canada, please visit the MagResyn website for more information. 

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Klaus Klarskov, Ph.D., Professor at Université de Sherbrooke, Canada

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