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