Magnetic microparticles with chelated Zr4 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 Zr-IMAC microparticles have a flexible linker (to reduce steric hindrance) activated with phosphonate groups for Zr4 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 Ti-IMAC, MagReSyn TiO2 and/or MagReSyn ZrO2 to increase phosphoproteome coverage.
The new High Performance (HP) version of our zirconium IMAC was externally validated by SUMS (Stanford University Mass Spectrometry click here). The product offers potentially increased recovery and coverage, with application for low-quantity peptide samples. Zirconium IMAC is more stable than titanium IMAC for long term storage, making it suitable for extended studies.
Each batch of product for phosphopeptide enrichment is validated for the application using our stringent mass spectrometry based QC procedures to ensure maximum reproducibility.