MagReSyn Zr-IMAC HP (10 ml)
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.