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. Products for phosphopeptide enrichment are validated for the intended application using our stringent QC procedures.
This product is available in Standard or High Performance.
"PhenoSwitch Bioscience Inc has provided us with outstanding efficacious service, high quality data and exemplary data analysis over the past three years."