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.
IMPORTANT NOTE: To ensure optimal enrichment using this product please ensure your sample is free of contaminating compounds by using sample preparation procedures such as PAC, and ensure sufficient mixing to ensure beads remain in suspension for good contact between your sample and the magnetic beads.
Support: Proprietary polymer microparticles containing iron oxide (magnetite)
Bead size: ~5-10 µm
Formulation: 20 mg.ml-1 suspension in 20% ethanol