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. Products for phosphopeptide enrichment are validated for the intended application using our stringent QC procedures.
Support: Proprietary polymer microparticles containing iron oxide (magnetite)
Bead size: ~5-10 µm
Formulation: 20 mg.ml-1 suspension in 20% ethanol
TERMS AND CONDITIONS
Products supplied by ReSyn Biosciences (Pty) Ltd are for research purposes only. ReSyn products are not to be used for diagnostic, therapeutic or commercial means any use resulting in monetary gain, including, but not limited to, incorporation in a kit, repackaging and re-formulation. Please enquire about sub-licenses for commercial use.