TiO2 – functional microparticles for highly-specific phosphopeptide enrichment
Protein phosphorylation plays a pivotal role in most cellular processes, with 30% of the proteome transiently phosphorylated. It is therefore a widely studied post-translational modification. However, the low-abundant nature of phosphopeptides, the low stoichiometry of the modification, and the physico-chemical properties of phosphorylated peptides make proteome-wide characterization of phosphorylation a significant challenge to proteomics researchers.
Consequently, technologies than can specifically enrich phosphopeptides, and are compatible with mass spectrometric analyses, are highly desirable. MagReSyn® TiO2 microparticles allow highly specific, reproducible enrichment of phosphopeptides from complex biological samples such as protein digests. Titanium dioxide enrichment shows selective affinity for phosphoserine (pSer), phosphothreonine (pThr) and phosphotyrosine (pTyr) residues. MagReSyn® TiO2 microparticles have been engineered to achieve the ultimate specificity, outperforming competitor products, with excellent phosphopeptide recovery.
MagReSyn® TiO2 microparticles may be used alone or in combination with MagReSyn® ZrO2, MagReSyn® Zr-IMAC and/or MagReSyn® Ti-IMAC microparticles to enrich diverse types of phosphopeptides for comprehensive phosphoproteomics analyses
Support: Proprietary polymer microparticles containing iron oxide (magnetite)
Bead size: ~5-10 µm
Formulation: 25 mg.ml-1 suspension in 20% ethanol
MagReSyn® TiO2 Performance Superiority
Comparative assessment of MagReSyn® TiO2 (green bars) vs a leading competitor (orange bars) for phosphopeptide enrichment.
32P labelled CHK1 tryptic digests were enriched for phosphopeptides and analyzed by LC/MS/MS.
MagReSyn® TiO2 showed exceptional specificity with up to 100% of identified peptides being phosphorylated, vs 78% for the competitor.
Phosphopeptide recovery was 78% using MagReSyn® TiO2 and 70% using alternate TiO2.
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.
Citations and References
Chemical genetics of AGC-kinases reveals shared targets of Ypk1, Protein Kinase A and Sch9
– Michael Plank et al.
Protein aggregation capture on microparticles enables multi-purpose proteomics sample preparation
– Tanveer Singh Batth et al.
MOLECULAR & CELLULAR (2019)
Probability-based detection of phosphoproteomic uncertainty reveals rare signaling events driven by oncogenic kinase gene fusion
– Xavier Robin et al.
Cell-Specific labeling for analysing bidirectional signaling by mass spectrometry
– Christopher J. Tape & Claus Jørgensen
KINASE SIGNALING NETWORKS pp 219-234, part of the Methods in Molecular Biology book series, MIMB, volume 1636 (2017)
Oncogenic KRAS Regulates Tumor Cell Signaling via Stromal Reciprocation
– Christopher J. Tape et al
Cell 165 (2016)
Reproducible Automated Phosphopeptide Enrichment using magnetic TiO2 and Ti-IMAC
– Christopher J. Tape et al
Analytical Chemistry 86 (2014)
Inhabiting EGF Receptor or SRC family kinase signaling overcomes BRAF Inhibitor Resistance in melanoma
– Maria R. Girotti et al
Cancer Discovery 3 (2013)