MagReSyn® TiO2

TiO– 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. 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: 25 suspension in 20% ethanol

***Product not for sale in China***

Product Resources

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.


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

Heterocellular OSM-OSMR signalling reprograms fibroblasts to promote pancreatic cancer growth and metastasis

–  Brian Y. Lee et al.

Nature Communications (2021)

MagReSyn® TiO2

Zirconium(IV)-IMAC Revisited: Improved Performance and Phosphoproteome Coverage by Magnetic Microparticles for Phosphopeptide Affinity Enrichment

–  Ignacio Arribas Diez et al.

J. Proteome Res. (2020)

MagReSyn® Zr-IMAC, Ti-IMAC, TiO2

Phosphoproteomic Effects of Acute Depletion of PP2A Regulatory Subunit Cdc55

–  Michael Plank et al.

Proteomics (2020)

MagReSyn® Ti-IMAC, TiO2, & ZrO2

Parallel global profiling of plant TOR dynamics reveals a conserved role for LARP1 in protein translation

–  M. Regina Scarpin et al.

BioRxiv (2020)

MagReSyn® TiO2

HIPK4 is essential for murine spermiogenesis

–   J. Aaron Crapster et al.

eLife (2020)

MagReSyn® Ti-IMAC & TiO2

Chemical Genetics of AGC-kinases Reveals Shared Targets of Ypk1, Protein Kinase A and Sch9

–   Michael Plank et al.

Mol. Cell. Proteomics (2020)

MagReSyn® Ti-IMAC, ZrO2, & TiO2

Protein aggregation capture on microparticles enables multi-purpose proteomics sample preparation

–   Tanveer Singh Batth et al.

Mol. Cell. Proteomics (2019)

MagReSyn® Ti-IMAC, TiO2, HILIC, Amine

Probability-based detection of phosphoproteomic uncertainty reveals rare signaling events driven by oncogenic kinase gene fusion

–   Xavier Robin et al.

BioRxiv (2019)

MagReSyn® Ti-IMAC & TiO2

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)

MagReSyn® Ti-IMAC, MagReSyn® TiO2

Oncogenic KRAS Regulates Tumor Cell Signaling via Stromal Reciprocation

–   Christopher J. Tape et al

Cell 165 (2016)

MagReSyn® TiO2 & Ti-IMAC

Reproducible Automated Phosphopeptide Enrichment using magnetic TiO2 and Ti-IMAC

–   Christopher J. Tape et al

Analytical Chemistry 86 (2014)

MagReSyn® TiO2 & Ti-IMAC

Inhabiting EGF Receptor or SRC family kinase signaling overcomes BRAF Inhibitor Resistance in melanoma

–   Maria R. Girotti et al

Cancer Discovery 3 (2013)

MagReSyn® TiO2