NEW: MagReSyn® Ti-IMAC HP

Magnetic microparticles with chelated Ti4+ 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® Ti-IMAC microparticle have a flexible linker (to reduce steric hindrance) activated with phosphonate groups for Ti4+ 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® TiO2, MagReSyn® Zr-IMAC and/or MagReSyn® ZrO2 to increase phosphoproteome coverage.

The new High Performance (HP) version of our popular titanium IMAC for phosphopeptide enrichment, was externally validated by the Olsen Lab, and the use first published in Nature Communications, by Dorte B Bekker Jensen et al., 2020. The product offers potentially increased recovery and sample coverage, with application to low-quantity peptide input.

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: This product has a limited shelf-life of 6 months due the instability of the chelated Titanium ions, please consider carefully how much product is required. Zr-IMAC & Zr-IMAC HP offer similar coverage for most sample types, and we would recommend evaluation of these products for low throughput applications. 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

ORDER NOW
***Product not for sale in China***

MagReSyn® Ti-IMAC

Magnetic microparticles with chelated Ti4+ metal ions for highly-specific phosphopeptide enrichment

Our classic and highly published research tool for phosphopeptide enrichment, consisting of phosphonate groups chelated with Ti4+

MagReSyn® Ti-IMAC has also been used in the development of new innovative sample preparation protocols. As an example Leutert et al., 2017, illustrated efficient enrichment of ADP-ribosylated peptides using Ti-IMAC, providing a comprehensive protocol in Methods in Molecular Biology.

Support: Proprietary polymer microparticles containing iron oxide (magnetite)
Bead size: ~5-10 µm
Formulation: 20 mg.ml-1 suspension in 20% ethanol

ORDER NOW
***Product not for sale in China***

Product Resources

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.

Citation and Reference Examples

Please review our comprehensive method library to find the most relevant reference material for your particular application.

Systems level analysis of time and stimuli specific signaling through PKA

–  Michael Plank et al.

BioRxiv (2022)

MagReSyn® Ti-IMAC

Tissue-wide Effects Overrule Cell-intrinsic Gene Function in Cortical Projection Neuron Migration

–  Andi H Hansen et al.

BioRxiv (2022)

MagReSyn® Ti-IMAC

Phosphoproteomic profiling of influenza virus entry reveals infection-triggered filopodia induction counteracted by dynamic cortactin phosphorylation

–   Annika Hunziker et al.

Cell Reports (2022)

MagReSyn® Ti-IMAC

Temporal Analysis of Protein Ubiquitylation and Phosphorylation During Parkin-Dependent Mitophagy

–   Katharina I. Zittlau et al.

MCP (2022)

MagReSyn® Ti-IMAC

Unraveling virus-induced cellular signaling cascades by label-free quantitative phosphoproteomics

–   Annika Hunziker & Silke Stertz

STAR Protocols (2022)

MagReSyn® Ti-IMAC

UDP-glucose dehydrogenase expression is upregulated following EMT and differentially affects intracellular glycerophosphocholine and acetylaspartate levels in breast mesenchymal cell lines.

–   Qiong Wang et al.

Molecular Oncology (2021)

MagReSyn® Ti-IMAC

Plant Phosphoproteomics: Known Knowns, Known Unknowns, and Unknown Unknowns of an Emerging Systems Science Frontier

–   Pratigya Subba et al.

OMICS (2021)

MagReSyn® Ti-IMAC

Spatial-proteomics reveals phospho-signaling dynamics at subcellular resolution

–   Ana Martinez-Val et al.

Nature Communications (2021)

MagReSyn® Amine, MagReSyn® Ti-IMAC HP

Structural insights into an atypical secretory pathway kinase crucial for Toxoplasma gondii invasion

–  Gaëlle Lentini et al.

Nature Communications (2021)

MagReSyn® Ti-IMAC

Modulation of immune cell reactivity with cis-binding Siglec agonists

–  Corleone S. Delaveris et al.

PNAS (2021)

MagReSyn® Ti-IMAC

Unraveling the MAX2 Protein Network in Arabidopsis thaliana: Identification of the Protein Phosphatase PAPP5 as a Novel MAX2 Interactor

–  Sylwia Struk et al.

MCP (2021)

MagReSyn® Ti-IMAC

The membrane-localized protein kinase MAP4K4/TOT3 regulates thermomorphogenesis

–  Lam Dai Vu et al.

Nature Communications (2021)

MagReSyn® Ti-IMAC