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.

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.

Citations and References

Competitive binding of STATs to receptor phospho-Tyr motifs accounts for altered cytokine responses in autoimmune disorders

– Stephan Wilmes et al.

BioRxiv (2021)

MagReSyn® Ti-IMAC

The cGMP-Dependent Protein Kinase 2 Contributes to Cone Photoreceptor Degeneration in the Cnga3-Deficient Mouse Model of Achromatopsia

– Mirja Koch et al.

Int. J. Mol. Sci (2021)

MagReSyn® Ti-IMAC

An AKT2-specific nanobody that targets the hydrophobic motif induces cell cycle arrest, autophagy and loss of focal adhesions in MDA-MB-231 cells

– Tijs Merckaert et al.

Biomedicine & Pharmacotherapy (2020)

MagReSyn® Ti-IMAC

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

An Unbiased Approach to Mapping the Signaling Network of the Pseudorabies Virus US3 Protein

– RJJ Jansens et al.

Pathogens (2020)

MagReSyn® Ti-IMAC

Phosphoproteomic Effects of Acute Depletion of PP2A Regulatory Subunit Cdc55

– Michael Plank et al.

Proteomics (2020)

MagReSyn® ZrO₂, Ti-IMAC, TiO₂

The Diabetes Gene JAZF1 Is Essential for the Homeostatic Control of Ribosome Biogenesis and Function in Metabolic Stress

– Ahmad Kobiita et al.

Cell Reports (2020)

MagReSyn® Ti-IMAC

Cannabinoid exposure in rat adolescence reprograms the initial behavioral, molecular, and epigenetic response to cocaine

– Maria Scherma et al.

PNAS (2020)

MagReSyn® Ti-IMAC

Cyclin A triggers Mitosis either via the Greatwall kinase pathway or Cyclin B

– Nadia Hégarat et al.

The EMBO Journal (2020)

MagReSyn® Ti-IMAC

Fluorescence fluctuation analysis reveals PpV dependent Cdc25 protein dynamics in living embryos

– Boyang Liu et al.

PLOS Genetics (2020)

MagReSyn® Ti-IMAC

HIPK4 is essential for murine spermiogenesis

– J. Aaron Crapster et al.

eLife (2020)

MagReSyn® Ti-IMAC, & TiO₂

CDK8 fine-tunes IL-6 transcriptional activities by limiting STAT3 resident time at the gene loci

– Jonathan Martinez-Fabregas et al.

BioRxiv (2020)

MagReSyn® Ti-IMAC

CYCA3;4 Is a Post-Prophase Target of the APC/CCCS52A2 E3 Ligase Controlling Formative Cell Divisions in Arabidopsis

– Alex Willems et al.

BioRxiv (2020)

MagReSyn® Ti-IMAC

Rapid and site-specific deep phosphoproteome profiling by data-independent acquisition (DIA) without the need for spectral libraries

– Dorte B. Bekker-Jensen et al.

Nature Communications (2020)

MagReSyn® Ti-IMAC HP

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

A Compact Quadrupole-Orbitrap Mass Spectrometer with FAIMS Interface Improves Proteome Coverage in Short LC Gradients

– Dorte B. Bekker-Jensen et al.

Mol. Cell. Proteomics (2020)

MagReSyn® Ti-IMAC HP & Amine

Phosphorylation controls RNA binding and transcription by the influenza virus polymerase

– Anthony R Dawson et al.

BioRxiv (2020)

MagReSyn® Ti-IMAC

DYRK3-Controlled Phase Separation Organizes the Early Secretory Pathway

– Raffaella Gallo et al.

BioRxiv (2020)

MagReSyn® Ti-IMAC

R2‐P2 rapid‐robotic phosphoproteomics enables multidimensional cell signaling studies

– Mario Leutert et al.

Mol. Syst. Biol. (2019)

MagReSyn® Ti-IMAC, Zr-IMAC, & TiO₂

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

– Tanveer Singh Batth et al.

Mol. Cell. Proteomics (2019)

MagReSyn® HILIC, Ti-IMAC & TiO₂

CD8 regulates insulin secretion and mediates postnatal and stress-induced expression of neuropeptides in pancreatic β cells

– Jing Xue et al.

Cell Reports 28 (2019)

MagReSyn® Ti-IMAC

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, MagReSyn® TiO₂

Conduit integrity is compromised during acute lymph node expansion

– Victor G. Martinez et al.

BioRxiv (2019)

MagReSyn® Ti-IMAC

Proteasome-mediated remodeling of the proteome and phosphoproteome during kiwifruit pollen germination

– Candida Vannini et al.

Journal of Proteomics 192 (2019)

MagReSyn® Ti-IMAC

Direct Coupling of Dispersive Extractions with Magnetic Particles to Mass Spectrometry via Microfluidic Open Interface

– Marcos Gascon et al.

Analytical Chemistry (2019)

MagReSyn® Ti-IMAC

Pptc7 is an essential phosphatase for promoting mammalian mitochondrial metabolism and biogenesis

– Natalie M. Niemi et al.

Nature Communications (2019)

MagReSyn® Ti-IMAC

Peanut Stunt Virus and Its Satellite RNA Trigger Changes in Phosphorylation in N. benthamiana Infected Plants at the Early Stage of the Infection

– Barbara Wrzesinkska et al.

Int. J of Moleecular Sciences 19 (2018)

MagReSyn® Ti-IMAC

Phosphoproteomic-based kinase profiling early in influenza virus infection identifies GRK2 as antiviral drug target

– Emilio Yángüez et al.

Nature Communications 9 (2018)

MagReSyn® Ti-IMAC

Ultra-high pressure (>30,000 psi) packing of capillary columns enhances depth of shotgun proteomic analyses

– Evgenia Shishkova et al.

Analytical Chemistry (2018)

MagReSyn® Ti-IMAC

The auxin-related CrRLK1L kinase ERULUS controls cell wall composition during root hair tip growth

– Sébastjen Schoenaers et al.

Current Biology 28 (2018)

MagReSyn® Ti-IMAC

Proteomic analysis of cell cycle progression in asynchronous cultures, including mitotic subphrases, using PRIMMUS

– Tony Ly et al.

ELIFE 6, pii: e27574 (2017)

MagReSyn® Ti-IMAC

HIV-1 activities T cell signaling independently of antigen to drive viral spread

– Alice C.L. Len et al.

Cell Reports 18 (2017)

MagReSyn® Ti-IMAC

Comparative genetic, proteomic and phosphoproteomic analysis of C. elegans embryos with a focus on ham-1/STOX and pig-1/MELK in dopaminergic neuron development

– Sarah-Lena Offenburger et al.

Nature Scientific Reports 7, 4314 (2017)

MagReSyn® Ti-IMAC

Cell-Specific Labeling for Analyzing Bidirectional Signaling by Mass Spectrometry

– Christopher J. Tape et al.

Kinase Signaling Networks pp 219-234. Part of the Methods in Molecular Biology, MIMB, volume 1636 (2017)

MagReSyn® Ti-IMAC, MagReSyn® TiO₂

Identification of ADP-Ribose Acceptor Sites on In Vitro Modified Proteins by Liquid Chromatography–Tandem Mass Spectrometry

– Mario Leutert et al.

Poly(ADP-Ribose) Polymerase: Methods and Protocols, Methods in Molecular Biology, vol. 1608 (2017)

MagReSyn® Ti-IMAC

GSK3α and GSK3β Phosphorylate Arc and Regulate its Degradation

– Agata Golds et al.

Frontiers in Molecular Neuroscience 10 (2017)

MagReSyn® Ti-IMAC

Proteome Profiling of Wheat Shoots from Different Cultivars

– Lam Dai Vu et al.

Frontiers in Plant Science (2017)

MagReSyn® Ti-IMAC

Phosphoproteomics with Activated Ion Electron Transfer Dissociation

– Nicholas M. Riley et al.

Analytical Chemistry (2017)

MagReSyn® Ti-IMAC

Human RIF1 and protein phosphatase 1 stimulate DNA replication origin licensing but suppress origin activation

– Shin-ichiro Hiraga et al.

EMBO Reports (2017)

MagReSyn® Ti-IMAC

A Role for Barley Calcium-Dependent Protein Kinase CPK2a in the Response

– Agata Cieśla et al.

Frontiers in Plant Science 7 (2016), Article 1550

MagReSyn® Ti-IMAC

An up-to-date workflow for plant (phospho)proteomics identifies differential drought-responsive phosphorylation events in maize leaves

– Lam Dai Vu et al.

J. Proteome Research 15 (2016)

MagReSyn® Ti-IMAC

Oncogenic KRAS Regulates Tumor Cell Signaling via Stromal Reciprocation

– Christopher J. Tape et al.

Cell 165 (2016)

MagReSyn® Ti-IMAC, MagReSyn® TiO₂

Cell-specific labelling enzymes for analysis of cell-cell communication in continuous co-culture

– Christopher J. Tape et al.

Mol. Cell. Proteomics 13 (2014)

MagReSyn® Ti-IMAC

Reproducible automated phosphopetide enrichment using magnetic TiO2 and Ti-IMAC

– Christopher J. Tape et al.

Analytical Chemistry 86 (2014)

MagReSyn® Ti-IMAC, MagReSyn® TiO₂

NEW: MagReSyn® Ti-IMAC HP

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

MagReSyn® Ti-IMAC

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

Product Resources

Citations and References

Competitive binding of STATs to receptor phospho-Tyr motifs accounts for altered cytokine responses in autoimmune disorders

The cGMP-Dependent Protein Kinase 2 Contributes to Cone Photoreceptor Degeneration in the Cnga3-Deficient Mouse Model of Achromatopsia

An AKT2-specific nanobody that targets the hydrophobic motif induces cell cycle arrest, autophagy and loss of focal adhesions in MDA-MB-231 cells

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

An Unbiased Approach to Mapping the Signaling Network of the Pseudorabies Virus US3 Protein

Phosphoproteomic Effects of Acute Depletion of PP2A Regulatory Subunit Cdc55

The Diabetes Gene JAZF1 Is Essential for the Homeostatic Control of Ribosome Biogenesis and Function in Metabolic Stress

Cannabinoid exposure in rat adolescence reprograms the initial behavioral, molecular, and epigenetic response to cocaine

Cyclin A triggers Mitosis either via the Greatwall kinase pathway or Cyclin B

Fluorescence fluctuation analysis reveals PpV dependent Cdc25 protein dynamics in living embryos

HIPK4 is essential for murine spermiogenesis

CDK8 fine-tunes IL-6 transcriptional activities by limiting STAT3 resident time at the gene loci

CYCA3;4 Is a Post-Prophase Target of the APC/CCCS52A2 E3 Ligase Controlling Formative Cell Divisions in Arabidopsis

Rapid and site-specific deep phosphoproteome profiling by data-independent acquisition (DIA) without the need for spectral libraries

Chemical genetics of AGC-kinases reveals shared targets of Ypk1, Protein Kinase A and Sch9

A Compact Quadrupole-Orbitrap Mass Spectrometer with FAIMS Interface Improves Proteome Coverage in Short LC Gradients

Phosphorylation controls RNA binding and transcription by the influenza virus polymerase

DYRK3-Controlled Phase Separation Organizes the Early Secretory Pathway

R2‐P2 rapid‐robotic phosphoproteomics enables multidimensional cell signaling studies

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

CD8 regulates insulin secretion and mediates postnatal and stress-induced expression of neuropeptides in pancreatic β cells

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

Conduit integrity is compromised during acute lymph node expansion

Proteasome-mediated remodeling of the proteome and phosphoproteome during kiwifruit pollen germination

Direct Coupling of Dispersive Extractions with Magnetic Particles to Mass Spectrometry via Microfluidic Open Interface

Pptc7 is an essential phosphatase for promoting mammalian mitochondrial metabolism and biogenesis

Peanut Stunt Virus and Its Satellite RNA Trigger Changes in Phosphorylation in N. benthamiana Infected Plants at the Early Stage of the Infection

Phosphoproteomic-based kinase profiling early in influenza virus infection identifies GRK2 as antiviral drug target

Ultra-high pressure (>30,000 psi) packing of capillary columns enhances depth of shotgun proteomic analyses

The auxin-related CrRLK1L kinase ERULUS controls cell wall composition during root hair tip growth

Proteomic analysis of cell cycle progression in asynchronous cultures, including mitotic subphrases, using PRIMMUS

HIV-1 activities T cell signaling independently of antigen to drive viral spread

Comparative genetic, proteomic and phosphoproteomic analysis of C. elegans embryos with a focus on ham-1/STOX and pig-1/MELK in dopaminergic neuron development

Cell-Specific Labeling for Analyzing Bidirectional Signaling by Mass Spectrometry

Identification of ADP-Ribose Acceptor Sites on In Vitro Modified Proteins by Liquid Chromatography–Tandem Mass Spectrometry

GSK3α and GSK3β Phosphorylate Arc and Regulate its Degradation

Proteome Profiling of Wheat Shoots from Different Cultivars

Phosphoproteomics with Activated Ion Electron Transfer Dissociation

Human RIF1 and protein phosphatase 1 stimulate DNA replication origin licensing but suppress origin activation

A Role for Barley Calcium-Dependent Protein Kinase CPK2a in the Response

An up-to-date workflow for plant (phospho)proteomics identifies differential drought-responsive phosphorylation events in maize leaves

Oncogenic KRAS Regulates Tumor Cell Signaling via Stromal Reciprocation

Cell-specific labelling enzymes for analysis of cell-cell communication in continuous co-culture

Reproducible automated phosphopetide enrichment using magnetic TiO2 and Ti-IMAC

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

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