MOAC micro-SPE cartridge for enrichment of low concentration phosphopeptide samples
TiO2 • ZrO2 • Mixed TiO2/ZrO2
[AUTOMATABLE]

• Simple, fast enrichment with minimal sample loss
• MOAC NuTip enriches phosphorylated Ser, Tyr, and Thr, in a highly sensitive and reproducible way, with minimal non-specific binding
• Media directly embedded on inner cartridge wall (no matrix) for reduced contamination, no back pressure
• Different sizes to accomodate samples of varying volumes/concentrations (e.g., as small as 0.1 µL volume)

Phosphopeptide Enrichment NuTip provides MOAC, one of the most widely used strategies in phosphoproteomics, powered by Glygen’s patented NuTip micro-SPE technology. This enables separation of low-concentration phosphopeptide samples by maximizing media surface area in contact with the sample.

MOAC media is embedded directly in the inner surface of the tip: there are no polymers, glues or matrices. This proprietary design prevents contamination or permeability problems common in competitor tips.

Learn more about NuTip technology.

NuTip technology has powered research resulting in many publications: Explore literature featuring NuTip.

How NuTip works

Media selection
Phosphopeptide Enrichment NuTips embedded with proprietary MOAC media. The literature suggests only 30% overlap in phosphopeptides isolated by TiO2 vs. ZrO2, emphasizing importance of an informed (and perhaps mixed-media) approach to enrichment.

Specifications
Sold in packs of 96 tips.

Selected references

“Both MALDI and ESI-MS analyses of [Glygen’s] TiO2 NuTip eluents resulted in the reproducible observation of a greater number of unique sites of phosphorylation with the least amount of nonspecific binding compared with the other MOAC resins. …Enrichment procedures …dramatically improve detection & sequencing of phosphopeptides…” (Gates, et al)

• Gates, et al [NIH]. ‘Comparison of metal and metal oxide media for phosphopeptide enrichment prior to mass spectrometric analyses.’ JASMS June 2010.
• Mikkat S, et al. MS characterization of qualitative protein polymorphisms in the spinal cords of inbred mouse strains. Proteomics. 2010 Mar;10(5):1050-62.

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