PP0410
PhosphoProfile™ I Phosphopeptide Enrichment Kit
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About This Item
UNSPSC Code:
12352200
usage
sufficient for 24 purifications
shipped in
wet ice
storage temp.
2-8°C
Application
The PhosphoProfile I Phosphopeptide Enrichment Kit is designed to increase the concentration of phosphopeptides from tryptic digests by immobilized metal affinity chromatography (IMAC). The enriched solution helps to overcome the limitations of mass spectrometry of phosphopeptides. The provided reagents are compatible with downstream LC-MS and MALDI-TOF MS analysis.
Features and Benefits
- Low non-specific binding - high data confidence
- No bias in phosphorylation states - accurate representation of phosphorylation types present for sample comparisons
- Fast sample processing - reduces time to data generation from sample collection
- Complete optimized set of reagents and enzymes - Reduce cost and effort with total sample management in one package
Other Notes
The kit is a convenient collection of all materials necessary to perform phosphopeptide enrichments from crude samples following tryptic digestion. The supplied phosphopeptide capture matrix is a novel Ga (III) chelate silica based on Sigma-Aldrich′s proprietary nitriloacetic acid (NTA) analog. The matrix is packed into spin columns for easy, microscale affinity capture of phosphopeptides.
Legal Information
PhosphoProfile is a trademark of Sigma-Aldrich Co. LLC
Kit Components Also Available Separately
Product No.
Description
SDS
- T6567Trypsin from porcine pancreas, Proteomics Grade, BioReagent, DimethylatedSDS
- Trypsin Solubilization Reagent
Regulatory Information
新产品
Certificates of Analysis (COA)
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Maria V Turkina et al.
Methods in molecular biology (Clifton, N.J.), 355, 305-316 (2006-11-10)
Reversible protein phosphorylation is crucially involved in all aspects of plant cell physiology. The highly challenging task of revealing and characterizing the dynamic protein phosphorylation networks in plants has only recently begun to become feasible, owing to application of dedicated
Thomas Nühse et al.
Current protocols in molecular biology, Chapter 18, Unit 18-Unit 18 (2008-02-12)
The identification of protein phosphorylation sites from cell-derived proteins is crucial to the understanding of signal transduction pathways. While determining the modified sites on individual proteins can present a significant challenge, recent progress in the rapid, large-scale identification of phosphopeptides
Yeong Hee Ahn et al.
Rapid communications in mass spectrometry : RCM, 18(20), 2495-2501 (2004-09-24)
The enrichment of phosphopeptides using immobilized metal ion affinity chromatography (IMAC) and subsequent mass spectrometric analysis is a powerful protocol for detecting phosphopeptides and analyzing their phosphorylation state. However, nonspecific binding peptides, such as acidic, nonphosphorylated peptides, often coelute and
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