Enrichment of phosphorylated peptides derived from phosphorylated proteins can be used when studying the cellular processes of enzyme activation or inactivation, cell signalling and protein-protein interactions.
|Research Objectives||Phosphoproteome analysis|
Phosphorylated proteins are implicated in various cellular processes such as enzyme activation/inactivation, cell signalling and protein-protein interactions. Phosphorylated proteins are investigated by using phosphorylated peptides derived from the original proteins. Phosphoproteomics can provide an indication of which protein or pathway is activated since a change in phosphorylation status is generally indicative of a change in protein activity. In addition, information derived from phosphoproteomics can help identify proteins that could be effective drug targets.
Phosphorylated peptides are generally found in low abundance. Several strategies have therefore been developed for phosphopeptide enrichment. The CPGR offers phosphopeptide enrichment using titanium dioxide (TiO2) beads (ReSyn), gallium(III) and iron(III) resins. Protein samples supplied by the client re digested using trypsin and the phosphorylated peptides extracted using an affinity medium. The enriched sample is then submitted for LC-MS analysis.
An analytical report will be provided detailing the experimental steps taken to enrich and identify the phosphopeptides and consequently the phosphorylated protein(s). The phosphopeptide enriched samples will also be supplied along with a polyacrylamide gel of the protein extract.
- Samples must be shipped on ice.