PhosphoScan® Phosphorylation Proteomics

The reversible addition of phosphate groups by protein kinases can activate or inhibit protein function. Phosphorylation signaling cascades, for example the MAP kinase signaling pathways, are important for transmitting information from outside to inside the cell where it ultimately results in modulation of gene transcription. Aberrant phosphorylation is widespread in diseases including cancer, diabetes, and neurodegeneration. Therefore, identifying the phosphorylation status of proteins is crucial to understanding cellular processes in both health and disease.

Apply PhosphoScan^® proteomics for

• Pathway profiling
• Biomarker discovery
• Target validation

Why consider antibody enrichment for phosphorylation proteomics?

• More focused discovery of phosphosites based on amino acid (S/T/Y) or motif of interest than IMAC.
• PTMScan^® methods and IMAC enrich different pools of phosphopeptides making them highly complementary. For the most complete dataset customers should use both types of enrichment. View data.

Profiling tyrosine phosphorylation in MKN-45 cells. Peptides from MKN-45 cells treated for 2hr with DMSO (control), 1 μM SU11274 ,or 200 nM Staurosporine #9953 for were enriched using the PTMScan® Phospho-Tyrosine Rabbit mAb (P-Tyr-1000) Kit #8803 (above). In parallel, total protein levels were profiled by running unenriched material in LC-MS/MS (below). Peptides that decreased in abundance with SU11274 or Staurosporine are indicated in red, peptides that increased with treatment in green. A % CV histogram of analytical replicates for each enrichment is shown on the right with the median % CV indicated in blue.