Phosphoprotein/Peptide Analysis [S-0033]
Phosphopeptide identification
Identifying posttranslational modifications including phosphorylation is a necessary prerequisite to elucidating the role of a protein in a signaling pathway or in other biochemical pathways. We have extensive experience in method development for enriching phosphopeptide using either Titanium dioxide (TiO2) or Immobilized Metal Affinity Chelate (IMAC) enrichment approach. Apart from TiO2 or IMAC approaches, we also have the capability of using SCX fractionation for phosphopeptide fractionation / enrichment. To obtain good MS/MS, we monitor neutral loss in our MS/MS and trigger MS/MS/MS automatically on observing 98 Da loss for phosphoric acid.
Our peptide sequencing, protein identification and Phosphopeptide mapping services by tandem mass spectrometry includes:
a) Titanium dioxide (TiO2) or Immobilized Metal Affinity Chelate (IMAC) Enrichment,
b) Tandem mass spectrometry analysis using nano-LC/MS/MS,
c) Database search.
Cost is per sample.
Contact Us for more information on this service.
LC/MS/MS SERVICES
- Protein Identification & Characterization by LC/MS/MS [S-0030]
- In-gel digestion of protein spot with protein sequencing by mass spectrometry [S-0010.2]
- In-solution digestion of protein sample with sequencing by mass spectrometry [S-0031]
- Post Translational Modification Mapping by Mass Spectrometry [S-0032]
- Phosphoprotein / Peptide Analysis [S-0033]
- SCX Mudpit Analysis [S-0034]
- iTRAQ Mass Spectrometry Service [S-0037.1]
- Analysis of Serum/Plasma after depletion of 14 abundant proteins using lgY column[S-0037.2]
- Analysis of Serum/Plasma after depletion of Albumin and lgG using the ASKc Column[S-0037.2]
- Mass Spectrometry Analysis of Urine Samples [S-0038.1]
*Example
Fig 1. Precursor mass selected for MS/MS fragmentation.
Fig 2. Most abundant peak represents a loss of phosphoric acid (98 Daltons/2 = 49 due to the fact that the peptide has a +2 charge state).



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