Our Quantitative Proteome-Wide PTM Profiling
service is designed for the identification and quantification of protein PTMs (phosphorylation, acetylation, methylation, and ubiquitination) from either a cell culture or tissue samples. A denaturing protein lysate is generated from the sample and the resulting protein(s) are digested with trypsin (or other protease) to produce peptide fragments that are immunoaffinity enriched for the appropriate PTM containing peptides. The resulting peptides are analyzed by LC-MS/MS for identification and quantification to determine relative PTM peptide abundance between control and treatment conditions.
How Can Lighthouse Proteomics Assist You With Your Research?
- Characterize quantitative changes in protein PTMs related to cell phenotype
- Quantify protein PTM changes related to treatment condition
- Quantitatively monitor global protein PTM levels upon compound treatment
- Explore effect of compound treatment to phospho-signaling (or other PTMs)
- Monitor protein-PTM status through a series developmental stages
- Identify key protein-PTMs for biomarker discovery
- Identify regulated protein-PTMs to explore mechanism of action
- Monitor protein PTMs within specific signaling pathway
- Examine extent of cross-talk among different PTMs
- Explore mechanism-of-action of drug
- Identify PD biomarkers to monitor drug response or efficacy
- Monitor status of Histone PTMs in response to compound treatmenty
flash frozen tissue, cell culture slurry or cell pellet
Protein quantification with high resolution LC-MS/MS technology
A data package will be provided electronically in the form of an XLS result table(s) and a PowerPoint summary report. The data package is also accompanied with a consultation to review the results with you and address any questions you have about the analysis.
Phosphorylation: S, T, Y; Acetylation; Succininylation; Methylation &