Protein identification, post-translational modifications (PTMs)

We make use of high resolution protein mass spectrometry to identify proteins, their primary sequences, and PTMs (e.g. phosphorylation, Lys-acetylation, ubiquitination, proteolytic cleavage, glycosylation) from a broad range of samples, from purified proteins and protein complexes, to gel bands, IPs, BioID experiments, organelles, cells, tissues (fresh-frozen and FFPE), and biofluids.

Label free quantitation (LFQ), isobaric tags (TMT, iTRAQ), targeted MS (MRM, PRM)

We use a range of technologies for the relative (discovery) and absolute quantitation (validation) of proteins and PTMs in biological samples, from as little as 3 samples per condition to hundreds of samples. Robust experimental and computational workflows enable us to identify candidate proteins and PTMs that are significantly regulated between samples.

Our targeted MS assays enable the multiplexed, precise quantitation of protein concentrations of 100s of proteins through the use of stable isotope labeled standard (SIS) peptides as internal standards.

Clinical assays for proteins, metabolites, and drugs, therapeutic drug monitoring (TDM)

We develop mass spectrometry-based assays of medical interest and implement these in a clinical setting.  Applications include assays for metabolites and proteins of diagnostic value, and therapeutic drug monitoring.  We further translate proteomics and metabolomics approaches for the clinical use, such as robust assays for the precise quantitation of cancer proteins in tumor tissues (FFPE and fresh-frozen) with ultra-high sensitivity.