NIH Research Festival
We are experts in mass spectrometry based proteomics for identification and quantitation of proteins and their posttranslational modifications (PTM). Our workflows for relative protein quantitation are based on label-free, SILAC and TMT approaches. We can also help investigators identify and quantify protein posttranslational modifications, including phosphorylation, nitrosylation, acetylation, ubiquitination, succinylation, etc. We provide training in proper sample preparation and lead the researchers through mass spectrometric analysis to data searching and interpretation. Users have access to a variety of proteomics software platforms (Mascot, Proteome Discoverer, Sequest, Scaffold) for re-searching the data or viewing the results. We offer the following types of analyses: -Protein identification (from in-solution, 1D/2D gel) -Relative protein quantitation (label-free, SILAC, TMT, DIGE) -Peptide/protein fractionation using gels, offline basic reversed LC, IEF or SCX -Protein post-translational modifications – identification and relative quantification (phosphorylation, acetylation, succinylation, malonylation, nitrosylation, ubiquitination, nitration, SUMO, sulfhydration, proline oxidation) -Serum depletion and protein identification/quantification -We work with investigators on custom projects (either targeted proteins or systems biology approaches) Our research is focused on developing new approaches for PTM characterization and absolute protein quantitation (e.g. measuring occupancy of nitrosylation with cys-TMT tags, acetylation occupancy, tissue ubiquitination and absolute quantification of a mitochondrial protein panel).
Scientific Focus Area: Research Support Services
This page was last updated on Friday, March 26, 2021