Proteomics and Mass Spectrometry

The Proteomics Core will provide targeted and untargeted, quantitative proteomics analysis of various biological samples (i.e., serum, plasma, urine, saliva, cell culture and tissues). Typhoon FLA 7000

The facility will be fully equipped with state-of-the-art mass spectrometers coupled to high-resolution HPLC systems and software tools required for identification of proteins from complex mixtures, to monitor their post-translational modifications and to quantify their abundance across various samples. The core also has the capabilities to analyse and quantify small peptides, carbohydrates and lipids. As part of these efforts, the core also uses quantitative proteomics technologies to map the interacting partners or interactome of a given target (protein-protein, protein-nucleic acid, and protein-small molecule) together with an array of complementary experiments to validate these interactions (BiaCore/surface plasmon resonance "SPR", Time-resolved fluorescence resonance energy transfer "TR-FRET", Fluorescence polarization "FP" and Far Western). Such efforts will enable the development of models that predict the dynamic behaviour of living systems.

Services

Global and targeted, label-free differential proteomics analysis of various biological samples.
Gel-based Proteomics using 1D-SDS-PAGE, 2D-PAGE, 2D-DIGE.
Protein identification and characterization using silver, Coommassie or Sypro ruby.
Mass Spec-based characterization of post-translational modifications.
Mass Spec-based peptide sequencing.
Molecular weight-based pre-fractionation of complex samples for protein identification.
Advices on sample preparation for a wide range of sample types and protein compartments.
Identification of unknown partners of interaction (affinity chromatography, tandem affinity purification, pull-down, co-immunoprecipitation).
Analysis, statistics, and bioinformatics for Proteomics data streams.