THE PROTEOMICS CORE FACILITY

The Proteomics Core Facility (PCF) of the Medical Faculty Mannheim of the University of Heidelberg is sited in building 22. It provides a full proteomics infrastructure for the identification, characterization and quantification of proteins and small molecules such as peptides, metabolites and xenobiotica.

The infrastructure of the PCF comprises a variety of instrumentations including different mass spectrometers to enable in depth analysis of complex specimens.

This website wants to give crucial information for sample submission to the PCF and a collection of protocols for sample preparation is provided. However, it is strongly recommended to involve the PCF at an early timepoint of the experimental planning. The PCF can give valuable advice for optimization of preanalytical conditions and experimental bias that is related to unwanted degradation of analytes can be avoided. Furthermore the PCF is offering support related to data-analysis and -interpretation.

If you are missing specific information, please do not hesitate and contact any member of the PCF-staff to answer your questions.

SERVICES

The Proteomics Core Facility offers a range of techniques for the identification, characterization and quantification of very complex clinical specimens and even whole proteomes. However, also more focused approaches for protein characterization and quantification are also available. Furthermore various small molecules (metabolites, xenobiotica) can also be analyzed.  The following topics are highlighting the most frequent applications.

Proteomics:

  • Identification of proteins in complex mixtures (serum, plasma, other body fluids,  tissue, cell culture)
  • Multi-dimensional peptide separation (isoelectric focusing and liquid chromatography)
  • Identification of post-translational modifications.
  • Enrichment of phosphopeptides (TiO2 and IMAC)
  • Identification of proteins Protein quantification by stable-isotope labeling (SILAC, TMT and dimethyl labelling)
  • Protein quantification by label-free approaches and differential display analyses

Analysis of intact proteins:

  • Molecular weight determination (coomassie and silver-stained gels)
  • Determination of N- and C-termini of proteins and products of limited proteolysis
  • Verification of incorporation of non-natural amino acids