Protein-protein interactions are a hallmark of signal transmission and key to understanding regulatory mechanisms. Therefore, we developed the Protein Interaction Screen on Peptide Matrix (PRISMA) together with our partners from Max-Delbruck-Center for Molecular Medicine (MDC) to systematically explore the interactome.
- Peptides are synthesized on a cellulose membrane
- Peptides of up to 25 amino acids length may represent sequence diversity and contain post-translational modifications
- The membrane is incubated with a biological sample for affinity enrichment of soluble proteins and protein complexes
- Proteins interacting with the peptide matrix are then identified and quantified by mass spectrometry
- Identification of protein-protein interaction partners
- Systematic exploration of the interactome
- Decode the influence of post-translational modifications
- Discovery of the influence of sequence diversity on protein interactions
- Comparison of cell states
- Identification of complexes
- Mapping of pathways
- Hundreds of protein interactions can be detected and identified as potential interaction partners
- Modulatory effects of numerous different PTMs and mutations can be assessed
- Validated assay based on comparison with other affinity enrichment approaches, conventional immunoblotting analysis, and co-occurrence
- Quantification of proteins possible
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The Human Proteome Peptide Catalog
More than 400,000 validated reference peptides covering essentially all human proteins