Interactomics

Protein interaction (PI) is the fundament of nearly every process in living cells. Dysregulation of protein organization and its interplay is coupled to many human diseases. We offer interactome studies including conventional methods like affinity purification coupled to MS (AP-MS) which are mainly suitable for strong protein-protein interactions. Chemical cross-linking of protein complexes (XL-MS) enable the study of more complex and larger interactomes by capturing snap shots of trasient interactions. More recently, we added methods using proximity labeling techniques with biotin ligase (BioID) or ascorbate peroxidase (PL-APEX), which enable excellent depth and coverage of protein-protein interactions. These affinity-based methods can be complemented by biochemical separation techniques (termed co-elution or protein correlation profiling), where mild solubilization preserves protein complexes which can be size-fractionated before quantitative MS.

Beside protein-protein interaction profiling, we also offer profiling of DNA-bound protein (complexes), RNA-bound protein (complexes; RBPome studies) as well as quality control of antibodies by independent target validation.