Profile the ubiquitination pathway
Ubiquitination is a key regulatory mechanism which attaches the small protein modifier ubiquitin to protein substrates, thereby modifying their structure, function, cellular location, or targeting them for destruction via proteolysis. Inappropriate regulation of ubiquitination pathways is linked with a number of human diseases. In recent years, components of these pathways have emerged as a new and relatively untapped class of targets for drug discovery, with applications in cancer, neurodegenerative disorders such as Alzheimer's and Parkinson's disease, viral infection, diabetes, and inflammation.
Eurofins has removed the complexity of drug discovery in this emerging area by providing assays for both ubiquitination and de-ubiquitination, with off-the-shelf assays for functional E3 ligase cascades, we have made this target class readily accessible for research and drug discovery.
Advantages of Ubiquitin Profiling with Eurofins:
Figure 1. Ubiquitination Pathway
The ubiquitination pathway consists of three sequential steps: 1) an ATP dependent step of loading E1 activating enzyme with ubiquitin, 2) transfer of the E1's ubiquitin to an E2 conjugating enzyme and 3) the E3 ligase-mediated transfer of ubiquitin from an E2 to the substrate. This process can be repeated to polyubiquinate a substrate, leading to its proteasome mediated degradation, whereas monoubiquitinated targets (e.g., cell surface receptors) will have altered signaling properties.