Advance your drug discovery using UbiQ’s reagents enabling lead on target validation and lead optimization. Our reagents can be used for various applications and targets within the ubiquitin proteasome system. Beside our catalogue reagents we offer the service to develop highly specialized custom reagents.
- target inhibitor profiling (affinity, selectivity, and specificity profiling)
- chemical proteomics
- E1, E2, E3 enzymes
- DUBs and Ubl proteases
activity assay reagents
UbiQ-Assay reagents enable compound library screening and activity assays for DUBs & Ub-like proteases. They are available in various flavors for a wide range of assay read outs, e.g. fluorescence intensity read-out, fluorescence polarization and FRET.
See UbiQ-Assay fact sheets for more information, available options and references
UbiQ’s wide selection of activity-based probes make it possible to crystallize, identify and validate dozens of enzymes as potential targets involved in protein ubiquitination and de-ubiquitination, as well as lead on target validation.
See UbiQ-Probes fact sheets for more information, available options and references
all 8 natively-linked di-ubiquitin chains
UbiQ is the original and only manufacturer of all 8 di-ubiquitin chain linkages. Access to all 8 linkages is key to further investigating their biological roles:
- study linkage specificity of DUBs
- study ubiquitin-associated domains or ubiquitin-interacting motifs (UIMs)
See UbiQ-Chains fact sheets for more information, available options and references.
custom ubiquitinated peptides
UbiQ provides ubiquitinated peptides with a range of custom modifications to meet your research needs. Peptides up to 20 amino acids long are site-selectively ubiquitinated via a native isopeptide link using our proprietary Ub ligation technology. These can be used for:
- epitope mapping (e.g. with DUBs) and immunization
- peptide pull-down experiments (proteomics)
- ligand for X-ray analysis of proteins
> See UbiQ-PEP fact sheets for more information, available options and references.