Learn more about how researchers are using
Dianthus to evaluate the affinity and specificity
of their PROTAC candidates here:
nanotempertech.com/dianthus-for-protacs/
Does my target become ubiquitinated?
Once the ternary complex has formed and
the E3 ligase and target protein are in close
proximity, the E3 ligase needs to catalyze the
ubiquitination of the target protein.
You commonly track these steps by
performing ubiquitination assays in live cells,
utilizing the cell's own machinery to detect
ubiquitination under native conditions. On the
other hand, you can use cell-free systems, such
as immunoblotting of immunoprecipitated
proteins or mass spectrometry.
Targeted protein degradation is an exciting new direction in the field of drug discovery, but you still
have to overcome many hurdles in order to work with the most challenging targets. Therefore, when
exploring protein degrader compounds, make sure to ask yourself these questions. They will help you
address common roadblocks present in key steps of the degradation pathway — so that you make
sure your final product results in a complete protein degradation.
Does the ubiquitination drive the protein to
be degraded by the proteasome?
Ubiquitination of a protein target marks it for
degradation via the ubiquitin proteasome
system, or UPS. But the success of your
PROTAC is ultimately assessed by the complete
degradation of your target protein.
You can use methods like Western blot or mass
spectrometry — which detect intracellular
protein levels — to evaluate the degree of
degradation of your protein target.
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