Mass photometry to study the oligomerization of the ubiquitin ligase HACE1

Ubiquitin ligases (E3) are therapeutically relevant enzymes that orchestrate many key cellular pathways. This makes it important to understand the mechanisms that regulate their activity and substrate specificity.

In this webinar, Sonja Lorenz – Group Leader at the Max Planck Institute for Multidisciplinary Sciences – explains how she used mass photometry for the study of the HACE1 ubiquitin ligase. In her work, mass photometry complemented cryo-EM and other biophysical techniques by characterizing the oligomerization behavior of WT HACE1 and several mutational variants at nanomolar concentrations, which helped to reveal dimerization as the key regulatory mechanism for HACE1.

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FURTHER RESOURCES:

TwoMP product page - https://www.refeyn.com/twomp-mass-pho...

TwoMP Auto product page - https://www.refeyn.com/twomp-auto-mas...

Blog - Mass photometry saves you time and money in cryo-EM experiments  - https://www.refeyn.com/post/mass-phot...

Blog - Studying protein oligomerization with mass photometry - https://www.refeyn.com/post/studying-...

Webinar - Characterizing protein oligomerization dynamics with automated mass photometry -    • Characterizing protein oligomerizatio...  

Webinar - Harnessing mass photometry for AAV sample characterization in GMP-regulated environments -    • Harnessing mass photometry for AAV sa...  


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