Electron-based dissociation (ExD) methods have a long history in aiding the characterization of biomolecules. The electron-capture dissociation (ECD) method primarily cleaves peptide backbone, resulting in c and z ions, thus obtaining a higher sequence coverage compared to the traditional collision-induced dissociation (CID). Besides, ECD leaves the side chain intact, making this dissociation method useful in identifying post-translational modifications of proteins. Hot ECD (hECD), which employs higher kinetic energy, enables secondary dissociation, which can, for instance, differentiate leucine and isoleucine. However, conventional ExD methods, such as ECD and electron-transfer dissociation (ETD), mainly dissociate multiply charged ions, leaving singly or doubly charged ions less accessible to dissociation. Recently, EAD, which comprises of ECD and hECD, was shown to be flexible in dissociating ions with a wide range of charge states. The enzymatic digestion of ADCs yields peptides with various length and small molecule linker-payloads, making EAD highly valuable for the characterization of ADCs, where the dissociation of differently protonated species may be achieved.