• Together with a series of papers and preprints published this year, it establishes RNF114 as a reader of ADPrUb

• Observation that serine mono-ADPrUb increases in ARH3 KO cells, raising the intriguing question of its potential role in ARH3 mutation–associated neurodegeneration

• First reagent specific for ADPrUb, enabling both immunoblotting and immunoprecipitation

• First mass spectrometric evidence of ADPrUb, regardless of the target residue

• Serine mono-ADPrUb as a new type of DNA damage-induced histone modification

• First evidence that, in cells, serine mono-ADPr by the PARP1/HPF1 writer complex is targeted by this unconventional ubiquitylation

These new antibody development efforts align with our vision that the fundamental discovery of Serine ADP-ribosylation can be converted into a technology that transforms the study of ADP-ribosylation and related PTMs.

This preprint is part of a larger manuscript on additional antibodies and their applications to biological questions. The goal of this preprint is to share these poly-ADPr with the community without delay, as we believe they wil benefit many laboratories.

As with our other tools, the AbD64138 clone should become widely accessible in a few months. For those familiar with our popular AbD43647 antibody, the new AbD64138 clone provides similar advantages for poly-ADPr as AbD43647 does for mono-ADPr.

We’re particularly excited to share with the community the exceptionally high sensitivity we’ve achieved for poly-ADPr immunoblotting, all while using a faster and simpler protocol enabled by a sophisticated SpyTag-HRP format that eliminates the need for secondary antibodies.