Anti-ARH3 antibody - C-terminal,Abcam,AB199171

Target data ADP-ribosylhydrolase that preferentially hydrolyzes the scissile alpha-O-linkage attached to the anomeric C1'' position of ADP-ribose and acts on different substrates, such as proteins ADP-ribosylated on serine and threonine, free poly(ADP-ribose) and O-acetyl-ADP-D-ribose (PubMed : 21498885, PubMed : 29907568, PubMed : 30045870, PubMed : 30401461, PubMed : 30830864, PubMed : 33186521, PubMed : 33769608, PubMed : 33894202, PubMed : 34019811, PubMed : 34321462, PubMed : 34479984, PubMed : 34625544). Specifically acts as a serine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to serine residues on proteins, thereby playing a key role in DNA damage response (PubMed : 28650317, PubMed : 29234005, PubMed : 30045870, PubMed : 33186521, PubMed : 34019811, PubMed : 34625544). Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (PubMed : 29480802, PubMed : 33186521, PubMed : 34625544). Does not hydrolyze ADP-ribosyl-arginine, -cysteine, -diphthamide, or -asparagine bonds (PubMed : 16278211, PubMed : 33769608). Also able to degrade protein free poly(ADP-ribose), which is synthesized in response to DNA damage : free poly(ADP-ribose) acts as a potent cell death signal and its degradation by ADPRHL2 protects cells from poly(ADP-ribose)-dependent cell death, a process named parthanatos (PubMed : 16278211). Also hydrolyzes free poly(ADP-ribose) in mitochondria (PubMed : 22433848). Specifically digests O-acetyl-ADP-D-ribose, a product of deacetylation reactions catalyzed by sirtuins (PubMed : 17075046, PubMed : 21498885). Specifically degrades 1''-O-acetyl-ADP-D-ribose isomer, rather than 2''-O-acetyl-ADP-D-ribose or 3''-O-acetyl-ADP-D-ribose isomers (PubMed : 21498885). See full target information ADPRS