PARP8 (Poly(ADP-ribose) polymerase 8) is a member of the PARP enzyme family, which catalyzes the transfer of ADP-ribose units to target proteins, influencing processes like DNA repair, chromatin remodeling, and stress response. Unlike well-characterized PARPs (e.g., PARP1/2), PARP8 remains understudied, though it shares the conserved catalytic PARP domain. Emerging evidence suggests PARP8 localizes to the cytoplasm and nucleus, potentially regulating transcription, cell cycle progression, and mitochondrial function. Its expression is tissue-specific, with higher levels observed in the brain, liver, and testes.
PARP8 antibodies are critical tools for investigating its expression, localization, and molecular interactions. These antibodies, often raised against unique epitopes in its N-terminal or catalytic domains, enable applications such as Western blotting, immunofluorescence, and immunoprecipitation. Researchers use them to study PARP8's role in diseases, including cancer, where dysregulated PARP8 expression has been linked to tumor progression and therapy resistance. For instance, PARP8 overexpression in glioblastoma or hepatocellular carcinoma correlates with poor prognosis, suggesting its potential as a therapeutic target.
Challenges in PARP8 research include antibody specificity due to homology with other PARP family members. Recent studies highlight PARP8's distinct substrate preferences and its possible crosstalk with PARP inhibitors like olaparib, though its exact mechanistic contributions remain unclear. Validating PARP8 antibodies with knockout controls is essential to ensure reliability. Ongoing work aims to clarify PARP8's physiological and pathological functions, leveraging these antibodies to explore its interplay with cellular stress pathways and therapeutic potential.