HERC5 (HECT and RLD domain containing E3 ubiquitin protein ligase 5) is a member of the HERC family of ubiquitin ligases, which play critical roles in protein post-translational modification. Primarily studied in humans, HERC5 is unique for its dual functionality: it acts as an E3 ubiquitin ligase and mediates ISG15 (interferon-stimulated gene 15) conjugation, a process termed ISGylation. This enzyme is strongly induced by type I interferons during viral infections, linking it to innate immune responses. HERC5 targets viral and host proteins for ISGylation, which can disrupt viral replication or modulate immune signaling pathways.
HERC5 antibodies are essential tools for investigating its expression, localization, and interactions in immune regulation, antiviral defense, and cancer. Researchers use these antibodies in techniques like Western blotting, immunofluorescence, and immunoprecipitation to study HERC5's role in stress responses, cell cycle regulation, and its potential tumor-suppressive or oncogenic effects in various cancers. Dysregulation of HERC5 has been implicated in diseases such as hepatitis, autoimmune disorders, and malignancies, making its study clinically relevant. Antibody specificity is critical due to structural similarities among HERC family members. Recent studies also explore HERC5's involvement in mRNA translation regulation during interferon responses, highlighting its multifaceted roles in cellular physiology.