SENP8. also known as DEN1/NEDP1. is a member of the sentrin/SUMO-specific protease (SENP) family, which regulates post-translational protein modification by cleaving ubiquitin-like modifiers. Unlike most SENPs that primarily process small ubiquitin-like modifier (SUMO) proteins, SENP8 specifically hydrolyzes the ubiquitin-like protein NEDD8 (neural precursor cell expressed, developmentally downregulated 8) from conjugated substrates. This activity is critical for modulating the neddylation pathway, a process analogous to ubiquitination that regulates protein stability, localization, and function. SENP8-mediated deneddylation counteracts the activity of NEDD8-conjugating enzymes, thereby influencing key cellular processes such as cell cycle progression, DNA repair, and stress responses. Notably, SENP8 plays a regulatory role in the Cullin-RING ubiquitin ligase (CRL) family by removing NEDD8 from Cullin proteins, which is essential for maintaining CRL activity and substrate turnover.
Antibodies targeting SENP8 are vital tools for studying its expression, localization, and function in biological systems. They enable detection of SENP8 in immunoassays (e.g., Western blot, immunoprecipitation) and visualization in cellular or tissue contexts (e.g., immunofluorescence, immunohistochemistry). Research using SENP8 antibodies has elucidated its involvement in diseases such as cancer, where dysregulated neddylation contributes to tumorigenesis, and neurodegenerative disorders linked to protein aggregation. These antibodies also aid in exploring SENP8’s crosstalk with other post-translational modification pathways, including ubiquitination and SUMOylation. Due to SENP8’s specificity for NEDD8. its antibodies are distinct from those targeting SUMO-directed SENPs, emphasizing the need for rigorous validation to ensure specificity in experimental models.