SUMO (Small Ubiquitin-like Modifier) proteins are a family of ubiquitin-like molecules that post-translationally modify target proteins to regulate their activity, localization, or interactions. The SUMO family includes SUMO1. SUMO2. and SUMO3. with SUMO2 and SUMO3 sharing ~97% sequence identity and often referred to collectively due to their functional redundancy. SUMOylation involves covalent conjugation of SUMO to lysine residues on substrate proteins via an enzymatic cascade, influencing diverse cellular processes like nuclear transport, DNA repair, transcriptional regulation, and stress responses.
Antibodies targeting SUMO2/3 are critical tools for studying SUMOylation dynamics. These antibodies detect either free SUMO2/3 or SUMO-conjugated proteins, enabling researchers to investigate SUMOylation in contexts such as cellular stress, cell cycle progression, or disease states. Unlike SUMO1. SUMO2/3 can form poly-SUMO chains, which are implicated in stress responses and protein degradation pathways. Specificity is a key consideration, as some antibodies distinguish SUMO2 from SUMO3. while others recognize both isoforms.
SUMO2/3 antibodies are widely used in techniques like Western blotting, immunofluorescence, and immunoprecipitation to map SUMOylation sites, identify substrates, or explore crosstalk with other post-translational modifications. Dysregulation of SUMO2/3 modification is linked to cancer, neurodegeneration, and viral infection, making these antibodies valuable for both basic research and therapeutic target discovery. Their utility also extends to validating SUMO protease activity or assessing the effects of SUMOylation inhibitors in experimental models.