Small Ubiquitin-Related Modifier (SUMO) proteins are a family of ubiquitin-like proteins that play a crucial role in various cellular processes through a post-translational modification known as SUMOylation. SUMOylation involves the attachment of SUMO proteins to target proteins, influencing their stability, activity, and subcellular localization. SUMO2 and SUMO3 are two closely related members of this family, often referred to collectively as SUMO2/3 due to their high sequence similarity and functional overlap.
The SUMOylation process is a multi-step enzymatic cascade that includes activation, conjugation, and ligation. It begins with the activation of SUMO proteins by the E1 activating enzyme, followed by their transfer to the E2 conjugating enzyme. Finally, the E3 ligase enzyme facilitates the attachment of SUMO proteins to specific lysine residues on target proteins. This modification can be reversed by SUMO-specific proteases, allowing for dynamic regulation of protein function.
SUMO2/3 proteins are involved in a wide range of cellular processes, including:
One notable interaction of SUMO2/3 is with the p65 subunit of NF-κB, a key regulator of immune and inflammatory responses. Research has shown that SUMO2/3 can stabilize p65 in the cytoplasm, preventing its translocation to the nucleus and subsequent activation of NF-κB target genes . This interaction has implications for various diseases, including hepatocellular carcinoma (HCC), where SUMO2/3-p65 interaction may play a role in tumorigenesis .
Mouse anti-human SUMO2/3 antibodies are monoclonal antibodies specifically designed to detect human SUMO2/3 proteins. These antibodies are widely used in research to study the expression, localization, and function of SUMO2/3 in various biological contexts. They are valuable tools for techniques such as immunohistochemistry, immunofluorescence, and co-immunoprecipitation, enabling researchers to investigate the role of SUMO2/3 in health and disease.