Anti-SUMO2/3, clone SM23/496

1 mg/ml in sterile PBS, BSA free, sodium azide free. This antibody reacts with both SUMO2 and SUMO3. The small ubiquitin-related modifier (SUMO) proteins, which include SUMO1, 2 and 3, belong to the ubiquitin-like protein family. Like ubiquitin, the SUMO proteins are synthesized as precursors that undergo processing before conjugation to target proteins. Also, both utilize the E1, E2 and E3 cascade enzymes for conjugation. However, SUMO and ubiquitin differ with respect to targeting. Ubiquitination predominantly targets proteins for degradation, whereas sumoylation targets for a variety of cellular processing, including nuclear transport, transcriptional regulation, apoptosis and protein stability. The unconjugated SUMO1/2/3 proteins localize to the nuclear membrane, nuclear bodies and cytoplasm, respectively. SUMO1 utilizes Ubc9 for conjugation to several targets, which include MDM2, p53, PML and RanGap1. SUMO2 and 3 contribute to a greater percentage of protein modification than does SUMO1 and they can form polymeric chains. In addition, SUMO3 regulates beta-Amyloid generation and may be critical in the onset or progression of AlzheimerÆs disease. Protein function: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Polymeric SUMO2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins (PubMed:18408734, PubMed:18538659, PubMed:21965678, PubMed:9556629). Plays a role in the regulation of sumoylation status of SETX (PubMed:24105744). [The UniProt Consortium]