Anti-SUMO-2/3 Antibody, clone 8A2 clone 8A2, from mouse

Small ubiquitin-related modifier 2 (UniProt P61956; also known as HSMT3, Sentrin-2, SMT3 homolog 2, Smt3B, SUMO-2, Ubiquitin-like protein SMT3B) and 3 (UniProt P55854; also known as SMT3 homolog 1, Smt3A, SUMO-3, Ubiquitin-like protein SMT3A) are encoded by the SUMO2 (also known as SMT3B, SMT3H2; Gene ID 6613) and SUMO3 (also known as SMT3A, SMT3H1; Gene ID 6612) genes in human. SUMOylation, protein post-translation modification by small ubiquitin-like modifier (SUMO), is a signaling event in many cellular processes. SUMO proteins are translated as immature precursors and subsequently converted to their mature forms through the activity of sentrin/SUMO-specific proteases (SENPs). SUMOylation is a reversible process. SUMO E1 activating enzyme, E2 conjugating enzyme, and E3 ligase mediate SUMOylation of substrate proteins, while SENPs are responsible for the de-SUMOylation. SUMOylation usually occurs at lysine residues in the consensus KxD/E motif, although not all such lysines become SUMOylated and SUMOylation can also occur on lysine residues outside of this motif. SUMO2 and 3 share 97% identity at the amino acid level, while SUMO1 shares only about 50% sequence homology with SUMO-2 and 3. In addition to difference in their target substrates, SUMO2/3 can be SUMOylated and form chains, whereas SUMO1 cannot and may serve as chain terminator. SUMO-2 can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Its covalent attachment to its substrate via an isopeptide bond 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, CBX4 or ZNF451. 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. Although SUMO-2 functions in a manner similar to ubiquitin in that it is bound to target proteins as part of a post-translational modification system, however, unlike ubiquitin which targets proteins for degradation, SUMO-2 is involved in a variety of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability. It is not active until the last two amino acids of the carboxy-terminus (aa 94-95; propeptide) have been cleaved off.