Small Ubiquitin-Related Modifier 2 (SUMO2) is an Ubiquitin-like protein that belongs to the ubiquitin family with SUMO subfamily. It is a family of small, related proteins that can be enzymatically attached to a target protein by a post-translational modification process termed sumoylation. SUMO2 can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Covalent attachment via an isopeptidebond 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.

SUMO3 Protein, Human, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 18 KDa and the accession number is P55854.

SUMO3 Protein, Human, Recombinant (E.coli, His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 19 KDa and the accession number is P55854.

Small ubiquitin-like modifier (SUMO), also known as SUMO homologue and SMT3, is a member of the superfamily of ubiquitin-like polypeptides that become covalently attached to various intracellular target proteins as a way to alter their function, location, and/or half-life. Small ubiquitin-like modifiers include SUMO1, SUMO2, SUMO3, and SUMO4. Except for SUMO4, all other SUMOs are ubiquitously expressed, including in the brain. In human, SUMO2 and SUMO3 are two highly homologous proteins, collectively called SUMO2/3. Several studies suggest that SUMO3 are associated with pathogenesis in several neurological diseases, including Alzheimer's disease, Parkinson's disease, and cerebral ischemia/stroke.