Anti-SUMO2/3 Antibody

Small ubiquitin-like modifiers (SUMOs) are a family of small, related proteins (Sumo-1/2/3/4) that can be enzymatically attached to a target protein by a post-translational modification process termed sumoylation, which is a major regulator of protein function in cellular processes such as nuclear transport, transcriptional regulation, apoptosis and protein stability. All SUMO proteins localize to the nucleus and are covalently conjugated, affecting protein structure, function and interactions. SUMO2 and 3 are 96% identical and are more mobile within nucleus relative to SUMO1. Specific functional differences between SUMO1 and SUMO2 and 3 remain to be identified.

SUMO2/3 antibody was raised against a 15 amino acid synthetic peptide near the carboxy terminus of human SUMO2. The immunogen is located within the last 50 amino acids of SUMO2/3.

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, CBX4 or ZNF451 (PubMed:26524494) . 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) .