SUMO-1 Mutant Protein Set

Catalog #: K-712

The ubiquitin-like SUMO-1, SUMO-2 and SUMO3 proteins are conjugated to a variety of proteins in the presence of UbcH9 and the SAE1/SAE2 (human) or Aos1/Uba2 (yeast) activating enzyme. SUMO modification has been implicated in diverse functions such as nuclear transport, chromosome segregation and transcriptional regulation, apoptosis and protein stability. Human SUMO-1 shares 46% and 47% identity with SUMO-2 and SUMO-3 respectively and does not contain the exact ψΚXE consensus sequence found in SUMO-2 and SUMO-3. Within this sequence ψ represents a large hydrophobic amino acid (I, L, or V), K is the lysine that becomes modified, X is any residue and E is glutamic acid. Many known SUMO-1 conjugation sites occur within this motif, but SUMOylation also occurs on lysine residues located within non-consensus regions. SUMO-1 has been shown to form chains in vitro and in vivo but often the linkage is uncharacterized, and the function of SUMO chains has not yet been fully elucidated. SUMO-1 multimerization in vitro has been shown to occur predominantly via K7, K16 and K17. The proteins in this kit have these lysine residues mutated to arginine and can be used to investigate mono-SUMOylation requirements or to reduce poly-SUMO chain formation. Included is wild-type SUMO-1 to be used as a positive control in SUMO-1 conjugation assays which can be performed using the SUMO-1 Conjugation Kit (K-710).