Material Data Sheet

SUMO1 Mutant K7R/K17R

Price: $195.00
Catalog #: ULM-718

SUMO1 Mutant K7R/K17R

250 µg

Human SUMO-1 does not contain the exact ψΚXE consensus sequence found in SUMO-2 and SUMO-3. Within this motif 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 consensus sequence, 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 lysines K7, K16 and K17. Mutation of lysine 17 to arginine is useful to investigate monosumoylation requirements or can be used to reduce poly-SUMO chain formation.

Product Information

X mg/ml (XμM) in 50 mM HEPES pH 8.0, 150 mM NaCl, 1mM DTT. Actual concentration varies with lot number.
11.1 kDa
> 95% by SDS-PAGE

Use & Storage


Typical in vitro concentrations for conjugate formation is 10-50 μM depending on conditions. 

Store at -80°C once reconstituted. Avoid multiple freeze/thaw cycles.



Bencsath K. P., et al. (2002) J. Biol. Chem. 277: 47938–47945

Dohmen R.J., et al. (2004) Biochem. Biophys. Acta. 1695: 114-131

Johnson E. S. and Gupta A. A., (2001) Cell 106: 735–744

Johnson E.S. (2004) Annu. Rev. Biochem. 73: 355-382

Pedrioli G. A., et al. (2006) Nat. Meth.l 3:533-539

Pichler A., et al. (2002) Cell 108: 109-120

Rodriguez M.S., et al. (2001) J.Biol.Chem. 276: 12654-12659

Sampson D.A., et al. (2001) J.Biol.Chem. 276: 21664-21669

Takahashi Y., et all. (2003) J. Biochem. 133:415–422

Tatham M.H., et al. (2001) J.Biol.Chem. 276: 35368-35374.

Yang M., et al. (2006) J.Biol.Chem. 281: 8264-8274