SUMO2 [untagged]

Catalogue Number
Product Size
500 µg
Price £
Accession Number
Residues Expressed
Certificate of Analysis Size
500 ug
E. coli expression
500 µg
1 mg/ml
50 mM HEPES pH 7.5, 150 mM sodium chloride, 2 mM dithiothreitol, 10% glycerol
Molecular Weight
~10.6 kDa
12 months at -70°C; aliquot as required
Protein Sequence
Accession number: NP_008868. For full protein sequence information download the Certificate of Analysis pdf.
QA; Protein Identification
Confirmed by mass spectrometry.
QA Activity

E2 Thioester SUMO-2 Loading Assay: The activity of SUMO-2 was validated by loading SUMO-2 onto the active cysteine of the UBE2I E2 enzyme via a transthiolation reaction. Incubation of SUMO-2, SAE1/SAE2 and UBE2I enzymes in the presence of ATP at 30°C was compared at two time points, T0 and T10 minutes. Sensitivity of the SUMO-2/UBE2I thioester bond to the reducing agent DTT was confirmed.


Small Ubiquitin-like Modifiers (SUMOs) are a family of small, related proteins that can be enzymatically conjugated to a target protein by a post-translational modification process termed SUMOylation. SUMO-2 is a highly conserved, small ubiquitin-related modifier that has been shown to be covalently conjugated to a large variety of cellular proteins (Dai and Liew, 2001; Kamitani et al., 1997; Su and Li, 2002). Identification and cloning of human SUMO-2 was first described by Kamitani et al. (1997). Mouse and human SUMO-2 proteins are identical, with human SUMO-2 sharing 44% and 86% amino acid identity with SUMO-1 and SUMO-3, respectively (Su and Li, 2002). SUMO-2 has been shown to interact with the E3 ligase RNF28 through its RING domain (Dai and Liew, 2001). SUMO-2 is conjugated to a target protein in a similar way to ubiquitin and has been implicated in multiple cellular processes, including nuclear transport, cell cycle control, oncogenesis, inflammation and response to viral infection. SUMO-2 forms a number of conjugates similar to those of SUMO-1, first requiring cleavage of its C terminus for conjugation to occur (Kamitani et al., 1997). RANGAP1 is modified by either SUMO-2 or SUMO-1, and formation of the sentrinized (SUMOylated) RANGAP1 requires covalent linkage between itself and SUMO-2 or SUMO-1 (Kamitani et al., 1997). SUMO-2 has been localised predominantly to nuclear bodies, distinct from SUMO-1 and SUMO-3 which are found localised to the nuclear membrane (Matunis et al., 1996).


Dai KS, Liew CC (2001) A novel human striated muscle RING zinc finger protein, SMRZ, interacts with SMT3b via its RING domain. J Biol Chem 276, 23992-9.

Kamitani T, Kito K, Nguyen HP, Yeh ET (1997) Characterization of NEDD8, a developmentally down-regulated ubiquitin-like protein. J Biol Chem 272, 28557-62.

Matunis MJ, Coutavas E, Blobel G (1996) A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex. J Cell Biol 135, 1457-70.

Su HL, Li SS (2002) Molecular features of human ubiquitin-like SUMO genes and their encoded proteins. Gene 296, 65-73.