Anti-SUMO-2/3 (Human) mAb

WB - 2 ug/mL (chemiluminescence detection system) ICC - 5 ug/mL

Sumoylation, the covalent attachment of a small ubiquitin-like modifier (SUMO) peptide to lysine residues of targeted substrate, has recently emerged as an important mechanism in transcriptional control. The 15~17 kDa SUMO-1/UBL1/Sentrin is processed by SUMO hydrolase / isopeptidase to generate a free glycine residue that covalently attaches to protein substrates. Unlike ubiquitin, SUMO-1 does not appear to target proteins for degradation but seems to be involved in the modulation of protein-protein interactions. SUMO modification represses the activity of targeted transcriptional activators by altering their subcompartmentalization and binding properties. Sumoylation also recruits histone deacetylases, leading to SUMO-dependent transcriptional repression. Major SUMO-1 substrates include RanGAP1, PML, SP100, p53, Mdm2, c-Jun, topoisomerase I and II, and Iκ B.

1 mg/mL

100 ug IgG in 100 ul volume of PBS containing 50% glycerol, pH 7.2. No preservative is contained.

Human: 6613 Mouse: 170930

Full-length recombinant human SUMO-3

This antibody reacts with SUMO-2/3 (15 kDa) but not react with SUMO-1 (15~17 kDa) on Western blotting.

1 year

This antibody was purified from mouse ascites fluid using protein A agarose. This hybridoma was established by fusion of mouse myeloma cell P3U1 with Balb/c mouse lymphocyte immunized with the recombinant full-length human SUMO-2.

SUMO2/3