Storage instructionsShipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
Our Abpromise guarantee covers the use of ab5317 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|WB||1/1000. Predicted molecular weight: 12 kDa.|
FunctionUbiquitin-like protein which can be covalently attached to target lysines either as a monomer or as a lysine-linked polymer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Covalent attachment 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 or CBX4.
Tissue specificityExpressed predominantly in liver.
Sequence similaritiesBelongs to the ubiquitin family. SUMO subfamily.
Contains 1 ubiquitin-like domain.
modificationsPolymeric chains can be formed through Lys-11 cross-linking.
Cleavage of precursor form by SENP1, SENP2 or SENP5 is necessary for function.
- Information by UniProt
- Small ubiquitin like modifier 3 antibody
- Small ubiquitin related modifier 3 antibody
- Small ubiquitin-related modifier 3 antibody
Western blots of SUMO1 and SUMO3 antibody on arabidopsis extracts heat treated for the indicated times by moving them from 24 to 37 degrees C. The panel on the left was using ab5316, the panel on the right was using ab5317 - both antibodies were used at a dilution of 1/1000.Western blots of SUMO1 and SUMO3 antibody on arabidopsis extracts heat treated for the indicated times by moving them from 24 to 37 degrees C. The panel on the left was using ab5316, the panel on the right was using ab5317 - both antibodies were used at a dilution of 1/1000.
This product has been referenced in:
- Budhiraja R et al. Substrates related to chromatin and to RNA-dependent processes are modified by Arabidopsis SUMO isoforms that differ in a conserved residue with influence on desumoylation. Plant Physiol 149:1529-40 (2009). WB ; Arabidopsis thaliana . Read more (PubMed: 19151129) »
- Kurepa J et al. The small ubiquitin-like modifier (SUMO) protein modification system in Arabidopsis. Accumulation of SUMO1 and -2 conjugates is increased by stress. J Biol Chem 278:6862-72 (2003). Read more (PubMed: 12482876) »