UBA2 (D15C11) Rabbit mAb #8688
- WB
- IP
Supporting Data
| REACTIVITY | H M R Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 90 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Mk-Monkey
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:100 |
Storage
Protocol
Specificity / Sensitivity
UBA2 (D15C11) Rabbit mAb recognizes endogenous levels of total UBA2 protein.
Species Reactivity:
Human, Mouse, Rat, Monkey
The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.
Species predicted to react based on 100% sequence homology:
Xenopus, Zebrafish, Bovine, Dog, Horse
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gln421 of human UBA2 protein.
Background
The process of SUMO conjugation to target proteins is similar to the molecular chain of events observed with ubiquitin (1). SUMO is conjugated to target proteins through the coordinated action of the cellular SUMO conjugation machinery consisting of E1, E2, and E3 enzymes (2). The canonical SUMO E1 activating enzyme is a heterodimer consisting of SAE1 (AOS1) and UBA2 (SAE2) subunits. Mature SUMO is activated by E1 in an ATP-dependent reaction that generates adenylated SUMO, which functions as a high-energy intermediate in the formation of a thioester linkage between SUMO and Cys173 of UBA2 (3,4). SUMO is subsequently transferred from UBA2 to the SUMO E2 conjugating enzyme, UBC9 (5). Recent evidence suggests that redox regulation of UBA2 serves as a physiologic mechanism to modulate the cellular level of sumoylated target proteins (6).
- Geiss-Friedlander, R. and Melchior, F. (2007) Nat Rev Mol Cell Biol 8, 947-56.
- Tatham, M.H. et al. (2003) Biochemistry 42, 9959-69.
- Desterro, J.M. et al. (1999) J Biol Chem 274, 10618-24.
- Gong, L. et al. (1999) FEBS Lett 448, 185-9.
- Desterro, J.M. et al. (1997) FEBS Lett 417, 297-300.
- Bossis, G. and Melchior, F. (2006) Mol Cell 21, 349-57.
Limited Uses
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