Cell Signaling Technology

Product Pathways - Protein Stability

UBA2 (D15C11) Rabbit mAb #8688

Applications Reactivity Sensitivity MW (kDa) Isotype
W IP H M R Mk (X) (Z) (B) (Dg) (Hr) Endogenous 90 Rabbit IgG

Applications Key:  W=Western Blotting  IP=Immunoprecipitation
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey  X=Xenopus  Z=Zebrafish  B=Bovine  Dg=Dog  Hr=Horse
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

UBA2 (D15C11) Rabbit mAb recognizes endogenous levels of total UBA2 protein.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gln421 of human UBA2 protein.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using UBA2 (D15C11) Rabbit mAb.

Western Blotting

Western Blotting

Western blot analysis of extracts from 293T cells, either mock transfected (-) or transfected with a Myc/DDK-tagged cDNA expression construct encoding full-length human UBA2 (hUBA2, +), using UBA2 (D15C11) Rabbit mAb.

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).

  1. Geiss-Friedlander, R. and Melchior, F. (2007) Nat Rev Mol Cell Biol 8, 947-56.
  2. Tatham, M.H. et al. (2003) Biochemistry 42, 9959-69.
  3. Desterro, J.M. et al. (1999) J Biol Chem 274, 10618-24.
  4. Gong, L. et al. (1999) FEBS Lett 448, 185-9.
  5. Desterro, J.M. et al. (1997) FEBS Lett 417, 297-300.
  6. Bossis, G. and Melchior, F. (2006) Mol Cell 21, 349-57.

Application References

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Companion Products

For Research Use Only. Not For Use In Diagnostic Procedures.

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