Product Pathways - Protein Stability
Ubc13 Antibody #4919
PhosphoSitePlus® protein, site, and accession data: UBE2N
| Applications | Reactivity | Sensitivity | MW (kDa) | Source |
|---|---|---|---|---|
| W | H M R Mk | Endogenous | 16 | Rabbit |
Applications Key:
W=Western Blotting
Reactivity Key:
H=Human
M=Mouse
R=Rat
Mk=Monkey
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Protocols
- 4919:
- Western Blotting
Specificity / Sensitivity
Ubc13 Antibody detects endogenous levels of Ubc13 protein.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ile10 of human Ubc13 protein. Antibodies are purified by protein A and peptide affinity chromatography.
Background
Protein ubiquitination is an important posttranslational modification that regulates protein function and fate (1). Ubiquitin (Ub) can be conjugated to target proteins in either monomeric or polymeric forms. There are several different lysine residues within Ub that can be used as conjugation sites for poly-Ub chain formation. Different poly-Ub linkages mediate different functions of the target protein ranging from alterations in protein function to degradation (2). UBE2N/Ubc13 is a ubiquitin-E2-conjugating enzyme that catalyzes K63-linked poly-Ub chain formation (1,2). UBE2N forms a heterodimer with MMS2 or Uev1A to exert its E2 ligase function. The UBE2N/MMS2 and UBE2N/Uev1A heterodimers catalyze different modes of target protein ubiquitination to mediate various signaling pathways (3-5) including: DNA damage and recombination, p53 and check point control, the cell cycle (6-10), immunoreceptor signaling (11,12), and endocytosis (13). Most recently, UBE2N was shown to play an important role in inflammatory signaling by promoting K63-linked ubiquitination and activation of IKK downstream of the IL-1β receptor (14). Furthermore, interaction of UBE2N with the Triad1 E3 protein-ubiquitin ligase was shown to play an important role in myelopoiesis (15).
- Herrmann, J. et al. (2007) Circ Res 100, 1276-91.
- Wilkinson, K.D. et al. (2005) EMBO Rep 6, 815-20.
- Hofmann, R.M. and Pickart, C.M. (1999) Cell 96, 645-53.
- Deng, L. et al. (2000) Cell 103, 351-61.
- Andersen, P.L. et al. (2005) J Cell Biol 170, 745-55.
- Zhao, G.Y. et al. (2007) Mol Cell 25, 663-75.
- Kolas, N.K. et al. (2007) Science 318, 1637-40.
- Laine, A. et al. (2006) Mol Cell Biol 26, 8901-13.
- Huen, M.S. et al. (2008) Mol Cell Biol 28, 6104-12.
- Loring, G.L. et al. (2008) Cell Cycle 7, 96-105.
- Yamamoto, M. et al. (2006) Nat Immunol 7, 962-70.
- Yamamoto, M. et al. (2006) J Immunol 177, 7520-4.
- Duncan, L.M. et al. (2006) EMBO J 25, 1635-45.
- Xu, M. et al. (2009) Mol Cell 36, 302-14.
- Marteijn, J.A. et al. (2009) Leukemia 23, 1480-9.
Application References
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For Research Use Only. Not For Use In Diagnostic Procedures.