Product Pathways - Protein Stability
UBE2S Antibody #9630
|9630S||100 µl (10 western blots)||---||In Stock||---|
|9630||carrier free and custom formulation / quantity||email request|
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|W||1:1000||Human, Mouse, Rat, Monkey||Endogenous||26||Rabbit|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IP=Immunoprecipitation
Species predicted to react based on 100% sequence homology: Bovine, Dog, Horse.
Specificity / Sensitivity
UBE2S Antibody recognizes endogenous levels of total UBE2S protein.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human UBE2S protein. Antibodies are purified by protein A and peptide affinity chromatography.
Protein ubiquitination requires the concerted action of the E1, E2, and E3 ubiquitin-conjugating enzymes. Ubiquitin is first activated through ATP-dependent formation of a thiol ester with ubiquitin-activating enzyme E1. The activated ubiquitin is then transferred to a thiol group of ubiquitin-carrier enzyme E2. The final step is the transfer of ubiquitin from E2 to an ε-amino group of the target protein lysine residue, which is mediated by ubiquitin-ligase enzyme E3 (1).
The human anaphase promoting complex (APC/C) is a large macromolecular E3 ligase complex that is largely responsible for the timely progression through mitosis via the sequential targeting of cell cycle regulators for proteasomal degradation. Recent work has revealed that APC/C substrates are marked for proteasomal degradation during cell cycle progression through the covalent assembly of Lys11-linked ubiquitin chains, which occurs through a priming phase and elongation phase (2-5). The APC/C utilizes, in part, the UBE2C/UBCH10 E2 enzyme to prime substrates for degradation through the covalent attachment of short Lys11-linked chains (3,6). The Lys11-specific elongating E2 enzyme, UBE2S/E2-EPF, extends these short chains into long Lys11-linked ubiquitin chains on APC/C bound substrates (2,3,7).
In addition to the well-established biochemical role for UBE2S in cell cycle regulation, this enzyme has been shown to be overexpressed in many types of human cancer (8) and has also been implicated in hypoxia signaling (9,10). Indeed, UBE2S has been reported to associate with VHL and to target it for proteasomal degradation, thereby stabilizing HIF-1α (9).
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- Williamson, A. et al. (2009) Proc Natl Acad Sci U S A 106, 18213-8.
- Jin, L. et al. (2008) Cell 133, 653-65.
- Wu, T. et al. (2010) Proc Natl Acad Sci U S A 107, 1355-60.
- Song, L. and Rape, M. (2010) Mol Cell 38, 369-82.
- Summers, M.K. et al. (2008) Mol Cell 31, 544-56.
- Wickliffe, K.E. et al. (2011) Cell 144, 769-81.
- Tedesco, D. et al. (2007) Neoplasia 9, 601-13.
- Jung, C.R. et al. (2006) Nat Med 12, 809-16.
- Roos, F.C. et al. (2011) Am J Pathol 178, 853-60.
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For Research Use Only. Not For Use In Diagnostic Procedures.
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