New England Biolabs Canada

Product Pathways - Protein Stability

UBE2S (D5H9H) Rabbit mAb #11878

Item# Description List Price Web Price Qty
11878S UBE2S (D5H9H) Rabbit mAb - 100 µl $383.00
*On-line ordering is for Canadian customers only. Web pricing is applicable only to orders placed online at
Application Dilution Species-Reactivity Sensitivity MW (kDa) Isotype
W Human, Mouse, Rat, Monkey Endogenous 26 Rabbit IgG

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.

Specificity / Sensitivity

UBE2S (D5H9H) Rabbit mAb recognizes endogenous levels of total UBE2S protein.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human UBE2S protein.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using UBE2S (D5H9H) Rabbit mAb.

Western Blotting

Western Blotting

Western blot analysis of extracts from 293T cells, mock transfected (-) or transfected with a construct expressing Myc/DDK-tagged full-length human UBE2S (hUBE2S-Myc/DDK; +), using UBE2S (D5H9H) Rabbit mAb.

Western Blotting

Western Blotting

Western blot analysis of extracts from 293T cells, transfected with 100 nM SignalSilence® Control siRNA (Unconjugated) #6568 (-), or SignalSilence® UBE2S siRNA Ι #7220 (+), using UBE2S (D5H9H) Rabbit mAb (upper) or GAPDH (D16H11) XP® Rabbit mAb #5174 (lower). The UBE2S (D5H9H) Rabbit mAb confirms silencing of UBE2S expression, while the GAPDH (D16H11) XP® Rabbit mAb is used as a loading control.



Immunoprecipitation of UBE2S from 293T cell extracts, using Rabbit (DA1E) mAb IgG XP® Isotype Control #3900 (lane 2) or UBE2S (D5H9H) Rabbit mAb (lane 3). Lane 1 is 10% input. Western blot analysis was performed using UBE2S (D5H9H) Rabbit mAb.


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 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 an 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, researchers have found evidence that this enzyme is overexpressed in many types of human cancer (8), and has been implicated in hypoxia signaling (9,10). Indeed, UBE2S has been reported by researchers to associate with VHL and to target it for proteasomal degradation, thereby stabilizing HIF-1α (9).

  1. Hershko, A. (1988) J Biol Chem 263, 15237-40.
  2. Williamson, A. et al. (2009) Proc Natl Acad Sci U S A 106, 18213-8.
  3. Jin, L. et al. (2008) Cell 133, 653-65.
  4. Wu, T. et al. (2010) Proc Natl Acad Sci U S A 107, 1355-60.
  5. Song, L. and Rape, M. (2010) Mol Cell 38, 369-82.
  6. Summers, M.K. et al. (2008) Mol Cell 31, 544-56.
  7. Wickliffe, K.E. et al. (2011) Cell 144, 769-81.
  8. Tedesco, D. et al. (2007) Neoplasia 9, 601-13.
  9. Jung, C.R. et al. (2006) Nat Med 12, 809-16.
  10. Roos, F.C. et al. (2011) Am J Pathol 178, 853-60.

Application References

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