Cell Signaling Technology

Product Pathways - TGF-beta/Smad Signaling

Smurf2 (D8B8) Rabbit mAb #12024

Applications Reactivity Sensitivity MW (kDa) Isotype
W IP H M R Mk Endogenous 80 Rabbit IgG

Applications Key:  W=Western Blotting  IP=Immunoprecipitation
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

Specificity / Sensitivity

Smurf2 (D8B8) Rabbit mAb recognizes endogenous levels of total Smurf2 protein. This antibody also cross-reacts with proteins of unknown origin at 250 and 46 kDa in some cell lines.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro160 of human Smurf2 protein.

Western Blotting

Western Blotting

Western blot analysis of extracts from U-2 OS and ACHN cells using Smurf2 (D8B8) Rabbit mAb.

Background

Smad ubiquitin regulatory factor 2 (Smurf2) is a HECT domain E3 ubiquitin ligase. It was initially identified as an inhibitor of TGF-β/BMP signaling by targeting R-Smads and TGF type I receptor for ubiquitination and degradation (1-3). Subsequent studies have revealed its role in neuronal and planar cell polarity, as well as in the senescence response and suppression of tumorigenesis (4-8). Smurf2 has a broad range of substrates including RUNX2, AMSH, Rap1B, and RNF11 (5,9-11). Smurf2 is widely expressed in various tissues. The C2 domain of Smurf2 inhibits its catalytic activity by interacting with the HECT domain (12). Research studies have shown that Smurf2 functions as a tumor suppressor by maintaining genomic stability through targeting RNF20 (13).

  1. Zhang, Y. et al. (2001) Proc Natl Acad Sci U S A 98, 974-9.
  2. Kavsak, P. et al. (2000) Mol Cell 6, 1365-75.
  3. Izzi, L. and Attisano, L. (2004) Oncogene 23, 2071-8.
  4. Zhang, H. and Cohen, S.N. (2004) Genes Dev 18, 3028-40.
  5. Schwamborn, J.C. et al. (2007) EMBO J 26, 1410-22.
  6. Narimatsu, M. et al. (2009) Cell 137, 295-307.
  7. Nie, J. et al. (2010) J Biol Chem 285, 22818-30.
  8. Ramkumar, C. et al. (2012) Cancer Res 72, 2714-9.
  9. Subramaniam, V. et al. (2003) Br J Cancer 89, 1538-44.
  10. Li, H. and Seth, A. (2004) Oncogene 23, 1801-8.
  11. Kaneki, H. et al. (2006) J Biol Chem 281, 4326-33.
  12. Wiesner, S. et al. (2007) Cell 130, 651-62.
  13. Blank, M. et al. (2012) Nat Med 18, 227-34.

Application References

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

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