Cell Signaling Technology

Product Pathways - TGF-beta/Smad Signaling

SnoN Antibody #4973

Applications Reactivity Sensitivity MW (kDa) Source
W IF-IC H (Mk) Endogenous 80 Rabbit

Applications Key:  W=Western Blotting  IF-IC=Immunofluorescence (Immunocytochemistry)
Reactivity Key:  H=Human  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

SnoN Antibody detects endogenous levels of total SnoN protein.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser431 of human SnoN protein. Antibodies were purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from SW620, HT-1080 and MCF-7 cells using SnoN Antibody.

IF-IC

IF-IC

Immunofluorescent analysis of A-204 cells showing nuclear staining, using SnoN Antibody.

Background

Transforming growth factor-β (TGF-β) superfamily members are critical regulators of cell proliferation and differentiation, developmental patterning and morphogenesis and disease pathogenesis (1-3). Upon stimulation by TGF-β, activated receptors phosphorylate Smad2 and Smad3, resulting in their translocation to the nucleus, association with Smad4 and transcriptional regulation of target genes (4). Ski and SnoN are related oncoproteins originally discovered based on homology to v-Ski, the transforming protein of the Sloan-Kettering virus (5). They regulate TGF-β signaling by binding to Smad2 and Smad4 and repressing their ability to activate transcription (6). Following TGF-β stimulation, SnoN is rapidly degraded by the ubiquitin proteasome pathway providing negative feedback regulation (6-9). Overexpression of SnoN and Ski can transform avian fibroblasts and induce muscle differentiation (10). Mice heterozygous for SnoN and Ski display increased susceptibility to tumorigenesis (11,12). Interestingly, elevated expression of Ski and SnoN has been observed in many tumors and may serve as important prognostic markers (13,14). Taken together, these studies suggest possible dual functions of these proteins at different stages of tumorigenesis (15).

  1. Massagué, J. et al. (2000) Cell 103, 295-309.
  2. de Caestecker, M.P. et al. (2000) J. Natl. Cancer Inst. 92, 1388-1402.
  3. Derynck, R. et al. (2001) Nat. Genet. 29, 117-129.
  4. Miyazono, K. et al. (2000) Adv. Immunol. 75, 115-157.
  5. Nomura, N. et al. (1989) Nucleic Acids Res. 17, 5489-5500.
  6. Stroschein, S.L. et al. (1999) Science 286, 771-774.
  7. Bonni, S. et al. (2001) Nat. Cell Biol. 3, 587-595.
  8. Stroschein, S.L. et al. (2001) Genes Dev. 15, 2822-2836.
  9. Wan, Y. et al. (2001) Mol. Cell 8, 1027-1039.
  10. Boyer, P.L. et al. (1993) Oncogene 8, 457-466.
  11. Shinagawa, T. et al. (2001) Oncogene 20, 8100-8108.
  12. Shinagawa, T. et al. (2000) EMBO J. 19, 2280-2291.
  13. Zhang, F. et al. (2003) Cancer Res. 63, 5005-5010.
  14. Buess, M. et al. (2004) Neoplasia 6, 207-212.
  15. Zhu, Q. et al. (2007) Mol. Cell. Biol. 27, 324-339.

Application References

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Companion Products

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

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