Cell Signaling Technology

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SignalSlide™ Phospho-Stat1/3/5 IHC Controls #8105

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Description

Each control slide contains formalin fixed, paraffin-embedded 786-0 cells, both untreated and treated with interferon alpha (IFN-α), that serve as a control for Phospho-Stat1 (Tyr701), Phospho-Stat3 (Tyr705) and Phospho-Stat5 (Tyr694) immunostaining. Western blot analysis was performed on extracts derived from the same cells to verify the efficacy of the IFN-alpha treatment. SignalSlide™ Phospho-Stat1/3/5 IHC Control slides have not been tested as controls for Phospho-Stat1 (Ser727) or Phospho-Stat3 (Ser727) immunostaining.

Western Blotting

Western Blotting

Western blot analysis of extracts from 786-0 cells, untreated or IFN-α treated, using Phospho-Stat3 (Tyr705) (D3A7) Rabbit mAb #9145 (top) or Stat3 (79D7) Rabbit mAb #4904 (bottom). This assay serves as a control for the efficacy of the IFN-α treatment.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded 786-0 cells, untreated (left) or IFN-α treated (right), using Phospho-Stat3 (Tyr705) (D3A7) Rabbit mAb #9145.

Applications

These slides are intended for use in immunohistochemical assays. Please see our Companion Products list for products that can be used with these slides.

Companion Products

Background

The Stat3 transcription factor is an important signaling molecule for many cytokines and growth-factor receptors (1) and is required for murine fetal development (2). Stat3 is constitutively activated in a number of human tumors (3,4) and possesses oncogenic potential (5) and anti-apoptotic activities (3). Stat3 is activated by phosphorylation at Tyr705, which induces dimerization, nuclear translocation and DNA binding (6,7). Transcriptional activation seems to be regulated by phosphorylation at Ser727 through the MAPK or mTOR pathways (8,9). Stat3 isoform expression appears to reflect biological function as the relative expression levels of Stat3α (86 kDa) and Stat3β (79 kDa) depend on cell type, ligand exposure or cell maturation stage (10). It is notable that Stat3β lacks the serine phosphorylation site within the carboxy-terminal transcriptional activation domain (8).

  1. Heim, M.H. (1999) J. Recept. Signal Transduct. Res. 19, 75-120.
  2. Takeda, K. et al. (1997) Proc. Natl. Acad. Sci. USA 94, 3801-3804.
  3. Catlett-Falcone, R. et al. (1999) Immunity 10, 105-115.
  4. Garcia, R. and Jove, R. (1998) J. Biomed. Sci. 5, 79-85.
  5. Bromberg, J.F. et al. (1999) Cell 98, 295-303.
  6. Darnell Jr., J.E. et al. (1994) Science 264, 1415-1421.
  7. Ihle, J.N. (1995) Nature 377, 591-594.
  8. Wen, Z. et al. (1995) Cell 82, 241-250.
  9. Yokogami, K. et al. (2000) Curr. Biol. 10, 47-50.
  10. Biethahn, S. et al. (1999) Exp. Hematol. 27, 885-894.

Application References

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