Cell Signaling Technology

Product Pathways - Jak/Stat Pathway

Phospho-Stat3 (Ser727) (6E4) Mouse mAb #9136

Applications Reactivity MW (kDa) Source Isotype
W IP H M 86 Mouse IgG2b

Applications Key:  W=Western Blotting  IP=Immunoprecipitation
Reactivity Key:  H=Human  M=Mouse
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.

Specificity / Sensitivity

Phospho-Stat3 (Ser727) (6E4) Mouse mAb detects endogenous levels of Stat3 only when phosphorylated at serine 727. It does not significantly cross-react with the corresponding phosphorylated serines of other Stat proteins. The antibody does not cross-react with nonphosphorylated Stat3 or with Stat3 phosphorylated at other sites.

Source / Purification

Monoclonal antibody is produced by immunizing mice with a synthetic phospho-peptide (KLH-coupled) corresponding to residues surrounding Ser727 of mouse Stat3.

Western Blotting

Western Blotting

Western blot analysis of extracts from serum-starved HeLa cells, untreated or IL-6-treated (100 ng/ml), using Phospho-Stat3 (Ser727) (6E4) Mouse mAb.

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.

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