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Product Description

Nonphosphorylated Stat3 Cell Extracts: Total cell extracts from serum-starved HeLa cells prepared without treatment, serve as a negative control. Supplied in SDS Sample Buffer. Store at -20ºC.

Phosphorylated Stat3 Cell Extracts: Total cell extracts from serum-starved HeLa cells prepared with 100 ng/ml interferon-alpha 5 minute IFN-alpha treatment, serve as a positive control. Supplied in SDS Sample Buffer. Store at -20ºC.


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). Research studies have shown that 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. (2001) J Recept Signal Transduct Res 19, 75-120.

2.  Takeda, K. et al. (1997) Proc Natl Acad Sci U S A 94, 3801-4.

3.  Catlett-Falcone, R. et al. (1999) Immunity 10, 105-15.

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, J.E. et al. (1994) Science 264, 1415-21.

7.  Ihle, J.N. (1995) Nature 377, 591-4.

8.  Wen, Z. et al. (1995) Cell 82, 241-50.

9.  Yokogami, K. et al. (2000) Curr Biol 10, 47-50.

10.  Biethahn, S. et al. (1999) Exp Hematol 27, 885-94.



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