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Product Usage Information

For optimal ChIP results, use 10 μl of antibody and 10 μg of chromatin (approximately 4 x 106 cells) per IP. This antibody has been validated using SimpleChIP? Enzymatic Chromatin IP Kits.

Storage

Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 μg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

Specificity / Sensitivity

Phospho-Stat3 (Ser727) (D4X3C) Rabbit mAb is recognizes endogenous levels of Stat3 protein only when phosphorylated at Ser727.

Species Reactivity:

Human

Species predicted to react based on 100% sequence homology:

Mouse, Rat

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic phospho-peptide corresponding to residues surrounding Ser727 of human Stat3 protein.

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). 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.