Phospho-Stat3 (Tyr705) (D3A7) XP® Rabbit mAb (mFluor™ Red 780 Conjugate) #25023
- F
Supporting Data
| REACTIVITY | H M R Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | |
| Source/Isotype | Rabbit IgG |
Application Key:
- F-Flow Cytometry
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Mk-Monkey
Product Information
Product Description
Product Usage Information
| Application | Dilution |
|---|---|
| Flow Cytometry (Fixed/Permeabilized) | 1:50 |
Storage
Protocol
Specificity / Sensitivity
Phospho-Stat3 (Tyr705) (D3A7) XP® Rabbit mAb (mFluor™ Red 780 Conjugate) detects endogenous levels of Stat3 only when phosphorylated at Tyr705. This antibody does not cross-react with phospho-EGFR or the corresponding phospho-tyrosines of other Stat proteins.
Species Reactivity:
Human, Mouse, Rat, Monkey
The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.
Species predicted to react based on 100% sequence homology:
Hamster, Bovine, Pig, Horse
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr705 of mouse Stat3.
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).
- Heim, M.H. (2001) J Recept Signal Transduct Res 19, 75-120.
- Takeda, K. et al. (1997) Proc Natl Acad Sci U S A 94, 3801-4.
- Catlett-Falcone, R. et al. (1999) Immunity 10, 105-15.
- Garcia, R. and Jove, R. (1998) J Biomed Sci 5, 79-85.
- Bromberg, J.F. et al. (1999) Cell 98, 295-303.
- Darnell, J.E. et al. (1994) Science 264, 1415-21.
- Ihle, J.N. (1995) Nature 377, 591-4.
- Wen, Z. et al. (1995) Cell 82, 241-50.
- Yokogami, K. et al. (2000) Curr Biol 10, 47-50.
- Biethahn, S. et al. (1999) Exp Hematol 27, 885-94.
Limited Uses
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