Phospho-Stat6 (Tyr641) (D8S9Y) Rabbit mAb (Alexa Fluor® 647 Conjugate) #10205
- F
Supporting Data
| REACTIVITY | H M |
| SENSITIVITY | Endogenous |
| MW (kDa) | |
| Source/Isotype | Rabbit IgG |
Application Key:
- F-Flow Cytometry
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
Product Information
Product Description
Product Usage Information
| Application | Dilution |
|---|---|
| Flow Cytometry (Fixed/Permeabilized) | 1:50 |
Storage
Protocol
Specificity / Sensitivity
Phospho-Stat6 (Tyr641) (D8S9Y) Rabbit mAb (Alexa Fluor® 647 Conjugate) recognizes endogenous levels of Stat6 protein only when phosphorylated at Tyr641. Weak cross-reactivity with other tyrosine-phosphorylated proteins has been observed in some cell lines.
Species Reactivity:
Human, Mouse
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:
Rat
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic phospho-peptide corresponding to residues surrounding Tyr641 of human Stat6 protein.
Background
Upon activation by Janus kinases, Stat6 translocates to the nucleus where it regulates cytokine-induced gene expression. Stat6 is activated via phosphorylation at Tyr641 and is required for responsiveness to IL-4 and IL-13 (1-4). In addition, Stat6 is activated by IFN-α in B cells, where it forms transcriptionally active complexes with Stat2 and p48 (5,6). Protein phosphatase 2A is also involved in regulation of IL-4-mediated Stat6 signaling (7).
- Nelms, K. et al. (1999) Ann. Rev. Immunol. 17, 701-738.
- Malabarba, M.G. et al. (1996) Biochem. J. 319, 865-872.
- Hou, J. et al. (1994) Science 265, 1701-1706.
- Quelle, F.W. et al. (1995) Mol. Cell. Biol. 15, 3336-3343.
- Takeda, K. et al. (1996) Nature 380, 627-630.
- Gupta, S. et al. (1999) J. Immunol. 163, 3834-3841.
- Woetmann, A. et al. (2003) J. Biol. Chem. 278, 2787-2791.
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