Phospho-SMAD2 (Ser465/467)/SMAD3 (Ser423/425) (D27F4) Rabbit mAb #8828
- WB
Supporting Data
| REACTIVITY | H M R Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 52, 60 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Mk-Monkey
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Simple Western™ | 1:50 - 1:250 |
Storage
Protocol
Specificity / Sensitivity
Phospho-SMAD2 (Ser465/467)/SMAD3 (Ser423/425) (D27F4) Rabbit mAb recognizes endogenous levels of SMAD2 protein when phosphorylated at Ser465 and Ser467. This antibody also recognizes endogenous levels of SMAD3 protein when phosphorylated Ser422 only or at both Ser423 and Ser425.
Species Reactivity:
Human, Mouse, Rat, Monkey
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser465/467 of human SMAD2 protein.
Background
Members of the SMAD family of signal transduction molecules are components of a critical intracellular pathway that transmit TGF-β signals from the cell surface into the nucleus. Three distinct classes of SMADs have been defined: the receptor-regulated SMADs (R-SMADs), which include SMAD1, 2, 3, 5, and 9; the common-mediator SMAD (co-SMAD), SMAD4; and the antagonistic or inhibitory SMADs (I-SMADs), SMAD6 and 7 (1-5). Activated type I receptors associate with specific R-SMADs and phosphorylate them on a conserved carboxy-terminal SSXS motif. The phosphorylated R-SMADs dissociate from the receptor and form a heteromeric complex with SMAD4, initiating translocation of the heteromeric SMAD complex to the nucleus. Once in the nucleus, SMADs recruit a variety of DNA binding proteins that function to regulate transcriptional activity (6-8).
- Heldin, C.H. et al. (1997) Nature 390, 465-71.
- Attisano, L. and Wrana, J.L. (1998) Curr Opin Cell Biol 10, 188-94.
- Derynck, R. et al. (1998) Cell 95, 737-40.
- Massagué, J. (1998) Annu Rev Biochem 67, 753-91.
- Whitman, M. (1998) Genes Dev 12, 2445-62.
- Wrana, J.L. (2000) Sci STKE 2000, re1.
- Attisano, L. and Wrana, J.L. (2002) Science 296, 1646-7.
- Moustakas, A. et al. (2001) J Cell Sci 114, 4359-69.
Limited Uses
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