Phospho-SMAD2 (Ser465/Ser467) (E8F3R) Rabbit mAb #18338
- WB
- IP
- IF
- F
- ChIP
Supporting Data
| REACTIVITY | H M R |
| SENSITIVITY | Endogenous |
| MW (kDa) | 60 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- IF-Immunofluorescence
- F-Flow Cytometry
- ChIP-Chromatin Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
Product Information
Product Usage Information
For optimal ChIP results, use 10 μl of antibody and 10 μg of chromatin (approximately 4 × 106 cells) per IP. This antibody has been validated using SimpleChIP® Enzymatic Chromatin IP Kits.
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:100 |
| Immunofluorescence (Immunocytochemistry) | 1:400 - 1:1600 |
| Flow Cytometry (Fixed/Permeabilized) | 1:400 - 1:1600 |
| Chromatin IP | 1:50 |
Storage
For a carrier free (BSA and azide free) version of this product see product #94610.
Protocol
Specificity / Sensitivity
Phospho-Smad2 (Ser465/467) (E8F3R) Rabbit mAb recognizes endogenous levels of Smad2 protein when phosphorylated at Ser465 and Ser467.
Species Reactivity:
Human, Mouse, Rat
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.
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