SMAD3 Antibody #9513
Filter:
- WB
- IP
- IF
Supporting Data
| REACTIVITY | H M R |
| SENSITIVITY | Endogenous |
| MW (kDa) | 52 |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- IF-Immunofluorescence
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:25 |
| Immunofluorescence (Immunocytochemistry) | 1:50 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
SMAD3 Antibody detects endogenous levels of total SMAD3 protein.
Species Reactivity:
Human, Mouse, Rat
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to a central region unique to human SMAD3. Antibodies were purified by protein A and peptide affinity chromatography.
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).
Following stimulation by TGF-β, Smad2 and Smad3 become phosphorylated at their carboxyl termini (Ser465 and 467 on Smad2; Ser423 and 425 on Smad3) by TGF-β Receptor I. Phosphorylated Smad 2/3 can complex with Smad4, translocate to the nucleus and regulate gene expression (9-11).
Following stimulation by TGF-β, Smad2 and Smad3 become phosphorylated at their carboxyl termini (Ser465 and 467 on Smad2; Ser423 and 425 on Smad3) by TGF-β Receptor I. Phosphorylated Smad 2/3 can complex with Smad4, translocate to the nucleus and regulate gene expression (9-11).
- 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.
- Abdollah, S. et al. (1997) J. Biol. Chem. 272, 27678-27685.
- Souchelnytskyi, S. et al. (1997) J. Biol. Chem. 272, 28107-28115.
- Liu, X. et al. (1997) Proc. Natl. Acad. Sci. U S A 94, 10669-10674.
限制使用
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For Research Use Only. Not For Use In Diagnostic Procedures.
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