| Source / Purification | Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to a central region unique to Smad3. Antibodies were purified by protein A and peptide affinity chromatography. Western Blotting![Western Blotting]() Western blot analysis of extracts from HT1080, HeLa and B35 cell lines, using Smad3 Antibody. Western Blotting![Western Blotting]() Western blot analysis of extracts from HeLa cells transfected with Smad3, using Smad3 Antibody. IF-IC![IF-IC]() Immunofluorescent analysis of ACHN cells treated with or without of TGF-β, using total Smad3 Antibody and Phospho-Smad3 (Ser423/425)/Smad1 (463/465) Antibody #9514. |
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| 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 8; 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-Smad dissociates from the receptor and forms a heteromeric complex with the co-Smad (Smad4), allowing translocation of the complex to the nucleus. Once in the nucleus, Smads can target a variety of DNA binding proteins to regulate transcriptional responses (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). - Heldin, C.H. et al. (1997) Nature 390, 465-471.
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