|8828||Phospho-Smad2 (Ser465/467)/Smad3 (Ser423/425) (D27F4) Rabbit mAb||
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Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
Phospho-Smad2 (Ser465/467)/Smad3 (Ser423/425) (D6G10) XP® Rabbit mAb detects endogenous levels of phosporylated Smad2 and Smad3. Some reactivity is observed with non-phosphorylated Smad2 and 3 by western blot analysis. This antibody does not cross-react with other Smad-related proteins.
Mouse, Rat, Monkey, Xenopus, Bovine
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser465/467 of human Smad2. This region is highly conserved with Smad3 at Ser423/425.
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 (serines 465 and 467 on Smad2; serines 423 and 425 on Smad3) by the receptor kinase TGF-β R1(9-11). Following phosphorylation, Smad2 and Smad3 form a heteromeric complex with the co-smad family member Smad4. These complexes are translocated to the nucleus where they bind DNA and regulate gene transcription.
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