Phospho-Smad2 (Ser465/467) AntibodyProduct information
Product Pathways - TGF-beta/Smad Signaling
Phospho-Smad2 (Ser465/467) Antibody #3101
|3101L||300 µl (30 western blots)||---||In Stock||---|
|3101S||100 µl (10 western blots)||---||In Stock||---|
|3101||carrier free and custom formulation / quantity||email request|
|W||1:1000||Human, Mouse, Rat||Endogenous||60||Rabbit|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting
Species predicted to react based on 100% sequence homology: Chicken, Xenopus, Zebrafish.
Specificity / Sensitivity
Phospho-Smad2 (Ser465/467) Antibody detects endogenous levels of Smad2 only when dually phosphorylated at Ser465 and Ser467, and may detect phosphorylated Smad3 at its equivalent site. This antibody does not cross-react with other Smad-related proteins.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser465/467 of human Smad2. Antibodies are purified by protein A and peptide affinity chromatography.
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-beta, Smad2 and Smad3 become phosphorylated at their carboxyl termini by the receptor kinase (serines 465 and 467 on Smad2; serines 423 and 425 on Smad3) by TbetaR-I (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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