Anti-phospho-SMAD3 (Thr179)

This affinity-purified antibody is directed against the phosphorylated form of human Smad3 protein at the pT179 residue. The product was affinity purified from monospecific antiserum by immunoaffinity purification.  Antiserum was first purified against the phosphorylated form of the immunizing peptide.  The resultant affinity purified antibody was then cross adsorbed against the non-phosphorylated form of the immunizing peptide.  Reactivity occurs against human Smad3 pT179 protein and the antibody is specific for the phosphorylated form of the protein.   Reactivity with non-phosphorylated human Smad3 is minimal by ELISA and western blot.  Expect reactivity against phosphorylated Smad2.  Reactivity against other phosphorylated Smad family members is not known.  A BLAST analysis was used to suggest cross reactivity with Smad3 from human, mouse, rat, pig, dog, and marmoset based on 100% sequence homology with the immunogen.  Reactivity against homologues from other sources is not known. Protein function: Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD3/SMAD4 complex, activates transcription. Also can form a SMAD3/SMAD4/JUN/FOS complex at the AP-1/SMAD site to regulate TGF-beta-mediated transcription. Has an inhibitory effect on wound healing probably by modulating both growth and migration of primary keratinocytes and by altering the TGF- mediated chemotaxis of monocytes. This effect on wound healing appears to be hormone-sensitive. Regulator of chondrogenesis and osteogenesis and inhibits early healing of bone fractures. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator. [The UniProt Consortium]