Anti-phospho-SMAD2 (Ser465/Ser467)

Anti-SMAD2 pS465 pS467 antibody is directed against the phosphorylated form of human Smad2 protein at the pS465 and pS467 residues. 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 SMAD2. Reactivity with non-phosphorylated human Smad2 is minimal by ELISA and western blot. A BLAST analysis was used to suggest cross-reactivity with Smad2 protein from human, mouse, rat, orangutan, and bovine based on 100% homology with the immunizing sequence.  Reactivity against homologues from other sources is not known. Smad2 (Mothers against decapentaplegic homolog 2) is a member of the Smad family of proteins which are similar to the gene products of the Drosophila gene 'mothers against decapentaplegic' (Mad) and the C. elegans gene Sma. SMAD proteins are signal transducers and transcriptional modulators that mediate multiple signaling pathways. This protein mediates the signal of the transforming growth factor (TGF)-beta, and thus regulates multiple cellular processes, such as cell proliferation, apoptosis, and differentiation. This protein is recruited to the TGF-beta receptors through its interaction with the SMAD anchor for receptor activation (SARA) protein. In response to TGF-beta signal, this protein is phosphorylated by the TGF-beta receptors. The phosphorylation induces the dissociation of this protein with SARA and the association with the family member SMAD4. The association with SMAD4 is important for the translocation of this protein into the nucleus, where it binds to target promoters and forms a transcription repressor complex with other cofactors. Anti-SMAD2 pS465 pS467 antibody is ideal for researchers interested in Cancer, Immunology and Nuclear Signaling research.