Phospho-SMAD2 (Ser465, Ser467) Polyclonal Antibody, Invitrogen™

Description

SMAD2 (MADH2, MAD2) regulates multiple cellular processes, such as cell proliferation, apoptosis, and differentiation. SMAD2 interacts with the TGF-beta receptors through its interaction with the SMAD anchor for receptor activation into the nucleus is a central event in TGF beta signaling. Phosphorylation of threonine 8 in the calmodulin-binding region of the MH1 domain by extracellular signal regulated kinase 1 (ERK1) enhances SMAD2 transcriptional activity, which is negatively regulated by calmodulin. In response to the TGF-beta signal, SMAD2 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. SMAD2 can also be phosphorylated by activin type 1 receptor kinase, and mediates the signal from the activin. Alternatively spliced transcript variants encoding the SMAD2 protein have been observed.