SMAD1 (Phospho-Ser465) Antibody AP08024PU detects endogenous levels of Smad1 only when phosphorylated at Serine 465.
Purification
Immunoaffinity Chromatography: The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific phosphopeptide. The antibody against non-phosphopeptide was removed by chromatography using non-phosphopeptide corresponding to the phosphorylation site.
Immunogène
The antiserum was produced against synthesized phosphopeptide derived from Human Smad1 around the phosphorylation site of Serine 465 (I-S-S-V-SP).
SMAD proteins are signal transducers and transcriptional modulators that mediate multiple signaling pathways. SMAD1, as a transcriptional modulator, is activated by BMP (Bone Morphogenetic Protein) type 1 receptor kinase (it is a receptor-regulated SMAD or R-SMAD). BMPs are involved in a range of biological activities including cell growth, apoptosis, morphogenesis, development and immune responses. SMAD proteins have been implicated as downstream effectors of TGF beta/BMP signaling. In response to BMP ligands, SMAD1 can be phosphorylated (other sites besides the most prominent of S206, are S187, S195, and S214). S-206 is phosphorylated by ERK in response to mitogenic growth factors, or by recombinant ERK in vitro, this can be tested by treating cells with EGF or in cancer cells where Ras is activated. The phosphorylated form of this protein forms a complex with SMAD4, which is important for its function in the transcription regulation. This protein is also a target for SMADspecific E3 ubiquitin ligases, such as SMURF1 and SMURF2, and undergoes ubiquitination and proteasome-mediated degradation.Synonyms: BSP-1, BSP1, JV4-1, MAD homolog 1, MADH1, MADR1, Mad-related protein 1, Mothers against DPP homolog 1, Mothers against decapentaplegic homolog 1, SMAD 1, SMAD family member 1, SMAD-1, Transforming growth factor-beta-signaling protein 1