Anti-SMAD1 (Phospho-Ser463,465)/SMAD5 (Phospho-Ser463,465)/SMAD9

SMAD proteins are intracellular transcription factors and mediators of TGF-beta signaling. They are composed of an N-terminal MAD homology 1 (MH1) domain containing nuclear localization and DNA-binding sequences and a C-terminal MH2 domain that is essential for SMAD-receptor interactions, as well as SMAD-SMAD interactions. Binding of TGF-beta or bone morphogenetic protein (BMP) to their respective cell surface receptors initiates recruitment and activation of SMAD proteins. TGF-beta induces SMAD2 and SMAD3 activation, while BMP binding induces activation of SMAD1, SMAD5, and SMAD9 via phosphorylation of serine 463 and 465 (Ser463,465) in SMAD1 and SMAD5 and Ser465,467 in SMAD9. SMAD1, -5, and -9 activation is associated with hypertrophy in patients with osteoarthritis, but associated with inhibition of fibrotic gene expression in various fibrotic diseases, including chronic kidney disease (CKD). Cayman's SMAD1 (Phospho-Ser463,465)/SMAD5 (Phospho-Ser463,465)/SMAD9 (Phospho-Ser465,467) Rabbit Monoclonal Antibody (Clone RM487) can be used for Western blot (WB).. Cross reactivity: (+) SMAD1 (phospho-Ser463,465)/SMAD5 (phospho-Ser463,465)/SMAD9 (phospho-Ser465,467): (-) SMAD1/SMAD5/SMAD9 without phosphorylation. (+) Human: (+) Mouse, (+) Rat.. Protein function: Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD1 is a receptor- regulated SMAD (R-SMAD). SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1. May act synergistically with SMAD4 and YY1 in bone morphogenetic protein (BMP)- mediated cardiac-specific gene expression. [The UniProt Consortium]