Smad proteins, the mammalian homologs of the Drosophila Mothers against dpp (Mad), function downstream of TGF-β receptor Serine/Threonine kinases and undergo serine phosphorylation in response to receptor activation. Following BMP (bone morphogenic protein) or TGF-β binding to the targeted surface receptors, Smad1 (also designated Madr1 or JV4-1) becomes phosphorylated at Ser 463 and Ser 465. Activated Smad1 associates with Smad4 and translocates to the nucleus, where the Smad1/Smad4 complex recruits DNA-binding proteins to activate specific gene transcription. BMP binding induces phosphorylation of Smad1, which enhances the binding of Smad1 to CBP to stimulate Smad1-dependent transcription. In addition, ALK1 and ALK2 specifically phosphorylate Smad1 on residues located in the MH2 domain and induces Smad1-dependent pathways.
Specificity
Recognizes the dual serine phosphorylated Smad1 (Ser463/465).
Immunogen
peptide corresponding to (CGGSPHNPISpSVpSGG) corresponding to amino acids 455-465 of human Smad1 protein
Application
Detect phospho-Smad1 (Ser463/465) with Anti-phospho-Smad1 (Ser463/465) Antibody (Rabbit Polyclonal Antibody), that has been shown to work in WB.
Quality
routinely evaluated by immunoblot on RIPA lysates from P19 (mouse embryonal carcinoma) cells treated with BMP4
Target description
65 kDa
Physical form
Format: Purified
Analysis Note
Control BMP-4-treated HeLa or NIH/3T3 cells
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Legal Information
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
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Reproductive Sciences null
BMP signaling dynamics in embryonic orofacial tissue.
Partha Mukhopadhyay,Cynthia L Webb,Dennis R Warner,Robert M Greene,M Michele Pisano
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