TGF-β signaling: The antibody successfully detects phosphorylation of SMAD2 at Ser250 in human 293T cells treated with PMA/TPA or Calyculin A , confirming its role in TGF-β-induced activation.
Cancer research: In MCF-7 breast cancer cells, the antibody identified phosphorylated SMAD2 in response to TGF-β stimulation, correlating with increased transcriptional activity .
Subcellular localization: The antibody has been used to visualize nuclear translocation of phosphorylated SMAD2 in cells treated with TGF-β, highlighting its role in transcriptional regulation .
Species compatibility: Predicted reactivity with zebrafish, bovine, and sheep based on sequence alignment , making it suitable for comparative studies across species.
Epitope specificity: The antibody targets the phosphorylated Ser250 residue, part of the MH2 domain critical for SMAD2/SMAD4 complex formation .
Phosphorylation at Ser250 is a hallmark of SMAD2 activation by TGF-β type I receptor kinases. This modification facilitates:
Complex formation: Phosphorylated SMAD2 binds SMAD4, enabling nuclear translocation .
Transcriptional regulation: The complex activates genes involved in cell cycle arrest, apoptosis, and extracellular matrix production .
Pathological implications: Dysregulation of Ser250 phosphorylation is linked to cancers (e.g., colorectal carcinoma) and fibrotic diseases .