Phospho-Smad2 (Ser250)抗体;Phospho-Smad2 (Ser250) Antibody—艾普蒂

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     Western blot analysis of Phospho-Smad2 (S250) in (1) HeLa treated with alkaline phosphatase lysates; (2) HeLa lysates using Phospho-Smad2 (Ser250) antibody.    

  
  

The Phospho-Smad2 (Ser250) antibody is a specialized tool used to study the activation and regulation of Smad2. a key intracellular mediator of transforming growth factor-beta (TGF-β) signaling. Smad2 becomes phosphorylated in response to TGF-β receptor activation, triggering its association with Smad4 and translocation to the nucleus to regulate gene expression. While canonical TGF-β signaling typically involves phosphorylation at C-terminal serine residues (Ser465/Ser467), phosphorylation at Ser250 represents a non-canonical modification. This site-specific phosphorylation event is thought to modulate Smad2’s interaction with regulatory proteins or influence its subcellular localization, potentially fine-tuning TGF-β signaling outcomes in processes like cell proliferation, differentiation, and apoptosis.

The Phospho-Smad2 (Ser250) antibody enables detection of this specific phosphorylation state, aiding research into TGF-β pathway dynamics under physiological or pathological conditions, such as cancer, fibrosis, or immune regulation. Its applications include Western blotting, immunofluorescence, and immunohistochemistry, provided proper validation (e.g., knockout controls, peptide competition assays) confirms specificity. Researchers should consider cross-reactivity with related Smad family members and verify species compatibility (e.g., human, mouse, rat). Understanding Ser250 phosphorylation expands insights into Smad2’s diverse roles beyond canonical signaling, offering potential therapeutic targets for diseases driven by TGF-β dysregulation.