Phospho-Smad2(S250)抗体;Phospho-Smad2(S250) Antibody—艾普蒂 新品

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     Western blot analysis of Phospho-Smad2 (S250) expression in (1) HeLa cell treated with alkaline phosphatase lysate; (2) HeLa cell lysate.    

  
  

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     All lanes use the Antibody at 1:2K dilution for 1 hour at room temperature.    

  
  

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     All lanes use the Antibody at 1:2K dilution for 1 hour at room temperature.    

  
  

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     All lanes use the Antibody at 1:2K dilution for 1 hour at room temperature.    

  
  

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     All lanes use the Antibody at 1:1K dilution for 1 hour at room temperature.    

  
  

Phospho-Smad2 (S250) antibodies are essential tools for studying the TGF-β (transforming growth factor-beta) signaling pathway, which regulates diverse cellular processes, including proliferation, differentiation, and apoptosis. Smad2. a receptor-regulated Smad (R-Smad), is activated via phosphorylation by the TGF-β type I receptor kinase. While canonical Smad2 activation involves phosphorylation at C-terminal serine residues (S465/S467), phosphorylation at the serine 250 (S250) site represents a non-canonical modification associated with distinct regulatory mechanisms. This phosphorylation event has been implicated in fine-tuning Smad2 activity, potentially modulating its interaction with co-regulators, subcellular localization, or stability.

Phospho-Smad2 (S250)-specific antibodies enable researchers to detect this specific post-translational modification in techniques like Western blotting, immunofluorescence, or immunohistochemistry. Such antibodies are critical for investigating context-dependent TGF-β signaling dynamics, particularly in pathological conditions like fibrosis, cancer, or immune disorders, where aberrant Smad2 activation may drive disease progression. Studies suggest that S250 phosphorylation might occur independently of TGF-β receptor activation, possibly through alternative kinases (e.g., MAPK or CDK family members), highlighting its role in crosstalk with other signaling pathways.

Validation of these antibodies typically involves using cell models with induced phosphorylation (e.g., TGF-β stimulation) or genetic/pharmacologic inhibition to confirm specificity. Researchers must ensure minimal cross-reactivity with other Smad proteins (e.g., Smad3) or non-phosphorylated Smad2. Understanding S250 phosphorylation's functional impact remains an active area of research, making these antibodies valuable for unraveling Smad2's complexity in health and disease.