Phospho-Smad2 (Ser255)抗体;Phospho-Smad2 (Ser255) Antibody—艾普蒂 新品

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     Western blot analysis of Phospho-Smad2 (S255) in Hela treated with Okadaic acid and Calyculin A lysates using Phospho-Smad2 (Ser255) antibody.    

  
  

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     Immunohistochemistry analysis of paraffin-embedded Human transitional carcinoma of bladder using Phospho-Smad2 (S255) antibody.High-pressure and temperature Sodium Citrate pH 6.0 was used for antigen retrieval.    

  
  

The Phospho-Smad2 (Ser255) antibody detects Smad2 when phosphorylated at serine 255. a key post-translational modification in regulating TGF-β signaling. Smad2. a receptor-regulated Smad (R-Smad), is activated upon TGF-β ligand binding to cell surface receptors, which triggers phosphorylation of its C-terminal serine residues (e.g., Ser465/467) to facilitate complex formation with Smad4 and nuclear translocation. However, phosphorylation at Ser255. located in the linker region, is mediated by kinases such as CDK8/9 or MAPK and is associated with distinct regulatory mechanisms. This modification may influence Smad2 stability, subcellular localization, or interaction with transcriptional co-regulators, though its precise role remains under investigation.

The Phospho-Smad2 (Ser255) antibody is widely used in research to study TGF-β pathway dynamics, particularly in contexts like fibrosis, cancer, and immune regulation, where Smad2 activity is dysregulated. It enables detection of phosphorylation events in cell lysates (via Western blot) or tissue sections (via immunohistochemistry), helping to map signaling activity in disease models or developmental processes. Specificity validation (e.g., using phosphorylation-blocking peptides or kinase inhibitors) is critical, as cross-reactivity with other phosphorylated Smad family members may occur. Researchers often pair it with total Smad2 antibodies to assess activation ratios. Optimal results depend on proper sample preparation to preserve phosphorylation states, emphasizing the need for fresh lysates and phosphatase inhibitors during processing.