Phospho-Smad1 (Ser463/Ser465)抗体;Phospho-Smad1 (Ser463/Ser465) Antibody—艾普蒂

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     Western blot analysis of Phospho-Smad1 (Ser463/Ser465) in A549, U2OS, C6 lysates using Phospho-Smad1 (Ser463/Ser465) antibody.    

  
  

Phospho-Smad1 (Ser463/Ser465) antibodies are essential tools for studying the activation of the bone morphogenetic protein (BMP) signaling pathway. Smad1. a receptor-regulated Smad (R-Smad), transduces BMP signals from cell surface receptors to the nucleus. Upon BMP ligand binding, type I BMP receptors phosphorylate Smad1 at two critical serine residues (Ser463 and Ser465) within its C-terminal SSXS motif. This phosphorylation triggers Smad1’s dissociation from the receptor, enabling its binding to Smad4 (a co-Smad) and subsequent nuclear translocation, where it regulates transcription of target genes involved in cell differentiation, proliferation, and apoptosis.

Phospho-Smad1 (Ser463/Ser465) antibodies specifically recognize the dual phosphorylation at these sites, serving as biomarkers for active BMP signaling. Researchers use these antibodies in techniques like Western blotting, immunofluorescence, and immunohistochemistry to assess Smad1 activation status in various contexts, including embryonic development, osteogenesis, and tissue homeostasis. Dysregulated BMP/Smad1 signaling is implicated in diseases such as fibrosis, cancer, and vascular disorders, making these antibodies valuable for mechanistic and therapeutic studies.

It is critical to validate antibody specificity using appropriate controls (e.g., phosphorylation-deficient mutants or phosphatase-treated samples) to avoid cross-reactivity with similar phospho-epitopes in other Smad proteins. Commercial antibodies often provide application-specific optimization data, ensuring reliability across experimental models.