Phospho-Src (Tyr530)抗体;Phospho-Src (Tyr530) Antibody—艾普蒂

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     Western blot analysis of Phospho-Src (Tyr529) in rat lung lysates using Phospho-Src (Tyr530) antibody.    

  
  

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     Western blot analysis of Src (Phospho-Tyr529) in CHO-K1 lysates using Src (Phospho-Tyr529) antibody.    

  
  

Phospho-Src (Tyr530) antibodies are essential tools for studying the regulation and activity of Src kinase, a non-receptor tyrosine kinase involved in critical cellular processes such as proliferation, survival, adhesion, and migration. Src contains an N-terminal unique domain, SH3 and SH2 domains, and a catalytic kinase domain. Its activity is tightly controlled by phosphorylation at two key tyrosine residues: Tyr419 (in human Src; Tyr416 in many species) and Tyr530. Phosphorylation at Tyr530 (C-terminal inhibitory site) by C-terminal Src kinase (CSK) promotes intramolecular interaction between the phosphorylated Tyr530 and the SH2 domain, stabilizing a closed, inactive conformation. Conversely, dephosphorylation of Tyr530 disrupts this interaction, leading to Src activation and autophosphorylation at Tyr419.

Phospho-Src (Tyr530) antibodies specifically recognize Src family kinases (e.g., Src, Yes, Fyn) when phosphorylated at this inhibitory site, enabling researchers to assess the inactive state of Src in cells or tissues. These antibodies are widely used in techniques like Western blotting, immunohistochemistry (IHC), and immunofluorescence (IF) to study Src regulation in contexts such as cancer, immune signaling, and neuronal development. Dysregulated Src activity due to altered Tyr530 phosphorylation is associated with tumor progression and metastasis, making this antibody valuable for both mechanistic studies and therapeutic target validation. Specificity is typically confirmed using phosphorylation-deficient mutants or CSK-modulated samples.