Phospho-alpha 1 Sodium Potassium ATPase (Ser23)抗体;Phospho-alpha 1 Sodium Potassium ATPase (Ser23) Antibody—艾普蒂 新品

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     Western blot analysis of Phospho-alpha 1 Sodium Potassium ATPase (Ser23) in rat lysates using Phospho-alpha 1 Sodium Potassium ATPase (Ser23) antibody.    

  
  

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     Western blot analysis of Phospho-alpha 1 Sodium Potassium ATPase (Ser23) in rat brain lysates using ATP1 alpha1/Na+K+ ATPase1 (Phospho-Ser23) antibody. The lane on the right is blocked with the Phospho- peptide.    

  
  

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     Immunofluorescence analysis of Phospho-alpha 1 Sodium Potassium ATPase (Ser23) in NIH/3T3 using ATP1 alpha1/Na+K+ ATPase1 (Phospho-Ser23) antibody. The picture on the right is blocked using the Phospho- peptide.    

  
  

The Phospho-alpha 1 Sodium Potassium ATPase (Ser23) antibody is a specialized tool used to detect the phosphorylated form of the α1 subunit of the Na+/K+-ATPase at serine residue 23. Na+/K+-ATPase is a critical transmembrane enzyme responsible for maintaining electrochemical gradients by actively transporting sodium and potassium ions across cell membranes, essential for processes like neuronal excitability, muscle contraction, and nutrient transport. The α1 subunit is the catalytic core of the enzyme, and its activity is modulated by post-translational modifications, including phosphorylation. Phosphorylation at Ser23. located in the N-terminal cytoplasmic domain, has been implicated in regulating enzyme activity, cellular localization, or interactions with signaling partners, though its precise functional role remains under investigation.

This antibody is particularly valuable in studies exploring the regulation of Na+/K+-ATPase in physiological and pathological contexts, such as hypertension, heart failure, or neurological disorders. Researchers employ it in techniques like Western blotting, immunohistochemistry, or immunofluorescence to assess phosphorylation dynamics in response to stimuli like hormones (e.g., angiotensin II or insulin), oxidative stress, or kinase signaling pathways (e.g., PKC or PKA). Specificity for the phosphorylated Ser23 epitope ensures accurate detection of this regulatory modification. Its applications extend to understanding how dysregulated Na+/K+-ATPase phosphorylation contributes to diseases, offering insights for therapeutic targeting.