Phospho-Cardiac Troponin I (Ser22/Ser23)抗体;Phospho-Cardiac Troponin I (Ser22/Ser23) Antibody—艾普蒂 新品

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     EnzymeLinked Immunosorbent Assay (Phospho-ELISA) for Immunogen Phospho-peptide (Phospho-left) and NonPhospho-peptide (Phospho-right), using TNNI3 (Phospho-Ser22+Ser23) antibody.    

  
  

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     Western blot analysis of Phospho-Cardiac Troponin I (Ser22/Ser23) in SH-SY5Y lysates using Phospho-Cardiac Troponin I (Ser22/Ser23) antibody.    

  
  

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     Western blot analysis of Phospho-Cardiac Troponin I (Ser22/Ser23) in mouse heart lysates using Phospho-Cardiac Troponin I (Ser22/Ser23) antibody.The lane on the right is blocked with the Phospho- peptide.    

  
  

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     Immunohistochemistry analysis of paraffin-embedded Human skeletal muscle using TNNI3 (Phospho-Ser22+Ser23) antibody. High-pressure and temperature Sodium Citrate pH 6.0 was used for antigen retrieval.Sample with blocking peptide on the right.    

  
  

Phospho-Cardiac Troponin I (Ser22/Ser23) antibodies are specialized tools used to detect the phosphorylated form of cardiac troponin I (cTnI), a key regulatory protein in myocardial contraction. cTnI, a component of the troponin complex, inhibits actomyosin ATPase activity in cardiac muscle under low calcium conditions. Its function is modulated by phosphorylation at specific serine residues, including Ser22 and Ser23. which are primary targets of protein kinase A (PKA) during β-adrenergic stimulation. Phosphorylation at these sites reduces cTnI’s inhibitory effect, enhancing myocardial relaxation and contractility—a critical adaptive response to stress or increased metabolic demand.

These antibodies are widely employed in cardiovascular research to study signaling pathways involved in cardiac physiology and pathology. For example, phosphorylation at Ser22/Ser23 is altered in conditions like heart failure, ischemia-reperfusion injury, or hypertrophy, reflecting dysregulated adrenergic signaling or cellular stress. By selectively recognizing phosphorylated cTnI, these antibodies enable precise detection of post-translational modifications in tissue samples, cell cultures, or animal models using techniques like Western blotting, immunohistochemistry, or ELISA.

Clinically, understanding cTnI phosphorylation patterns may offer insights into disease mechanisms or therapeutic targets. However, current diagnostic applications primarily focus on total cTnI (unmodified) as a biomarker for myocardial injury. Research-grade phospho-specific antibodies remain vital for dissecting molecular pathways underlying cardiac dysfunction and potential interventions.