Anti-Phospho-Cardiac Troponin I (Ser23/24) Rabbit mAb

Cardiac troponin is composed of three subunits, namely cardiac troponin T (cTnT), cardiac troponin I (cTnI), and cardiac troponin C (cTnC). They collectively participate in the regulation of cardiac muscle contraction. The amino-terminal and carboxyl-terminal ends of cTnI molecules are prone to degradation through protein hydrolysis. Cardiac troponin I (cTnI) is an important regulatory factor that inhibits muscle contraction under normal circumstances. It binds to actin, preventing the interaction between actin and cardiac troponin C (cTnC), thus inhibiting muscle contraction. The phosphorylation status of cTnI can alter its affinity for actin, thereby influencing the regulation of muscle contraction. The serine residues at positions 22 and 23 of cTnI are susceptible to phosphorylation by protein kinase A, which regulates muscle contraction. Abnormal levels of phosphorylation may also contribute to muscle dysfunction or the development of heart disease.