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Cardiac troponin I, often denoted as cTnI, is presented in cardiac muscle tissue by a single isoform with a molecular weight of 23.9 kDa. Cardiac troponin I protein consists of 209 amino acid residues. The theoretical pI of cTnI is 9.05. cTnI is more sensitive and specific in diagnosing myocardial infarction.

Phosphorylation of ctni antibody changes the conformation of the protein and modifies its interaction with other troponins and the interaction with anti-TnI antibodies. These changes alter the myofilament response to calcium and are of interest in targeting heart failure. Multiple reaction monitoring of human cTnI has revealed 14 phosphorylation sites, and the pattern of phosphorylation observed in these sites changed in response to disease.

Measuring cardiac biomarkers can be a step toward making a diagnosis for a condition. Whereas cardiac imaging often confirms a diagnosis, more straightforward and less expensive cardiac markers test can advise a physician whether more complicated or invasive procedures are warranted. In many cases, medical societies recommend doctors to make biomarker measurements an initial testing strategy, especially for patients at low risk of cardiac death.