Troponin complex consists of three components, troponin I, T and C. The complex along with tropomyosin is located on the actin filament and is essential for the calcium-mediated regulation of skeletal and cardiac muscle contraction.
Three isoforms of troponin I have been described for striated muscle. Two isoforms are characteristic for fast and slow skeletal fibers and one isoform for cardiac muscle. Troponin I consists of 181-211 amino acid residues, and the cardiac isoform is larger due to the presence of an additional N-terminal peptide which has a biologically important function in the interactions of troponin I and troponin C. The main function of troponin I is the inhibition of actomyosin ATPase activity.
Cardiac troponin I and T are sensitive biomarkers of myocardial injury and have become central to the diagnosis of myocardial infarction. They are elevated in many clinical syndromes associated with direct myocardial injury, myocardial ischemia, or ventricular strain. They are also released in a number of clinical situations in which thrombotic complications of coronary artery disease. These situations include conditions like pulmonary embolism, sepsis, myocarditis, and acute stroke.
Western Blot: 1:2,000; Immunoprecipitation: 2 ?l;
Type: Primary
Antigen: TNN1 (troponin 1)
Clonality: Monoclonal
Clone: 3D10
Conjugation: Unconjugated
Epitope:
Host: Mouse
Isotype: IgG2b Kappa
Reactivity: Human
