Troponins are protein components of striated muscle. There are three different troponins: troponin C, troponin T and troponin I. Troponin T (cTnT) and troponin I (cTnI) are released only following cardiac damage They are present for, and remain elevated, a long time Unlike CK and CK-MB, cTnT and cTnI are released for much longer with cTnI detectable in the blood for up to 5 days and cTnT for 7-10 days following MI. This allows an MI to be detected if the patient presents late. Troponin T and I are very sensitive. There is always a low level release of CK and CK-MB from skeletal muscle at a low level all the time so there is always a background value. This is not the case for the cardiac structural proteins such as cTnT and cTnI and therefore, they are very sensitive. Studies have revealed that about one third of patients admitted with unstable angina, in which MI was apparently excluded by CK and CK-MB measurement, have raised levels of cTnT and cTnI. Elevation of cTnT or cTnI is absolutely indicative of cardiac damage, but this can occur as a result of causes other than MI e.g. myocarditis, coronary artery spasm from cocaine, severe cardiac failure, cardiac trauma from surgery or road traffic accident, and pulmonary embolus can cause cardiac damage with an accompanying elevation of cardiac troponin(s). Failure to show a rise in cTnT or cTnI does not exclude the diagnosis of ischemic heart disease. ||Both cTnT and cTnI may be elevated in patients with chronic renal failure and indicate a higher long-term risk of death. They can be distinguished from changes due to myocardial infarction by repeating the tests. Myocardial infarction causes a rise and fall in cTnT or cTnI, but in renal failure the elevated levels are sustained.||cTnI is a part of the troponin complex. It binds to actin in thin myofilaments to hold the actin-tropomyosin complex in place. Because of it myosin cannot bind actin in relaxed muscle. When calcium binds to the Troponin C it causes conformational changes which lead to dislocation of troponin I and finally tropomyosin leaves the binding site for myosin on actin leading to contraction of muscle. The letter I is given due to its inhibitory character.||Source:|Troponin-I, from mouse cardiac tissues||Molecular Weight:|~24kD||Applications: |Suitable for use in ELISA. Other applications not tested.||Recommended Dilution:|Optimal dilutions to be determined by the researcher.||Storage and Stability:|May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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