HyTest site uses cookies to improve user experience.

Troponin I Products

New Cardiac troponin I Booklet is available now. Download the Booklet.

At HyTest we have intensively studied troponin I for over 20 years and we are actively collaborating with researchers and clinicians in this field. For a list of publications, see "literature" tab. We constantly aim at developing improved antibodies to be used in immunoassays needed in accurate cardiac disease diagnostics.

Cardiac troponin I is currently considered as the gold standard biomarker test for myocardial infarction. Moreover, cTnI measurements by new generation of high-sensitivity cTnI assays could be helpful for long-term risk stratification of different patient groups including patients with heart failure or acute coronary syndrome.

HyTest troponin complex selected as reference material

In 2004, HyTest’s troponin I-T-C complex was selected by the American Association for Clinical Chemistry Standardization Subcommittee to be used by assay manufacturers as reference material in troponin I assays. The certified reference material (SRM 2921) is available only from the National Institute of Standards and Technology.

To see our Troponin products, click "products" tab.

 

 

HyTest R&D scientists have intensively studied troponin I for over 20 years and significantly contributed to development of reliable quantitative immunoassays for cTnI.

TechNotes

Cardiac troponin I Booklet

Articles

Noble JE, et al. (2010) Development of a candidate secondary reference procedure (immunoassay based measurement procedure of higher metrological order) for cardiac troponin I: I. Antibody characterization and preliminary validation. Clin Chem Lab Med 48(11): 1603-1610.

Tate JR, et al. (2010) Standardisation of cardiac troponin I measurement: past and present. Pathology 42(5): 402-408.

Panteghini M, et al. (2008) Standardization of troponin I measurements: an update. Clin Chem Lab Med 46(11): 1501-1506.

Ylikotila J, et al. (2006) Utilization of recombinant Fab fragments in a cTnI immunoassay conducted in spot wells. Clin Biochem 39 (8): 843-850.

Katrukha AG. (2003) Antibody selection strategies in cardiac troponin assays. Cardiac Markers, 2nd edition, Edited by Alan HB. Wu. 173-185.

Deng Y, et al. (2003) Phosphorylation of human cardiac troponin I G203S and K206Q linked to familial hypertrophic cardiomyopathy affects actomyosin interaction in different ways. J Mol Cell Cardiol 35(11): 1365-1374. 

Katrukha A, et al. (1999) Biochemical factors influencing measurement of cardiac troponin I in serum. Clin Chem Lab Med. 37(11-12): 1091-1095.

Katrukha A, et al. (1999) New approach to standardisation of human cardiac troponin I (cTnI). Scand J Clin Lab Invest Suppl. 230: 124-127.

Filatov VL, et al. (1999) Troponin: structure, properties, and mechanism of functioning. Biochemistry (Mosc) 64(9): 969-985.

Katrukha AG, et al. (1998) Degradation of cardiac troponin I: implication for reliable immunodetection. Clin Chem. 44(12): 2433-2440.

Filatov VL, et al. (1998) Epitope mapping of anti-troponin I monoclonal antibodies. Biochem Mol Biol Int. 45(6): 1179-1187.

Katrukha AG, et al. (1997) Troponin I is released in bloodstream of patients with acute myocardial infarction not in free form but as complex. Clin Chem. 43(8): 1379-1385.

Katrukha AG, et al. (1995) A new method of human cardiac troponin I and troponin T purification. Biochem Mol Biol Int 36(1): 195-202.

Katrukha AG, et al. (1993) Isolation of human cardiac troponin T and localization of epitopes recognized by monoclonal antibodies to cardiac troponin T. FEBS Lett. 315(1): 25-28.

 

Antibodies to selected epitopes

The epitope specificity of HyTest monoclonal anti-cTnI antibodies has been precisely determined using the SPOT technique or other methods utilizing different peptide libraries. We offer more than 30 specially selected antibodies specific to various epitopes along the cTnI molecule.

 

 Factors influencing cTnI immunodetection

Posttranslational modifications such as proteolytic degradation or complex formation as well as presence of autoantibodies or heparin in a clinical sample can have an effect on cTnI detection by antibodies. When designing a sensitive and precise immunoassay, it is important to take these factors into consideration.

 

Proteolytic degradation of cTnI may affect its detection

Purified cTnI is highly susceptible to proteolytic degradation. However, in a troponin complex the central part of the cTnI closely interacts with TnC which protects cTnI from endogenous proteases. Consequently, the epitopes located in the central part of the cTnI are significantly more stable than the epitopes located at the terminal parts of the molecule. Best two-site combinations of cTnI antibodies specific to the stable part of cTnI molecule tested with troponin complex before (green columns) and after (blue columns) incubation for 170 hours with a mixture of endogenous proteases from human cardiac tissue. Control assay M18-MF4 is sensitive to cTnI proteolytic degradation.