Troponin-C Human
Description
Cardiac Troponin-C Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 181 amino acids (1-161) and having a molecular mass of 20.5 kDa.
Cardiac Troponin-C is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
Cardiac Troponin-C (cTnC) is a crucial protein involved in the regulation of cardiac muscle contraction. It is one of the three subunits of the troponin complex, which also includes troponin I (cTnI) and troponin T (cTnT). The primary function of cTnC is to bind calcium ions (Ca²⁺), which triggers a series of conformational changes in the troponin complex, ultimately leading to muscle contraction. Recombinant human cardiac troponin-C is a laboratory-produced version of this protein, used extensively in research and clinical diagnostics.
Cardiac Troponin-C is a small, globular protein composed of 161 amino acids. It contains four EF-hand motifs, which are helix-loop-helix structures capable of binding calcium ions. Two of these EF-hand motifs (sites III and IV) are high-affinity calcium-binding sites, while the other two (sites I and II) are low-affinity sites. The binding of calcium to these sites induces a conformational change in cTnC, which is essential for the regulation of muscle contraction.
The troponin complex is located on the thin filament of the sarcomere, the basic unit of muscle contraction. In the absence of calcium, the troponin complex inhibits the interaction between actin and myosin, the two main proteins involved in muscle contraction. When calcium binds to cTnC, it causes a conformational change that moves the troponin complex away from the actin-myosin binding site, allowing these proteins to interact and initiate contraction.
Recombinant human cardiac troponin-C is produced using genetic engineering techniques. The gene encoding cTnC is inserted into an expression vector, which is then introduced into a host cell, typically Escherichia coli (E. coli). The host cells are cultured under conditions that promote the expression of the recombinant protein. After expression, the protein is purified using various chromatographic techniques to obtain a highly pure and functional product.
Recombinant human cardiac troponin-C is widely used in research to study the molecular mechanisms of muscle contraction and the regulation of the troponin complex. It is also used in the development of diagnostic assays for cardiac diseases. Elevated levels of cardiac troponins, including cTnC, in the blood are indicative of myocardial infarction (heart attack) and other forms of cardiac injury. Therefore, accurate measurement of these proteins is critical for the diagnosis and management of cardiac conditions.
