Troponin I Type 2 is a critical component of the troponin complex, which plays a pivotal role in the regulation of muscle contraction in skeletal and cardiac muscles. The recombinant form of this protein, tagged with a His (histidine) tag, is widely used in research and diagnostic applications due to its ease of purification and high specificity.
Troponin I is one of the three subunits of the troponin complex, the other two being Troponin T and Troponin C. Troponin I is the inhibitory subunit that binds to actin in thin myofilaments to hold the troponin-tropomyosin complex in place, thereby inhibiting muscle contraction. When calcium ions bind to Troponin C, a conformational change occurs, leading to the displacement of Troponin I and allowing muscle contraction to proceed.
The recombinant form of Troponin I Type 2 is produced using Escherichia coli (E. coli) expression systems. This method involves inserting the gene encoding Troponin I into E. coli, which then produces the protein. The His tag, typically consisting of six histidine residues, is added to the N-terminus of the protein. This tag facilitates the purification of the protein using immobilized metal ion affinity chromatography (IMAC), which exploits the affinity of histidine residues for metal ions like nickel or cobalt .
Recombinant Troponin I Type 2 with a His tag is used in various applications, including: