TNNT1 Human
Troponin T, slow skeletal muscle, TnTs, Slow skeletal muscle troponin T (sTnT), TNNT1, TNT.
Sterile Filtered White lyophilized (freeze-dried) powder.
Greater than 95.0% as determined by SDS-PAGE.
Description
TNNT1 Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 278 a.a and having a molecular mass of 32948 Dalton.
Product Specs
Troponin T, slow skeletal muscle, TnTs, Slow skeletal muscle troponin T (sTnT), TNNT1, TNT.
Product Science Overview
Troponin T (TnT) is a key component of the troponin complex, which plays a crucial role in muscle contraction. The troponin complex consists of three subunits: troponin T (TnT), troponin I (TnI), and troponin C (TnC). TnT binds to tropomyosin, anchoring the troponin complex to the thin filament of muscle fibers. This complex is essential for the regulation of muscle contraction in response to calcium ions (Ca²⁺).
There are three main isoforms of TnT, each specific to different types of muscle tissue:
- Cardiac Troponin T (cTnT): Found in cardiac muscle.
- Fast Skeletal Troponin T (fsTnT): Found in fast-twitch skeletal muscle fibers.
- Slow Skeletal Troponin T (ssTnT): Found in slow-twitch skeletal muscle fibers.
Slow Skeletal Troponin T (ssTnT) is specifically expressed in slow-twitch skeletal muscle fibers, which are responsible for sustained, endurance-type activities. These fibers are rich in mitochondria and rely on oxidative metabolism for energy production. ssTnT plays a critical role in the regulation of muscle contraction in these fibers.
Human recombinant slow skeletal troponin T (ssTnT) is a laboratory-produced version of the naturally occurring protein. Recombinant proteins are produced using recombinant DNA technology, which involves inserting the gene encoding the protein of interest into a host organism (such as bacteria, yeast, or mammalian cells) to produce the protein in large quantities.
The functional properties of ssTnT are essential for understanding its role in muscle physiology. ssTnT, along with TnI and TnC, forms the troponin complex in slow-twitch muscle fibers. This complex regulates the interaction between actin and myosin, the two main proteins involved in muscle contraction. When Ca²⁺ binds to TnC, it induces a conformational change in the troponin complex, allowing myosin to bind to actin and initiate contraction.
Research on ssTnT has provided valuable insights into muscle physiology and the mechanisms underlying muscle diseases. For example, studies have shown that ssTnT isoforms can regulate Ca²⁺ sensitivity and maximal force of contraction in muscle fibers . This knowledge has potential therapeutic applications, such as developing treatments for muscle disorders and improving muscle function in patients with heart failure.
