Myostatin is synthesized as a large precursor molecule that undergoes proteolytic cleavage to generate an N-terminal propeptide and a disulfide-linked C-terminal dimer, which is the biologically active form of the protein . The circulating form of myostatin consists of a latent complex of the C-terminal dimer and other proteins, including its propeptide, which maintain the C-terminal dimer in an inactive state. Activation of myostatin requires additional cleavage of the prodomain by a tolloid-like metalloproteinase .
Myostatin acts as a negative regulator of skeletal muscle growth. It inhibits the differentiation of myoblasts into mature muscle fibers, thereby controlling muscle mass. Studies have shown that myostatin could also play an important role in cardiac development and physiology . The inhibition of myostatin activity has been explored as a potential therapeutic approach for muscle-wasting diseases and conditions characterized by muscle loss.
Recombinant human myostatin is produced using various expression systems, such as Escherichia coli. The recombinant protein typically includes a His tag, which is a sequence of histidine residues added to the protein to facilitate purification and detection . The His tag allows for easy purification of the protein using affinity chromatography techniques, which are based on the binding affinity between histidine residues and metal ions.
Recombinant myostatin is used in research to study its mechanisms of action, its role in muscle development, and its potential therapeutic applications. It is also used as a positive control in assays such as Western blots and ELISA .
The study of myostatin has significant implications for understanding muscle biology and developing treatments for muscle-related diseases. Researchers use recombinant myostatin to investigate its effects on muscle cells, identify potential inhibitors, and explore its role in various physiological processes. The availability of high-purity recombinant myostatin with a His tag has facilitated these studies by providing a reliable and consistent source of the protein for experimental use .