GDF-8 Peptide

Myostatin (also known as growth differentiation factor 8, abbreviated GDF-8) is a myokine, a protein produced and released by myocytes that acts on muscle cells’ autocrine function to inhibit myogenesis: muscle cell growth and differentiation. In humans it is encoded by the MSTN gene. Myostatin is a secreted growth differentiation factor that is a member of the TGF beta protein family.

Animals either lacking myostatin or treated with substances that block the activity of myostatin have significantly more muscle mass. Furthermore, individuals who have mutations in both copies of the myostatin gene have significantly more muscle mass and are stronger than normal. Blocking the activity of myostatin may have therapeutic application in treating muscle wasting diseases such as muscular dystrophy.

GDF-8 (propeptide-Fc) is a muscle growth inhibitory factor muscle growth and development process. Muscle inhibin is present in the healing process of muscle, and its nature is the inhibition of muscleogenesis (muscle tissue formation process). Scientists have been researching a new method of enhancing the repair and regeneration of muscle and bone in some lesions by introducing recombinant myostatin peptides through new recombinant muscle.Myostatin / GDF-8 is a protein that in humans is encoded by the MSTN gene. It isproduced primarily in skeletal muscle cells, circulates in the blood and acts on muscle tissue. The myostatin propeptide is known to bind and inhibit myostatin in vitro. This interaction is relevant in vivo, with a majority (>70%) of myostatin in serum bound to its propeptide acting as a negative regulator of myostatin. Recombinant human Myostatin Propeptide is a non-glycosylated protein, containing 244 amino acids, with a molecular weight of 27.8 kDa. Our Myostatin 1mg is Tagged. The tags are chains/pile of amino acids/proteins, it is foreign protein that will cause immunization reaction in most cases.

Myostatin / GDF-8 is a member of the TGF beta superfamily of proteins. Human myostatin consists of two identical subunits, each consisting of 109 amino acid residues. Its total molecular weight is 25.0 kDa. The protein is made in an inactive form. For it to be activated, a protease cleaves the NH2-terminal, or “pro-domain” portion of the molecule, resulting in the now-active COOH-terminal dimer Myostatin (GDF-8) is a member of the transforming growth factor-beta (TGF-beta) superfamily that is highly expressed in skeletal muscle, and myostatin loss-of-function leads to doubling of skeletal muscle mass. Myostatin-deficient mice have been used as a model for studying muscle-bone interactions, and here we review the skeletal phenotype associated with altered myostatin signaling. It is now known that myostatin is a key regulator of mesenchymal stem cell proliferation and differentiation, and mice lacking the myostatin gene show decreased body fat and a generalized increase in bone density and strength.

The increase in bone density is observed in most anatomical regions, including the limbs, spine, and jaw, and myostatin inhibitors have been observed to significantly increase bone formation. Myostatin is also expressed in the early phases of fracture healing, and myostatin deficiency leads to increased fracture callus size and strength. Together, these data suggest that myostatin has direct effects on the proliferation and differentiation of osteoprogenitor cells, and that myostatin antagonists and inhibitors are likely to enhance both muscle mass and bone strength.