Myostatin Propeptide Human, HEK

Myostatin, also known as Growth Differentiation Factor 8 (GDF-8), is a member of the Transforming Growth Factor-beta (TGF-β) superfamily. It is a potent and specific negative regulator of skeletal muscle mass. Myostatin Propeptide is a naturally occurring inhibitor of myostatin, which binds to and neutralizes its activity. The recombinant form of Myostatin Propeptide, produced in Human Embryonic Kidney (HEK) cells, is used extensively in research to study muscle growth and related disorders.

Recombinant human Myostatin Propeptide produced in HEK cells is a single, glycosylated polypeptide chain consisting of 253 amino acids, with a calculated molecular mass of approximately 29.1 kDa . The recombinant protein is often fused to a C-terminal His tag to facilitate purification and detection.

The primary function of Myostatin Propeptide is to inhibit the activity of myostatin. In vitro studies have shown that Myostatin Propeptide can bind to myostatin and prevent it from interacting with its receptor, thereby neutralizing its inhibitory effect on muscle growth . This interaction is also relevant in vivo, where a majority of myostatin in serum is bound to its propeptide, acting as a natural regulator of myostatin activity .

Recombinant human Myostatin Propeptide is widely used in research to explore the mechanisms of muscle growth and to develop potential therapies for muscle-wasting diseases. By inhibiting myostatin, researchers aim to promote muscle growth and improve muscle function in conditions such as muscular dystrophy, cachexia, and sarcopenia.

The lyophilized form of recombinant human Myostatin Propeptide is stable at -20°C for long-term storage. Upon reconstitution, it is recommended to aliquot and store the protein at -20°C to maintain its stability and biological activity .