White Powder Research Peptide Human Myostatin Propeptide Gdf-8 1mg/Vial

White Powder Research Peptide Human Myostatin Propeptide Gdf-8 1mg/Vial

Myostatin/ GDF-8 Description:

Myostatin (also known as growth differentiation factor 8, abbreviated 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.

 Biochemistry

Myostatin 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 binds to the activin type II receptor, resulting in a recruitment of a coreceptor called Alk-3 or Alk-4. This coreceptor then initiates a cell signaling cascade in the muscle, which includes the activation of transcription factors in the SMAD family - SMAD2 and SMAD3. These factors then induce myostatin-specific gene regulation. When applied to myoblasts, myostatin inhibits their differentiation into mature muscle fibers.

Recently, myostatin has also been shown to inhibit Akt, a kinase that is sufficient to cause muscle hypertrophy, in part through the activation of protein synthesis.

Therefore, myostatin acts in two ways, by inhibiting muscle differentiation and by inhibiting Akt-induced protein synthesis.

 Discovery and sequencing

The gene encoding myostatin was discovered in 1997 by geneticists Alexandra McPherron and Se-Jin Lee who also produced a strain of mutant mice that lack the gene. These myostatin "knockout" mice have approximately twice as much muscle as normal mice. These mice were subsequently named "mighty mice".

Naturally occurring myostatin "nulls" have been identified in cattle, whippets, and humans; in each case the result is a dramatic increase in muscle mass. A mutation in the 3' UTR of the myostatin gene in Texel sheep creates target sites for the microRNAs miR-1 and miR-206. This is likely to cause the muscular phenotype of this breed of sheep.