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High Purity Growth Hormone Peptides Myostatin Peptide GDF-8 Lyophilized Powder
High Purity Growth Hormone Peptides Myostatin Peptide GDF-8 Lyophilized Powder
  • >= 10  Kilogram US $50.000
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5000 Kilogram/Kilograms per 0
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Guangzhou
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Place of Origin:
China (Mainland)
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Kafen
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Product Description

Product name:Myostatin GDF-8
Purity:95%
Specification:1mg/vial
Appearance:White powder
Certificate:GMP
Storage:Dry Cool Place
Grade:Medicine Grae

 

What is the GDF 8 / Myostatin ?

 

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.

 

Structure and mechanism of action
Human myostatin consists of two identical subunits, each consisting of 109 (NCBI database claims human myostatin is 375 residues long) amino acid residues. Its total molecular weight is 25.0 kDa. The protein is inactive until a protease cleaves the NH2-terminal, or "pro-domain" portion of the molecule, resulting in the active COOH-terminal dimer.

Myostatin also inhibits Akt, a kinase that is sufficient to cause muscle hypertrophy, in part through the activation of protein synthesis. However, Akt is not responsible for all of the observed muscle hyperthrophic effects which are mediated by myostatin inhibition Thus myostatin acts in two ways: by inhibiting muscle differentiation, and by inhibiting Akt-induced protein synthesis.

Application:
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.
tibody. Should this product contain a precipitate we recommend microcentrifugation

 

1.Myostatin (GDF-8), a member of the TGFbeta superfamily, is a potent and specific negative regulator of skeletal muscle mass. In serum, myostatin circulates as part of a latent complex containing myostatin propeptide and follistatin-relatedgene.

2.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. The myostatin propeptide is negative regulator of myostatin in vivo.

3.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.

 

Myostatin (GDF8) is expressed uniquely in human skeletal muscle as a 12 kDa mature glycoprotein consisting of 113 amino acid residues and secreted into plasma. Myostatin is a member of the transforming growth factor ß superfamily of secreted growth and differentiation factors that is essential for proper regulation of skeletal muscle mass. Studies have shown that myostatin could play an important role in cardiac development and physiology.

Myostatin Usage
A growth factor that regulates the size of muscles beginning in early embryonic development and continuing throughout life. Myostatin acts by inhibiting the growth of muscles, It prevents them from growing too large. Myostatin is also known as growth and differentiation factor 8 (GDF-8)

How does GDF-8 work?
Some studies show that the lack of myostatin gives rise to impressive results in the increase of muscle mass both in humans and in animals. In bones specifically, the lack of myostatin increases its mineral density, resulting in an increase of the calcium levels of the organism. GDF-8 is stored in bones and it is necessary for the correct functionality of the heart, muscles, and nerves as well as for blood clotting.

Application
1) The gene encoding myostatin was discovered in 1997 by geneticists Se-Jin Lee and Alexandra McPherron who 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".

2) Naturally occurring deficiencies of myostatin have been identified in cattle by Ravi Kambadur, 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.

3) Human myostatin consists of two identical subunits, each consisting of 109 (NCBI database claims human myostatin is 375 residues long) amino acid residues. Its total molecular weight is 25.0 kDa. The protein is inactive until a protease cleaves the NH2-terminal, or "pro-domain" portion of the molecule, resulting in the active COOH-terminal dimer. Myostatin binds to the activin type II receptor, resulting in a recruitment of either coreceptor 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.


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