Recombinant human Myostatin Propeptide protein
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Recombinant human Myostatin Propeptide protein is a Human Fragment protein, in the 24 to 266 aa range, expressed in Escherichia coli, with >98%, suitable for SDS-PAGE, FuncS.
View Alternative Names
GDF8, MSTN, Growth/differentiation factor 8, GDF-8, Myostatin
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate long-term storage conditions
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Myostatin Propeptide inhibits the function of myostatin a member of the Transforming Growth Factor-beta (TGF-beta) superfamily. Myostatin typically suppresses muscle growth so the propeptide acts as a decoy permitting muscle hypertrophy by blocking myostatin activity. This regulation is important in maintaining muscle mass and function. The propeptide does not usually function as part of a large complex instead acting directly to neutralize myostatin in the extracellular environment.
Pathways
Myostatin and its propeptide play major roles in the TGF-beta signaling pathway. This pathway is significant in regulating cell growth and differentiation in various tissues including muscle. Myostatin Propeptide's inhibition of myostatin leads to increased activation of the Akt/mTOR pathway promoting protein synthesis and muscle growth. It also interacts with related proteins such as follistatin another myostatin inhibitor which enhances the modulation of muscle mass through similar mechanisms.
Specifications
Form
Lyophilized
General info
Function
Acts specifically as a negative regulator of skeletal muscle growth.
Sequence similarities
Belongs to the TGF-beta family.
Post-translational modifications
Synthesized as 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 molecule. The circulating form consists of a latent complex of the C-terminal dimer and other proteins, including its propeptide, which maintain the C-terminal dimer in a latent, inactive state. Ligand activation requires additional cleavage of the prodomain by a tolloid-like metalloproteinase.
Target data
Product promise
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