Recombinant human Myostatin Propeptide protein
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.
別名を表示する
GDF8, MSTN, Growth/differentiation factor 8, GDF-8, Myostatin
Reactivity data
配列情報
出荷温度及び保存条件
出荷温度
短期保存期間
長期保存温度
補足情報
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.
製品の性状
製品の状態
Lyophilized
一般的な情報
機能
Acts specifically as a negative regulator of skeletal muscle growth.
配列の類似性
Belongs to the TGF-beta family.
翻訳後修飾
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.
ターゲットの情報
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