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Myostatin (also known as GDF8) and GDF11 are nearly identical in their active domains. Like other members of the TGFβ superfamily, myostatin and GDF11 are secreted in a small latent complex, which includes the prodomain linked to the active domain. The active domain is typically found as a dimer, linked by cysteine-bonds. On immunoblotting, active dimers migrate at 25 KDa and, if fully reduced to monomers, 12.5 KDa.
