GDF-8

Third-Party Tested

Independent lab verified

Batch-Specific CoA

Publicly accessible

YPB.233

Reference number

1mg

Lyophilized vial

Origin

GDF-8, commonly known as Myostatin, was discovered by Se-Jin Lee and Alexandra McPherron at Johns Hopkins University School of Medicine in 1997. Their landmark paper demonstrated that mice lacking the GDF-8 gene developed dramatically increased muscle mass — the 'mighty mice' phenotype that launched the myostatin research field.

Research Lineage

McPherron and Lee's 1997 Nature paper is one of the most cited in muscle biology. Naturally occurring myostatin mutations have since been identified in Belgian Blue cattle, Texel sheep, whippet racing dogs, and at least one documented human case (Schuelke et al., 2004). The compound is studied both as a reference standard for myostatin-related research and as a tool for understanding muscle growth regulation.

Mechanism of Action

GDF-8 signals through the activin type IIB receptor (ActRIIB) and ALK4/ALK5 type I receptors, activating the Smad2/Smad3 transcription factor pathway. This suppresses myoblast proliferation and differentiation, acting as a negative regulator of muscle mass. Myostatin also inhibits the Akt/mTOR pathway that drives muscle protein synthesis. It circulates in an inactive latent complex and requires proteolytic activation by BMP-1/tolloid metalloproteinases.

Structural Notes

Disulfide-bonded homodimeric protein. Each monomer: 109 amino acids (mature form after proteolytic processing). Total molecular weight: ~25 kDa (mature dimer). Member of the TGF-beta superfamily with the characteristic cystine knot motif.