Peptide Registry

GDF-8

Price range: $119.00 through $199.00

  • Contents: GDF-8 (Growth Differentiation Factor 8; Myostatin; mature recombinant form)
  • Form: Lyophilized powder
  • Purity: >99%
Quantity Discount Price
1 - 3 - -
4 - 7 10% -
8 + 18% -
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Description

GDF-8 is an endogenous member of the TGF-beta superfamily and one of the most thoroughly characterized negative regulators of skeletal muscle mass in the published literature. It is synthesized as a 375-amino acid precursor that undergoes sequential proteolytic processing: furin-like proprotein convertases cleave the precursor to yield a latent non-covalent complex of the N-terminal prodomain and the C-terminal mature growth factor, and subsequent tolloid metalloprotease cleavage within the prodomain destabilizes this complex and releases the active mature GDF-8 dimer. As the primary endogenous ligand for the ActRII/ALK4-ALK5 receptor system, it serves as a reference compound in specialty research peptide models.

Chemical Information

  • Chemical Name: Growth Differentiation Factor 8 (GDF-8; Myostatin)
  • Also Known As: Myostatin; GDF8; MSTN
  • Compound Class: Endogenous TGF-beta superfamily ligand (mature recombinant disulfide-linked dimer)
  • Precursor Length: 375 amino acids (full precursor)
  • Mature Form: 109 amino acids (C-terminal growth factor domain, disulfide-linked homodimer)
  • Molecular Weight: approximately 25 kDa (mature dimer)
  • Primary Receptors: ActRIIB (high affinity), ActRIIA, ALK4, ALK5
  • Downstream Pathway: SMAD2/3 phosphorylation; p38 MAPK; ERK1/2; Wnt
  • Gene: MSTN (chromosome 2q32.2)

Applications

  • ActRII receptor binding and signaling studies. GDF-8 provides the endogenous-sequence ligand for ActRIIA and ActRIIB receptor binding assays; used to characterize receptor affinity, kinetics, and downstream SMAD2/3 phosphorylation in cell-based signaling models
  • Antagonist characterization research. GDF-8 is the reference ligand for evaluating the neutralizing activity of pathway antagonists, including follistatin isoforms and decoy receptor constructs. Follistatin 315 and ACE-031 are both studied as GDF-8 pathway antagonists, making GDF-8 itself the essential reference compound in these experimental designs
  • Propeptide latency and activation mechanism research. The latent GDF-8 complex and its sequential furin/tolloid activation pathway are active research areas. GDF-8 mature form is used in models studying the prodomain-growth factor interface, activation kinetics, and propeptide inhibitory mechanisms
  • SMAD2/3 pathway studies in muscle satellite cell biology. GDF-8 activates canonical SMAD2/3 signaling in satellite cells, inhibiting myoblast proliferation and differentiation. Researchers use it when studying how TGF-beta family signaling regulates satellite cell fate
  • Reproductive and embryo biology research. GDF-8 is expressed in placenta and reproductive tissues. Studies document ALK5-SMAD2/3 signaling roles in trophoblast biology and embryo development, extending research relevance beyond skeletal muscle
  • Bone-muscle crosstalk research. GDF-8 signaling connects skeletal muscle biology to bone homeostasis through shared receptor systems, making it relevant in musculoskeletal system research beyond isolated muscle cell models
  • p38 MAPK and ERK1/2 non-canonical pathway research. GDF-8 activates non-SMAD pathways including p38 MAPK and ERK1/2; these pathways are studied alongside canonical SMAD signaling to characterize the full downstream signaling profile in different cell types

Storage and Handling

Store lyophilized powder at -20C for long-term stability. Store reconstituted solutions at 2-8C and use promptly. Avoid repeated freeze-thaw cycles, which can cause aggregation and loss of receptor binding activity. Protect from light and elevated temperatures. As a recombinant disulfide-linked homodimer, GDF-8 is sensitive to reducing conditions. Thus, avoid reducing agents in reconstitution buffers.

Compliance Notice

GDF-8 is for laboratory research use only. It is not for human or veterinary use and carries no therapeutic, diagnostic, or clinical indication. This product has not been evaluated by the FDA. By purchasing this product, the buyer confirms that they will follow appropriate institutional safety procedures and use it exclusively for controlled research.

Frequently Asked Questions

What is GDF-8 and how does it signal?

GDF-8 (growth differentiation factor 8, also known as myostatin) is an endogenous TGF-beta superfamily ligand that binds ActRIIB with high affinity and ActRIIA at lower affinity. Receptor binding recruits ALK4 or ALK5 type I receptors, forming a signaling complex that phosphorylates SMAD2 and SMAD3. Phosphorylated SMAD2/3 partners with SMAD4 and translocates to the nucleus to drive downstream gene transcription. GDF-8 also activates non-canonical pathways including p38 MAPK, ERK1/2, and Wnt. Researchers use recombinant mature GDF-8 as the reference endogenous ligand for ActRII pathway studies in cell-based experimental models.

Why is GDF-8 used as a reference compound in pathway antagonist research?

GDF-8 is the primary endogenous ligand for the ActRIIA/ActRIIB receptor system. Compounds studied as pathway antagonists, including follistatin isoforms and ACVR2B-based decoy receptors, are characterized by their capacity to prevent GDF-8 receptor engagement. Without the reference ligand, antagonist potency, binding affinity, and inhibitory mechanism cannot be measured in receptor binding or cell signaling assays. GDF-8 provides the defined endogenous-sequence ligand against which antagonist activity is quantified, making it an essential component of experimental designs using any ActRII pathway inhibitor.

What is the propeptide latency mechanism and why does it matter for research design?

GDF-8 is secreted as a latent complex in which the N-terminal prodomain non-covalently associates with the mature growth factor and prevents receptor binding. Tolloid metalloprotease cleavage within the prodomain destabilizes this complex and releases active GDF-8. Researchers studying myostatin biology need to account for this activation mechanism: experiments using GDF-8 in cell culture models require the mature active form to observe receptor signaling, while studies of endogenous myostatin regulation may involve the latent complex and its activation pathway. The propeptide itself is an endogenous inhibitor used in studies characterizing the prodomain-growth factor binding interface.