Comparison
Follistatin (FST) vs. Mod GRF (1-29)
Two peptides side-by-side — identity, evidence base, legal status and known adverse events.
Identity
Category
Growth
Growth
CAS no.
122956-17-2
863288-34-0
Molecular weight
35000 g/mol
3367.9 g/mol
Half-life
no data
0.5 h
Sequence
Glykoprotein, ~315 Aminosäuren in der zirkulierenden Hauptform (Sequenz isoformabhängig, kein einheitliches kurzes Peptid)Tyr-D-Ala-Asp-Ala-Ile-Phe-Thr-Gln-Ser-Tyr-Arg-Lys-Val-Leu-Ala-Gln-Leu-Ser-Ala-Arg-Lys-Leu-Leu-Gln-Asp-Ile-Leu-Ser-Arg-NH2Mechanism of action
Follistatin (FST)
Follistatin binds with high affinity to activin and to myostatin (GDF-8), as well as related TGF-β ligands such as GDF-11 and some BMPs, preventing their binding to the activin type-II receptors. Myostatin is a negative regulator of skeletal muscle mass; by sequestering myostatin, its growth-inhibiting signalling is removed (de-repression). Because follistatin additionally neutralises activin, it acts on several muscle-inhibiting pathways at once — in animal models this produced greater muscle gain than knocking out myostatin alone. Several isoforms exist (including FST-288 and FST-315) that differ in tissue binding via heparan sulfate. The FST344 variant used in gene therapy was chosen to reduce binding to off-target structures.
Mod GRF (1-29)
Synthetic analogue of the first 29 amino acids of growth-hormone-releasing hormone (GHRH 1-29). Four amino-acid substitutions (D-Ala at position 2, Gln at 8, Ala at 15, Leu at 27) are intended to slow degradation by dipeptidyl peptidase-IV and increase enzymatic stability relative to native GHRH. Like the native hormone and sermorelin, it binds the GHRH receptor on somatotroph cells of the anterior pituitary; mechanistically this is expected to stimulate endogenous growth-hormone release. Unlike the DAC-conjugated CJC-1295 variant, it lacks albumin binding, so its duration of action remains short.
Evidence base
Highest evidence
Human trial
Human trial
Studies
4
4
of which in humans
1
4
Effects recorded
4
3
Open conflicts
1
1
Documented adverse events
1
0
Legal status
Full entries
Frequently asked questions
- What is the difference between Follistatin (FST) and Mod GRF (1-29)?
- Follistatin (FST) is classified as "Growth", while Mod GRF (1-29) is classified as "Growth". Follistatin (FST): Follistatin is an endogenous glycosylated binding protein (~35 kDa, considerably larger than typical peptides) that binds and neutralises members of the TGF-β superfamily, including activin and myostatin (GDF-8). In animal models, raising follistatin de-represses muscle growth. Clinically it has been studied mainly via AAV gene therapy (FS344) in muscular dystrophies. Follistatin is not an approved drug; human efficacy and safety data are limited and stem mostly from early gene-therapy trials and preclinical research. A 'follistatin-344' product is sold on the grey market, the identity and purity of which cannot be verified without analytics. Mod GRF (1-29): Tetrasubstituted synthetic analogue of GHRH(1-29), traded on the grey market as "CJC-1295 without DAC". Closely related to sermorelin (GHRH 1-29); a short-acting growth-hormone-releasing-hormone analogue often combined with a GHRP/ghrelin mimetic. Not approved as a medicinal product. Direct human trials of this exact analogue are essentially absent; the factual basis relies on related GHRH(1-29) analogues. This page contrasts both neutrally and source-based — with no usage or dosing recommendation.
- Which peptide is better supported by science, Follistatin (FST) or Mod GRF (1-29)?
- The highest available evidence level is "Human trial" for Follistatin (FST) and "Human trial" for Mod GRF (1-29). A higher evidence level means more robust data, but says nothing about suitability for an individual. The full body of evidence is on each peptide's own page.
- What is the legal status of Follistatin (FST) and Mod GRF (1-29) in Germany and the United States?
- Germany: Follistatin (FST) — Unapproved, Mod GRF (1-29) — Unapproved. United States: Follistatin (FST) — Unapproved, Mod GRF (1-29) — Research only. These are factual summaries with source and review date on the individual pages.