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MUSCLE & GROWTHPEPTIDE PROFILE

Follistatin-315

Also known as FST-315, FS-315, Follistatin isoform 315

Follistatin-315 is the primary circulating isoform of follistatin, a glycoprotein that binds and neutralizes members of the TGF-β superfamily, most notably myostatin (GDF-8) and activin A. FST-315 is produced by alternative splicing and accounts for approximately 95% of circulating follistatin. Unlike the tissue-bound FST-288 isoform, FST-315 has lower heparin affinity and acts systemically, making it the dominant endocrine regulator of muscle mass.

Last updated June 25, 2026

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Follistatin-315: quick citable summary

Follistatin-315 is listed by PeptaHub as a muscle & growth peptide with a research only legal-status classification. The page summarizes mechanism, research context, common routes, safety notes, and references for writers and AI answer engines.

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PeptaHub. “Follistatin-315: Mechanism, Research Context, Safety.” peptahub.com, 2026. https://peptahub.com/peptides/follistatin-315. Licensed CC BY 4.0.

License: Creative Commons Attribution 4.0 International. Link back to https://peptahub.com/peptides/follistatin-315.

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What is Follistatin-315?

Follistatin-315 is the primary circulating follistatin isoform that neutralizes myostatin and activin A. Overexpression produces 200-300% muscle mass increases in mice. Note the Becker muscular dystrophy gene-therapy trials used the FST-344 isoform, not FST-315.

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Overview

Follistatin-315 is the primary circulating isoform of follistatin, a glycoprotein that binds and neutralizes members of the TGF-β superfamily, most notably myostatin (GDF-8) and activin A. FST-315 is produced by alternative splicing and accounts for approximately 95% of circulating follistatin. Unlike the tissue-bound FST-288 isoform, FST-315 has lower heparin affinity and acts systemically, making it the dominant endocrine regulator of muscle mass.

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Mechanism of action

Follistatin-315 binds myostatin and activin A with nanomolar affinity (Kd ~5–10 nM), forming high-affinity complexes that prevent ligand binding to the ActRIIB/ALK4/5 receptor complex on muscle satellite cells. By blocking myostatin signaling, FST-315 disinhibits Smad2/3-mediated suppression of muscle protein synthesis, promoting myofiber hypertrophy and satellite cell proliferation. It also inhibits activin A signaling in bone, gonads, and brain, producing broader endocrine effects beyond skeletal muscle.

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Reported study ranges

PurposeRouteReported rangeFrequency
myostatin inhibition researchsubcutaneous50200 mcgdaily (limited by ~90 min half-life)

Reported ranges are for research context only. Consult a qualified healthcare professional before using any peptide.

Convert Follistatin-315 research-range units

Need to convert mg to mcg, dose volume, or U-100 syringe units? The Follistatin-315 dose calculator is preloaded with these ranges, or use the general dose unit converter.

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Research summary

Follistatin overexpression in transgenic mice produces roughly 200–300% increases in muscle mass, and engineered follistatin improved dystrophic pathology in mdx mice. The clinical data most often cited for "follistatin" is Mendell's phase 1/2a Becker muscular dystrophy trial, but that trial delivered the FST-344 isoform by AAV gene therapy, not the FST-315 isoform this page describes and not a peptide injection; two of six patients improved on the 6-minute walk test. There is no human trial of FST-315 peptide itself. Recombinant peptide delivery is limited by a short (~90 minute) half-life, which is the usual rationale for pursuing gene therapy instead. Research in sarcopenia and metabolic disease is active but preclinical.[1][2][3][4][5]

📄This section cites 5 peer-reviewed sources. View all references →
§ 04b

Evidence grading

Each claimed benefit is graded by the strength of available evidence. Grades reflect study quality, not effect size.

strong
Binds myostatin and activin A at nanomolar affinityWell-characterized biochemical binding studies of follistatin confirm high-affinity binding to myostatin and activin A
moderate
Induces muscle hypertrophy via myostatin blockadeMouse follistatin-overexpression and engineered-follistatin studies show large muscle mass gains (Gilson 2009; Lee 2010; Iskenderian 2018, mdx mice). Rodent data; the specific 200-300% figure is from transgenic overexpression, not peptide dosing
preliminary
AAV gene therapy tested in Becker muscular dystrophy used the FST-344 isoform, not FST-315Mendell Mol Ther 2015: phase 1/2a AAV1.CMV.FS344 by intramuscular quadriceps injection in 6 BMD patients; two improved on the 6-minute walk test, one showed no change. This trial delivered the 344 isoform, so it does not directly test FST-315 as sold
preliminary
Short half-life limits peptide utilityThe ~90 min half-life is the rationale usually given for gene-therapy over peptide delivery; no dedicated FST-315 peptide pharmacokinetic study was located to confirm the exact figure
preliminary
Reproductive effects via activin A inhibitionActivin A has established reproductive roles; direct FST-315 reproductive safety data in humans is not characterized

Strong = multiple RCTs · Moderate = limited trials or observational · Preliminary = animal or in vitro only · Insufficient = anecdotal or no published data

§ 05

Side effects

Potential reproductive effects (activin A inhibition)
Possible joint hypermobility
Injection site reactions

Side effects vary by individual. This is not an exhaustive list. Report unusual symptoms to a healthcare professional.

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Common stacks

Peptides commonly paired with Follistatin-315 for synergistic effects.

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Sourcing & access

Research compound

Follistatin-315 is classified as a research compound. Regulatory status varies by jurisdiction. Always verify current legal status and source from vendors providing third-party certificates of analysis (COA).

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Frequently asked questions

Follistatin-315 is a glycoprotein produced by alternative splicing that accounts for approximately 95% of circulating follistatin. It binds and neutralizes myostatin and activin A, making it the dominant endocrine regulator of muscle mass.

Follistatin-315 binds myostatin and activin A with nanomolar affinity, preventing them from activating the ActRIIB/ALK4/5 receptor complex on muscle satellite cells. By blocking myostatin signaling, it disinhibits Smad2/3-mediated suppression of muscle protein synthesis, promoting myofiber hypertrophy and satellite cell proliferation.

Follistatin-315 is a research peptide with potential side effects including reproductive effects from activin A inhibition, possible joint hypermobility, and injection site reactions. No approved human therapeutic applications exist; gene therapy approaches are in early clinical trials.

Mouse studies show dramatic 200-300% muscle mass increases with follistatin overexpression, but recombinant FST-315 peptide injection has limited utility due to its short half-life of about 90 minutes, and no human trial of the FST-315 peptide exists. The Becker muscular dystrophy gene-therapy trials that are often cited delivered the FST-344 isoform by AAV, not FST-315 and not a peptide, so they are not direct evidence for this product.

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Research references

  1. Inhibition of myostatin with emphasis on follistatin as a therapy for muscle diseaseRodino-Klapac LR, Haidet AM, Kota J, et al.Muscle Nerve, 2009PubMed
  2. Follistatin induces muscle hypertrophy through satellite cell proliferation and inhibition of both myostatin and activinGilson H, Schakman O, Kalista S, et al.Am J Physiol Endocrinol Metab, 2009PubMed
  3. Regulation of muscle mass by follistatin and activinsLee SJ, Lee YS, Zimmers TA, et al.Mol Endocrinol, 2010PubMed
  4. Myostatin and activin blockade by engineered follistatin results in hypertrophy and improves dystrophic pathology in mdx mouse more than myostatin blockade alone (mice)Iskenderian A, Liu N, Deng Q, et al.Skelet Muscle, 2018PubMed
  5. A phase 1/2a follistatin gene therapy trial for Becker muscular dystrophy (used the FST-344 isoform, not FST-315)Mendell JR, Sahenk Z, Malik V, et al.Mol Ther, 2015ClinicalTrials.gov
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