Follistatin-315

Explore Follistatin-315, a circulating activin-binding protein studied for muscle growth, fibrosis control, and tissue repair.

Educational summaryPeptide research profile

(how we review)

Dosing & scaling, explained

The moderated mass amounts below are retained for comparison. Near-duplicates, mix-dependent volumes and device markings are excluded. This is educational source context, not a protocol or recommendation.

Mass amounts available for comparison

  1. Lower range100 mcgDose

    Recorded example with no verified study backing; shown for amount literacy only.

  2. Mid range300 mcgDose

    Recorded example with no verified study backing; shown for amount literacy only.

Only mcg or mg amounts are retained. The calculator derives mL, syringe units or pen clicks from the current vial strength, water volume and device.

No independently verified schedule

Evidence context

No clinical amount or schedule is inferred from this material. Source verification is pending, and every displayed amount remains educational context rather than guidance.

Storage, handling and interpretation

Product identity

Verify the exact compound, formulation and amount against the product label or certificate before calculation.

Storage & handling

Follow the product label, certificate and validated laboratory SOP; no universal storage assumption is applied here.

Prepared solutions

Label concentration and preparation date, use sterile technique where applicable, and follow a validated stability protocol.

Reported protocols for Follistatin-315

What published studies and recent community write-ups report about amounts, timing and course length. 4 clinical, 2 preclinical and 2 community-reported rows, each linked to its source. These are descriptions of what others report, not instructions, and nothing here is medical advice.

ContextDoseFrequencyRouteCourseSource
Clinical4 rows
Becker muscular dystrophy gene transfer, phase 1/2a6 adults with Becker muscular dystrophy, in two cohorts of 33 x 10^11 vg/kg per leg (cohort 1) or 6 x 10^11 vg/kg per leg (cohort 2) of AAV1.CMV.FS344Single administration, given as direct injections into both quadricepsIntramuscularOne procedure, followed for up to 2 yearsNot applicable; gene transfer is a single eventMolecular Therapy (PubMed Central)2015
Two patients gained 58 m and 125 m on the 6-minute walk test and one did not change in the lower-dose cohort; in the higher-dose cohort two gained 108 m and 29 m and one did not improve. Biopsies showed less endomysial fibrosis, less central nucleation and fibre hypertrophy, most at the high dose, with no adverse effects reported. The vector carries FS344, which becomes FST-315 once the signal peptide is cleaved, so this is the closest human evidence for this isoform and it is gene transfer rather than injected protein.
Sporadic inclusion body myositis gene transfer6 ambulatory adults with sporadic inclusion body myositis, compared with 8 untreated patients matched for age, sex and baseline6 x 10^11 vg/kg of rAAV1.CMV.huFS344Single administration to the quadriceps of both legsIntramuscularOne procedure, with an exercise regimen alongside and outcomes annualized to a median 1 yearNot applicableMolecular Therapy (PubMed)2017
Walking distance improved by 56.0 m per year in the treated group against a 25.8 m per year decline in the untreated comparison group. Four of six treated patients gained 58 to 153 m while two gained only 5 to 23 m, and the authors note that more advanced disease with established muscle loss remained a problem. Every participant also followed an exercise programme, so the treatment effect cannot be isolated.
Registered three-cohort dose escalation15 patients with Becker muscular dystrophy or sporadic inclusion body myositis2 x 10^11 vg/kg to one quadriceps, then 3 x 10^11 and 6 x 10^11 vg/kg per quadriceps bilaterallySingle administration per participantIntramuscularOne procedure, with safety as the primary endpoint over 2 yearsNot applicableClinicalTrials.gov2012
This is the registration behind the published Becker and inclusion body myositis reports, run at Nationwide Children's Hospital from 2012 and completed in October 2017. Its listed primary outcome is safety at 2 years, the enrolment is 15 across the three cohorts, and no results have been posted to the registry.
Plasmid injection aimed at raising circulating FST-31543 adult volunteers of both sexes, aged 23-88, median age 4650 mcg of FST-344 plasmid complexed with linear polyethyleneimine in 400 microlitres of salineSingle injectionSubcutaneous, into abdominal fatOne injection, with measurements at baseline and 3 monthsNone describedMinicircle Inc. (company preprint, medRxiv)2024
The stated design was to transfect abdominal fat cells with the 344 variant so they would secrete FST-315 into the blood. Serum follistatin rose from a mean 8.58 ng/mL to 24.03 ng/mL at three months, fat-free mass rose 1.96 lb on average, body fat fell 0.87% and extrinsic epigenetic age fell 7.10 years, with no severe adverse effects reported. This was a single-arm, company-run study with no control group, a three-month window and a preprint that has not been peer reviewed, and a minority of participants had a large rise in LDL cholesterol.
Preclinical2 rows
Primate gene transfer, the study behind the human trialsCynomolgus macaque monkeys1 x 10^13 vector genomes in total per treatment, given as three injections into one quadricepsSingle administrationIntramuscularOne procedure, with long-term follow-up of transgene expressionNot applicableScience Translational Medicine (PubMed)2009
Muscle size and strength rose markedly and durably in the injected leg, and long-term expression produced no abnormal changes in the morphology or function of key organs, which is the safety argument that carried the approach into people. PubMed records an erratum to this paper published by Science Translational Medicine in August 2026.
Engineered FST-315 fusion protein in mice, repeated dosingC57BL/6 wild-type mice and mdx dystrophic mice1-50 mg/kg in the wild-type dose range; 3, 10 and 30 mg/kg in the mdx studiesTwice weeklyIntravenous or subcutaneous4 weeks in wild-type mice, 12 weeks in the mdx studiesNone describedSkeletal Muscle (PubMed Central)2018
Muscle mass and fibre size rose dose dependently, grip strength and tetanic force improved, and necrosis, inflammation and fibrosis markers fell at 10 and 30 mg/kg, with larger effects than an anti-myostatin antibody at the same dose. This is the only repeated-dose protein schedule published for a follistatin-based molecule, and it required an engineered Fc fusion at milligram-per-kilogram doses rather than native protein.

How a course is commonly described

  1. Days 1-7Community-reported

    Community charts describe 100 mcg once daily subcutaneously as the conservative starting figure, drawn as 10 units from a 1 mg vial reconstituted in 1 mL of bacteriostatic water. Nothing is measured at this stage and no study supports the route.

  2. Weeks 2-3Community-reported

    The commonly quoted figure rises to 200 mcg once daily, with 300 mcg listed as the reported ceiling. Daily injection is justified on the grounds that the protein clears from circulation within hours, a point every one of these pages concedes is unmeasured for this product.

  3. End of a 10-30 day blockCommunity-reported

    Blocks are described as running 10 to 30 days rather than months, and the stated reason is arithmetic rather than biology: 12 weeks at 200 mcg a day would consume roughly 17 vials of 1 mg. Guides that discuss stopping give no biomarker or endpoint to check.

  4. Clinical comparisonClinical

    Human dosing on record is a single event, not a course: one intramuscular AAV administration at 3 x 10^11 or 6 x 10^11 vg/kg per leg, with outcomes measured over 1 to 2 years afterwards. No repeated-dose schedule of follistatin protein has been tested in a person by any route.

  • There is no validated human dose, frequency or cycle length for injected follistatin protein of any isoform, and no published pharmacokinetic study of FST-315 in people. The 50-300 mcg daily figures in circulation come from vendor charts and self-experimentation reports, and the pages that publish them say so.
  • Scale is the central problem with those figures. The follistatin molecule that produced hypertrophy in dystrophic mice had to be engineered, with heparan-sulfate binding removed and an IgG4 Fc attached to slow clearance, and it was dosed at 3 to 30 mg/kg twice weekly. That is thousands of times more protein exposure than a flat 100 mcg injection.
  • The isoform difference is a safety matter, not a marketing one. Follistatin interacts with the pituitary activin and inhibin axis and can suppress follicle-stimulating hormone, which is why the gene therapy programme deliberately used the FS344 variant that matures into FST-315, the form with roughly ten-fold lower activin affinity than FST-288. Follistatin is not approved anywhere and sits on the WADA prohibited list.
Sources for this section (14)
  1. A phase 1/2a follistatin gene therapy trial for Becker muscular dystrophyMolecular Therapy (PubMed Central)2015Clinical
  2. Follistatin Gene Therapy for Sporadic Inclusion Body Myositis Improves Functional OutcomesMolecular Therapy (PubMed)2017Clinical
  3. Follistatin Gene Transfer to Patients With Becker Muscular Dystrophy and Sporadic Inclusion Body Myositis (NCT01519349)ClinicalTrials.gov2012Clinical
  4. Follistatin Gene Therapy Improves Ambulation in Becker Muscular DystrophyJournal of Neuromuscular Diseases (PubMed)2015Clinical
  5. Hair regrowth following a Wnt- and follistatin containing treatment: safety and efficacy in a first-in-man phase 1 clinical trialJournal of Drugs in Dermatology (PubMed)2011Clinical
  6. Plasmid delivery of follistatin gene therapy safely improves body composition and lowers extrinsic epigenetic age in sex- and age-diverse adult human subjectsMinicircle Inc. (company preprint, medRxiv)2024Clinical
  7. Follistatin gene delivery enhances muscle growth and strength in nonhuman primatesScience Translational Medicine (PubMed)2009Preclinical
  8. Myostatin and activin blockade by engineered follistatin results in hypertrophy and improves dystrophic pathology in mdx mouse more than myostatin blockade aloneSkeletal Muscle (PubMed Central)2018Preclinical
  9. Biological activity of follistatin isoforms and follistatin-like-3 is dependent on differential cell surface binding and specificity for activin, myostatin, and bone morphogenetic proteinsEndocrinology (PubMed)2006Preclinical
  10. Insights into the Impact of Heterogeneous Glycosylation on the Pharmacokinetic Behavior of Follistatin-Fc-Based BiotherapeuticsDrug Metabolism and Disposition (PubMed)2015Preclinical
  11. Regulation of muscle mass by follistatin and activinsMolecular Endocrinology (PubMed)2010Preclinical

Plus 3 community resources (dosing guides, forum threads and vendor write-ups), reported above but not linked.

Overview

Follistatin-315 is the mature, circulating form of human follistatin: the product of the FST gene's 344-residue precursor (UniProt P19883, computed mass 38,007 daltons) once its 29-residue signal peptide is removed, leaving a glycosylated 315-residue chain. It binds activin A and myostatin and keeps them off the activin type IIB receptor, and because its acidic C-terminal tail stops it from sticking to cell-surface heparan sulfate it stays in the blood instead of on tissue, which is the practical difference between it and the shorter FST-288 isoform. PubChem holds no compound record for any follistatin isoform, so there is no molecular formula, CAS number, InChIKey or molar mass to report here; PubChem indexes the protein only under accession P19883, and the identifier quoted on older pages (178101631) is a PubChem substance number rather than a compound record for follistatin. No human study has ever injected recombinant follistatin protein of either isoform: the human record is intramuscular AAV gene transfer of the FS344 variant, which is processed to FST-315 after secretion, one company-run plasmid study, and a 26-subject dermatology trial of a cell-derived complex containing follistatin alongside KGF and VEGF, where hair shaft thickness rose 6.3% and terminal hair density 20.6% at 12 weeks. It is approved nowhere, is sold as a research chemical, and myostatin-pathway inhibitors are on the WADA prohibited list.

What researchers are exploring

These themes organize the educational information currently available. Individual claims remain under source review and are not treatment claims.

  • 1

    Muscle Growth Research

    Myostatin inhibition and performance insights

  • 2

    Inflammation & Fibrosis

    Autoimmune, pulmonary, and radiotherapy studies

  • 3

    Vascular & Organ Support

    Endothelial recovery and renal protection

  • 4

    Biomarkers & Protein Engineering

    Disease monitoring and synthetic derivatives

  • 5

    Summary

    Research considerations

What is known and what still needs verification

Available context is organized without assigning unsupported study models or evidence grades.

  • Not graded

    Muscle Growth Research

    Myostatin inhibition and performance insights

  • Not graded

    Inflammation & Fibrosis

    Autoimmune, pulmonary, and radiotherapy studies

Amounts recorded for Follistatin-315

These amount records are independent from vial strength, reconstitution volume and measuring device. A recorded source is not the same as study backing, and these values are not recommendations.

  • 1
    Dose · lower endpointSign in for schedule, duration and source context.
    100 mcg
  • 2
    Dose · upper endpointSign in for schedule, duration and source context.
    300 mcg

Identity, limitations and unknowns

Molecular profile

Sequence
GNCWLRQAKN GRCQVLYKTEL SKEECCSTGR LSTSWTEEDV NDNTLFKWMIF NGGAPNCIPCK ETCENVDCGP GKKCRMNKKN KPRCVCAPDCS NITWKG PVCGLDGKTYR NECALLKARCK EQPELEVQYQG RCKKTCRDVFC PGSSTCVVDQT NNAYCVTCNRI CPEPASSEQYL CGNDGVTYSSA CHLRKATCLLG RSIGLAYEGKC IKAKSCEDIQC TGGKKCLWDFK VGRGRCSLCDE LCPDSKSDEP VCASDNATYA SECAMKEAACS SGVLLEVKHS GSCNSISEDTE EEEDE DQDYSFPISSILEW
Molecular Weight
~35 kDa (mature protein)
Synonyms
Activin-binding protein, FSH-suppressing protein, FST-315

Important limitations

  • Individual claims and source links have not yet completed editorial verification.
  • Evidence level, applicable study model, formulation, route and population remain unassigned.

Sources

1 link carried over from the earlier page, awaiting verification.

  1. Source link (pmc.ncbi.nlm.nih.gov)Verification pendingNot graded