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Compound record / IGF & growth factors

MGF

A splice variant of IGF-1 expressed by muscle in response to mechanical loading and damage.

Animal models only Research use only Banned in sport
Written by Lindy Health editorial Updated 2026-10-18 Also known as Mechano Growth Factor, IGF-1Ec, IGF-1 splice variant
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MGF · molecular diagram awaiting verified source

What is MGF?

MGF stands for mechano growth factor. It is a version of insulin-like growth factor 1 (IGF-1) that muscle makes for itself after it is stretched, overloaded or damaged. Scientists call it IGF-1Ec in humans, after the particular way the IGF-1 gene is spliced to produce it.

It was described in the late 1990s by Geoffrey Goldspink's group in London, who cloned different forms of IGF-1 from exercised muscle. One of them was only detectable after injury or mechanical activity, so they named it mechano growth factor.6 The group proposed that it acts as a local repair signal rather than a hormone that circulates around the body.

MGF is not an approved drug. A synthetic peptide based on its unique tail is sold online as a research chemical, mostly to bodybuilders who hope it will help muscles grow and recover. It is banned in sport.

  1. Anecdotal only
  2. In vitro only
  3. Animal models only
  4. Preliminary human
  5. Clinical trials
  6. Regulator approved
About 1 published human study. Evidence level describes the literature, not a recommendation.
US statusNot FDA approved
Half-life~5-7 minutes
RoutesSubcutaneous, Intramuscular
Reported range100-200 mcg
Banned in sportYes (WADA)

How MGF works

Muscle fibers cannot divide. To grow or repair, they rely on a pool of stem cells called satellite cells that sit along the fiber, wake up after damage, multiply and fuse into the fiber to add new nuclei. The theory is that MGF is the early wake-up signal for those cells, released in a pulse after hard exercise or injury. Ordinary IGF-1 then takes over to drive protein building.7

That theory also explains the interest in aging. Older muscles appear less able to switch on MGF after exercise, which might be one reason they repair and grow less well.1

In more precise terms, alternative splicing of the IGF-1 gene produces precursor proteins with different E-domain tails. In MGF, a reading-frame shift gives a distinct C-terminal sequence and a different mode of action from liver IGF-1.6 The peptide sold as MGF is usually a synthetic version of this E-domain tail, about 24 amino acids long, rather than the full precursor. The original group proposed that this distinct sequence is what replenishes the satellite cells.1 It is thought to act apart from the standard IGF-1 receptor, but the mechanism is still poorly understood.4

The growth hormone axis
Hypothalamus GHRH (+) Somatostatin (−) Pituitary releases GH in pulses Ghrelin receptor(GHS-R) GH Liver IGF-1 Muscle, bone, fat growth, repair, fat use IGF-1 feeds back to slow GHRH and GH release, which is why the axisself-limits.

IGF-1 analogues act at the end of the axis, directly on tissues, bypassing the pituitary and the liver.

What the research shows on MGF

Almost all the research is in cells and animals. In animal models, MGF expression rises in muscle, bone and tendon after mechanical damage and in brain and heart after loss of blood supply. MGF and its short peptide have been tested as experimental therapies for muscular dystrophy and brain injury in animals.4 In animal muscle, MGF has been shown to activate satellite cells, leading to hypertrophy or regeneration.4

Human work is observational. Studies taking muscle biopsies before and after resistance exercise found that MGF messenger RNA rises after short-term high-resistance exercise in young people but not in older people.5 Other work suggested that growth hormone treatment combined with resistance training shifted IGF-1 splicing toward MGF in older adults.1 These studies measure the body's own MGF gene activity. They do not test injecting a synthetic peptide.

That gap is the key point. There are no published controlled trials of injected MGF peptide in humans for muscle growth, recovery or any disease. Some independent labs have also had trouble reproducing the claim that the E-domain peptide acts separately from IGF-1, so the basic biology is still debated.

Studied for: Satellite cell activation research, Muscle repair studies.

MGF reference data

Molecular weight2,867 Da
FDA statusNot approved for any indication.
Prohibited in sportYes, under the WADA prohibited list

MGF dosage in published research

Read this first These figures describe ranges reported in published research and in practitioner protocols. They are a reference, not a recommendation, and this page is not a prescription. Dosing for any compound should be set by a licensed clinician.
Reported range100-200 mcg
FrequencyPost-training, localised
Typical cycle4 weeks
Reconstitution2 mg vial + 2 mL bacteriostatic water = 1.0 mg/mL
On a 100-unit syringe100 mcg = 10.0 units · 200 mcg = 20.0 units

Open this in the dosage calculator ↗

How MGF is used in practice

MGF is not prescribed by US doctors or telehealth services, and it is not a lawful compounding ingredient. It is bought as freeze-dried powder from research-chemical sites, mixed with bacteriostatic water and injected, often straight into a trained muscle right after a workout. The practice is based on the local, pulsed way the body releases its own MGF. Some sellers also market it for tendon, joint and even brain recovery, pointing to animal work on MGF in bone, tendon and brain injury.4 None of those uses has been tested in people.

The native peptide breaks down in minutes in blood, which is why vendors also sell a pegylated version. There is no evidence that injecting the short peptide reproduces what natural MGF does inside muscle. Bodybuilding interest was flagged early by researchers, who warned that a factor that kick-starts hypertrophy had obvious abuse potential.2

Quality is a real issue. Research-chemical peptides have no checks on identity, purity, dose or sterility. A fragile peptide that degrades quickly is especially likely to arrive inactive or contaminated.

MGF risks and side effects

Because there are no human trials, there is no reliable list of side effects. Users report injection-site soreness, redness and fatigue. Intramuscular injection of non-sterile products risks infection and abscesses. Because MGF is related to IGF-1, low blood sugar is a theoretical concern, especially if it is combined with insulin or IGF-1 analogs, but this has not been measured.

The theoretical concern is cancer. MGF is part of the IGF-1 system, which promotes cell growth and survival, and IGF-1 signaling is involved in many tumors. Anyone with active or suspected cancer, or a strong history of it, should avoid it. It should not be used in pregnancy. Interactions with insulin, growth hormone and other peptides are uncharacterized.

For competitive athletes, MGF is on the World Anti-Doping Agency's prohibited list, and testing methods for IGF-1 analogs exist.

Reported side effects

Injection-site reactionsTransient fatigue
ContraindicationsActive or suspected malignancy, Pregnancy
InteractionsPoorly characterised

Alternatives to MGF

The most reliable way to raise your own MGF and build muscle is progressive resistance training, which works even in older adults.3 Adequate protein intake, creatine monohydrate and good sleep have solid evidence for muscle size and strength. For recovery between hard sessions, planned rest days, enough total calories and sensible training volume do more than any injected product.

For people with diagnosed growth hormone deficiency, approved somatropin products are the medical option. For age-related muscle loss, there is no approved drug, and supervised exercise remains the standard treatment.

The bottom line on MGF

MGF is a real and interesting piece of muscle biology, but the evidence stops at cells, animals and gene-expression studies. There are no human trials of the injected peptide, the products are unregulated and unstable, and it is banned in sport. Resistance training remains the proven way to put the body's own MGF to work.

Questions for a clinician

  • What evidence applies to my situation, and at what level?
  • What established alternatives should I consider first?
  • What monitoring would be necessary, and how often?
  • Can this be prescribed at all where I live, or only sold for research?

MGF FAQ

What is MGF?

A splice variant of IGF-1 expressed by muscle in response to mechanical loading and damage. It is classed as IGF & growth factors.

Is MGF FDA approved?

No. MGF is not approved by the FDA for any indication. Material sold online is labelled for research use only.

Is MGF legal in the US?

MGF is not FDA approved and is not on FDA’s 503A bulks list. US compounding pharmacies cannot routinely prepare it.

What dose of MGF is used in research?

Published research and practitioner protocols report 100-200 mcg, post-training, localised, typically for 4 weeks. This is a reference range, not a recommendation; dosing should be set by a licensed clinician.

How is MGF reconstituted?

A 2 mg vial mixed with 2 mL of bacteriostatic water gives 1.0 mg/mL. At that concentration 100 mcg is 10.0 units on a 100-unit insulin syringe.

What are the side effects of MGF?

Reported side effects include injection-site reactions, transient fatigue. Contraindications: active or suspected malignancy, pregnancy.

What is the half-life of MGF?

The reported half-life of MGF is ~5-7 minutes.

Is MGF banned in sport?

Yes. MGF falls under the World Anti-Doping Agency prohibited list.

References

Regulatory and primary sources

  1. FDA: Bulk drug substances that may present significant safety risks (Category 2 and withdrawn nominations) ↗ · content current as of April 22, 2026; checked October 18, 2026
  2. FDA: Bulk drug substances used in compounding under section 503A ↗ · how the 503A categories work
  3. WADA Prohibited List ↗ · current year
  4. FDA: Unapproved drugs and "research use only" products ↗ · regulatory status of non-approved products

Published literature

  1. Goldspink G, Harridge SD. Growth factors and muscle ageing.Exp Gerontol 2004.PubMed 15501012 · doi:10.1016/j.exger.2004.08.010
  2. Goldspink G, Wessner B, Bachl N. Growth factors, muscle function and doping.Curr Opin Pharmacol 2008.PubMed 18353722 · doi:10.1016/j.coph.2008.02.002
  3. Harridge SD. Ageing and local growth factors in muscle.Scand J Med Sci Sports 2003.PubMed 12535315 · doi:10.1034/j.1600-0838.2003.20235.x
  4. Dai Z, Wu F, Yeung EW, et al.. IGF-IEc expression, regulation and biological function in different tissues.Growth Horm IGF Res 2010.PubMed 20494600 · doi:10.1016/j.ghir.2010.03.005
  5. Janssen JA. Impact of Physical Exercise on Endocrine Aging.Front Horm Res 2016.PubMed 27348867 · doi:10.1159/000445158
  6. Goldspink G. Gene expression in skeletal muscle.Biochem Soc Trans 2002.PubMed 12023866
  7. Goldspink G. Age-related loss of skeletal muscle function; impairment of gene expression.J Musculoskelet Neuronal Interact 2004.PubMed 15615114
  8. Heilig CW, Deb DK, Abdul A, et al.. GLUT1 regulation of the pro-sclerotic mediators of diabetic nephropathy.Am J Nephrol 2013.PubMed 23817135 · doi:10.1159/000351989

Literature retrieved from PubMed on October 16, 2026, favouring human studies and reviews. Numbered markers in the text show which paper supports which statement; uncited entries are background reading.

A useful next read.