Compounds / MGF

MGF

Also known as: Mechano Growth Factor, IGF-1Ec, IGF-1 Ec splice variant

No human data Not FDA-approved Category: Growth Factors

The compounds described in this library are research-use-labeled chemicals and are not FDA-approved for human use. This content is factual scientific reference drawn from published literature. It is not medical, dosing, or purchasing advice. VialReport does not sell, supply, or distribute any compound.

Short summary

"MGF" is a market name for a synthetic peptide corresponding to part of the E-domain associated with an IGF-1 splice variant. The splice variant is genuinely expressed after mechanical stress, but whether the standalone synthetic peptide corresponds to a naturally released human product remains uncertain, and its claimed cellular effects have not been consistently replicated. No human clinical data.

Dive deeper

Origin and Development

The IGF-1 gene is alternatively spliced into several isoforms. The predominant circulating form, IGF-1Ea, is produced mainly by the liver under growth hormone stimulation. A separate variant, IGF-1Ec in humans, is expressed locally in mechanically stressed or damaged tissue and carries a unique C-terminal E-domain not present in the systemic isoform. That E-domain peptide is what is sold as MGF. It was first characterized by Yang and Goldspink in the 1990s.

Mechanism as Understood in the Literature

The commonly cited finding is that the E-domain peptide appears to act on muscle satellite cells through an interaction not blocked by IGF-1 receptor antibodies, which has been taken to suggest a distinct receptor or co-receptor. No such receptor has been identified, and the proposal remains speculative. Reviews have also noted that the additional proteolytic step required to release a standalone 24-residue human peptide has not been observed. Independent groups have failed to reproduce reported effects of the synthetic peptide on myoblast proliferation, differentiation, and ERK activation.

Research Status

Preclinical only, and contested. Cell culture and animal work has examined satellite cell activation and muscle repair, but key findings have not been independently replicated. No human pharmacokinetic, pharmacodynamic, or clinical data exists for the peptide as sold. Claims about a very short serum half-life are widely repeated but should not be treated as established for the specific synthetic peptide without a direct validated pharmacokinetic study.

Regulatory status

Not FDA-approved for any indication. Prohibited in competitive sport under World Anti-Doping Agency rules.

Commonly Confused With

Three different things get called MGF and should be kept apart: the IGF-1Ec messenger RNA and propeptide, the full-length splice-variant products, and the synthetic 24-residue E-domain peptide that vendors actually sell. Only the third is what is in the vial. Also not the same as IGF-1, and distinct from IGF-1 LR3, which is a modified version of the mature hormone rather than a splice-variant fragment. Nomenclature in the literature is inconsistent, with the same designation appearing as MGF, IGF-1Ec, and IGF-1Eb depending on species and source.

How This Compound Is Marketed

Vendor marketing for this compound typically references muscle repair, satellite cell activation, and recovery. VialReport does not evaluate or endorse these claims. See Research Status above for what the published literature actually establishes.

Analytical Profile

The human E-domain peptide is 24 amino acids. Distinguished by mass from IGF-1 and from IGF-1 LR3, both of which are far larger. Because nomenclature varies, a vial labeled MGF should be verified against a reference standard for the specific sequence rather than assumed.

Stability and Handling

Supplied lyophilized. Stability depends on molecular form, formulation, moisture, container closure, temperature, and reconstitution conditions, and published data may not apply to research-channel material.

Key Literature

  1. 01 Yang SY, Goldspink G. Different roles of the IGF-I Ec peptide (MGF) and mature IGF-I in myoblast proliferation and differentiation. FEBS Lett. 2002;522(1-3):156-160.
  2. 02 Goldspink G. Mechanical signals, IGF-I gene splicing, and muscle adaptation. Physiology. 2005;20:232-238.

VialReport publishes factual reference information and independent test data. Nothing here is medical, dosing, or purchasing advice.

Published reports

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