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Emerging Research

MGF (Mechano Growth Factor)

Tissue Repair & Recovery · ['Mechano Growth Factor', 'IGF-1Ec', 'IGF-1 splice variant']

A splice variant of insulin-like growth factor 1 expressed in mechanically stressed and damaged muscle, whose unique C-terminal E-domain peptide is studied for roles in satellite-cell activation and early tissue-repair signaling.

🔬 Research use only — not for human or veterinary use. K4 Elite does not provide dosing instructions.
Molecular Weight
~2867 Da (E-domain peptide) g/mol
Research Level
Emerging Research
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Mechano Growth Factor (MGF) is an alternatively spliced isoform of insulin-like growth factor 1, also designated IGF-1Ec. It is produced locally in skeletal muscle in response to mechanical loading and tissue damage. What distinguishes MGF from systemic IGF-1 is its distinct C-terminal E-domain, an inserted peptide sequence generated by the alternative splicing event.

Research interest centers on this E-domain peptide, which in experimental systems appears to act independently of the mature IGF-1 domain to influence muscle stem (satellite) cells. Many laboratory studies use a synthetic peptide corresponding to the unique MGF C-terminal region rather than the full-length protein.

MGF is handled exclusively as a research reagent for the study of muscle repair and growth-factor signaling.

The full-length MGF molecule contains a mature IGF-1 region capable of engaging the IGF-1 receptor, but its distinctive C-terminal E-domain peptide is reported to have separate biological activity. In cell-culture studies this peptide has been associated with activation and proliferation of muscle satellite cells, which are progenitors involved in muscle repair after mechanical stress.

The E-domain peptide's actions in experimental models appear not to require IGF-1R binding, and investigators have proposed distinct, as-yet incompletely defined receptor or signaling interactions to account for its effects on stem-cell recruitment.

  • Satellite (muscle stem) cell activation and proliferation after mechanical loading
  • Local versus systemic IGF-1 splicing in exercised and damaged muscle
  • Early-phase muscle tissue repair and regeneration signaling
  • Cardioprotective and neuroprotective signaling of the E-domain peptide in preclinical models
  • Structure-function studies of the MGF C-terminal peptide independent of the IGF-1 domain
📋 How published studies were conducted — a research reference summarizing study designs from the literature. This is not usage, dosing, or administration guidance. K4 Elite does not provide dosing instructions; determining any research protocol is the sole responsibility of the qualified researcher.

The following summarize published experimental studies for reporting purposes only and are not usage instructions.

Goldspink and Yang characterized MGF as a mechanically activated IGF-1 splice variant, reporting that its expression rises in muscle after resistance loading or damage and that the E-domain peptide stimulates satellite-cell proliferation in culture (Yang & Goldspink, 2002).

Preclinical cardiac studies have reported that administration of the MGF C-terminal peptide in animal models of myocardial injury was associated with markers of reduced cardiomyocyte loss; these findings are cited as research observations only.

Combinations examined in the research literature. Descriptive only — not a recommendation to combine compounds.

IGF-1Compatible
MGF is a splice variant of IGF-1; the two are studied together in muscle growth-factor biology.
IGF-1 receptorNeutral
The mature domain can bind IGF-1R, but the unique E-domain peptide is reported to act via distinct signaling in experimental models.
Follistatin-344Compatible
Both are studied in muscle hypertrophy and repair research and are sometimes referenced together.
MyostatinCaution
As a negative muscle regulator, myostatin is often examined as a counterpoint to growth-promoting factors like MGF in study design.

References are being compiled for this entry.

What is MGF?
Mechano Growth Factor is an alternatively spliced isoform of IGF-1 (IGF-1Ec) expressed in mechanically loaded and damaged muscle, notable for a unique C-terminal E-domain peptide studied in tissue-repair research.
How is MGF different from IGF-1?
MGF shares the mature IGF-1 domain but adds a distinct E-domain peptide from alternative splicing; this peptide is reported to act on muscle satellite cells through signaling separate from the IGF-1 receptor.
Does MGF have a PubChem CID?
The synthetic E-domain peptide and full protein are catalogued in protein/peptide databases rather than as a verified small-molecule PubChem compound, so no CID is listed here.
What is being researched?
Studies focus on satellite-cell activation, local IGF-1 splicing after exercise, early muscle repair signaling, and cardioprotective and neuroprotective actions of the E-domain peptide in preclinical models.
Is MGF intended for human or veterinary use?
No. MGF is offered for laboratory research use only. It is not a drug or supplement and is not intended to diagnose, treat, cure, or prevent any disease in humans or animals.
Disclaimer: This profile summarizes published preclinical and laboratory research for reference only. It is not medical advice and makes no claim of safety or efficacy in humans. Determining any research protocol is the sole responsibility of the qualified researcher. Products are sold strictly for in-vitro research and have not been evaluated by the FDA.