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Free U.S. shipping on orders over $150MGF (IGF-1 Ec) is a specialized form of IGF-1 released after exercise or muscle strain to jump-start the body’s repair process.
It helps activate muscle stem cells, supports recovery, and promotes healthy tissue rebuilding. Research also shows MGF may aid nerve protection and balanced immune responses, making it a key peptide for repair and resilience.
Mechano-growth factor (MGF), also known as IGF-1 Ec, MGF-E, and MGF Ec, is a 24-amino acid splice variant of the insulin-like growth factor-1 (IGF-1) gene that is uniquely expressed in response to mechanical loading, tissue strain, and muscular microdamage [1].
While classical IGF-1 isoforms (such as IGF-1 Ea, the most ubiquitous form) participate in endocrine and paracrine signaling related to growth, metabolism, and recovery, MGF represents a specialized version with distinct biological roles.
The key difference lies in its E-domain sequence, which alters receptor binding dynamics and shifts its function toward local tissue repair rather than systemic growth signaling.
Native IGF-1 promotes pathways like PI3K/Akt and mTOR, while MGF is believed to stimulate satellite cell activation, promoting local cellular proliferation and preparing damaged fibers for subsequent IGF-1–mediated differentiation [2].
Because of its rapid, short-lived expression following mechanical stress, endogenous MGF acts as the body’s immediate “alert” peptide for muscle and connective-tissue adaptation.
MGF (IGF-1 Ec) is most recognized for its involvement in the early stages of muscle repair, where it acts as a rapid-response signal following mechanical strain or localized microdamage.
Unlike systemic IGF-1 isoforms that are involved in sustained anabolic activity, MGF initiates the activation and proliferation of satellite cells, the stem-like cells responsible for muscle regeneration.
An in vitro study used primary human muscle cell cultures from donors of different ages (neonatal, young adult, old adult) to investigate the effects of MGF (IGF-1 Ec) on muscle regeneration pathways [3].
MGF (IGF-1 Ec) administration resulted in:
The peptide substantially enhanced satellite cell activation, proliferation, and fusion, supporting improved muscle repair and maintenance.
Because its effects are strongest in neonatal and young adult muscle, MGF (IGF-1 Ec) may represent a promising therapeutic strategy for preventing age-related sarcopenia.
Beyond its well-established role in muscular adaptation, MGF (IGF-1 Ec) has been investigated for its influence on neural resilience and regenerative signaling within the central and peripheral nervous systems.
A preclinical in vivo/in vitro model of neuronal ischemia evaluated neuroprotective mechanisms of MGF (IGF-1 Ec) [4]. Results showed:
The MGF (IGF-1 Ec) peptide demonstrates potent, sustained neuroprotective effects in both in vivo and in vitro ischemia models. Its ability to act independently of the IGF-1 receptor makes this peptide a promising therapeutic candidate for stroke recovery.
MGF (IGF-1 Ec) also plays a meaningful role in coordinating immune activity, especially in environments where mechanical stress or localized injury triggers an inflammatory response.
Because MGF is rapidly upregulated in damaged tissue, it acts as an early signaling cue that helps transition the microenvironment from acute inflammation toward controlled regeneration.
An animal study investigated whether exogenous MGF can rescue impaired muscle regeneration in a mouse model of skeletal muscle contusion combined with macrophage depletion [5].
Mice underwent muscle contusion injury followed by macrophage depletion to model impaired regenerative conditions. After the injection of injured muscles with synthetic MGF (IGF-1 Ec), results showed:
Although MGF did not directly enhance muscle fiber regeneration lost due to macrophage depletion, it improved the detrimental effects of macrophage loss by modulating inflammation.
1 Schlegel, W., Raimann, A., Halbauer, D., Scharmer, D., Sagmeister, S., Wessner, B., et al. (2013) Insulin-like growth factor I (IGF-1) Ec/Mechano Growth factor--a splice variant of IGF-1 within the growth plate. PLoS One, Public Library of Science (PLoS) 8, e76133
2 Dai, Z., Wu, F., Yeung, E. W. and Li, Y. (2010) IGF-IEc expression, regulation and biological function in different tissues. Growth Horm. IGF Res., Elsevier BV 20, 275–281
3 Kandalla, P. K., Goldspink, G., Butler-Browne, G. and Mouly, V. (2011) Mechano Growth Factor E peptide (MGF-E), derived from an isoform of IGF-1, activates human muscle progenitor cells and induces an increase in their fusion potential at different ages. Mech. Ageing Dev. 132, 154–162
4 Dluzniewska, J., Sarnowska, A., Beresewicz, M., Johnson, I., Srai, S. K. S., Ramesh, B., et al. (2005) A strong neuroprotective effect of the autonomous C-terminal peptide of IGF-1 Ec (MGF) in brain ischemia. FASEB J., Wiley 19, 1896–1898
5 Liu, X., Zeng, Z., Zhao, L., Chen, P. and Xiao, W. (2019) Impaired skeletal muscle regeneration induced by macrophage depletion could be partly ameliorated by MGF injection. Front. Physiol., Frontiers Media SA 10, 601
Research Use Only. All findings described above are derived from preclinical studies (animal models and in vitro experiments). MGF IGF-Ec is not approved by the FDA for any diagnostic or therapeutic use in humans. Genesis Peptides makes no claims regarding human clinical efficacy. This product is sold exclusively for laboratory research.
Every lot undergoes six independent assays before release. Results are published in the lot-specific Certificate of Analysis.
Mechano growth factor (MGF) is described as a growth factor produced specifically following mechanical stimulus. MGF is an isoform of insulin-like growth factor 1 (IGF-1) and is recognized as a typical mechanically sensitive growth factor. In the heart, alternative splicing of the igf-I gene produces two isoforms, IGF-IEa and IGF-IEc, with IGF-IEc also called Mechano-growth factor (MGF).
IGF-1Ec shares the same mature IGF-1 sequence as the other proIGF-1 isoforms, which is responsible for IGF-1 receptor binding, but differs in its carboxy-terminal Ec-peptide extension. IGF-1Ec is one of three prohormone isoforms (proIGF-1s) that the IGF-1 gene may produce through alternative splicing, alongside IGF-1Ea and IGF-1Eb. In the heart, alternative splicing of the igf-I gene produces two isoforms, IGF-IEa and IGF-IEc, with MGF being the name for the Ec form.
In the study, IGF-1Ec shares the same mature IGF-1 sequence with the other proIGF-1 isoforms, IGF-1Ea and IGF-1Eb. This shared mature IGF-1 sequence is responsible for binding to the IGF-1 receptor. IGF-1Ec differs from IGF-1Ea and IGF-1Eb in its carboxy-terminal Ec-peptide extension. IGF-1Ec is one of three prohormone isoforms (proIGF-1s) that the IGF-1 gene may produce through alternative splicing, alongside IGF-1Ea and IGF-1Eb.
In a human clinical study, IGF-1Ec (mechano growth factor) expression was evaluated in deeply infiltrating endometriotic lesions, ovarian endometriomas, and eutopic endometrium of endometriosis patients, and compared with eutopic endometrium of women without endometriosis. The study observed a tendency toward lower IGF-1Ec expression in endometriomas without deeply infiltrating endometriosis (DIE) compared with endometriomas with concurrent DIE or with DIE nodules. The authors concluded that differential expression of IGF-1 isoforms may indicate that DIE with its associated ovarian lesions and simple ovarian endometriosis should be considered two forms of the disease developing under different molecular pathways.
Detection of this class of peptides, which includes IGF-1 and mechano growth factor, is difficult because of absorptive losses and very low concentrations in urine. In one in vitro study, peptides of the IGF-1 and mechano growth factor class were detected in urine samples after ultrafiltration to concentrate the urine, followed by solid phase extraction in a 96-well micro-elution plate. The extracted peptides were then detected on a triple quadrupole mass spectrometer coupled to standard flow liquid chromatography. In that study, the method's limit of detection for peptide classes other than insulin analogues, which include IGF-1 and mechano growth factor, was between 5 and 50 pg/ml.
In a rat study, the MGF E peptide reduced the progression of MIA-induced osteoarthritis. The peptide was reported to retard cartilage degeneration, upregulate type II collagen synthesis, and improve extracellular matrix distribution after 4 or 6 weeks.
In a rabbit partial ACL transection model, the ACL showed poor regenerative capacity in collagen and extracellular matrix synthesis after partial transection for 2 or 4 weeks. In that rabbit study, MGF remarkably accelerated ACL regeneration and restored the ligament's mechanical loading capacity after partial transection for four weeks.
In cultured periodontal ligament stem cells (PDLSCs), MGF promoted proliferation and fibrogenic differentiation by inducing Fyn-YAP Y357 phosphorylation, but not LATS1-YAP S127 phosphorylation. In these in vitro experiments, Fyn did not activate YAP directly; it activated YAP through RhoA in response to MGF stimulation. The study reported that the Fyn-RhoA-p-YAPY357 pathway is significant in facilitating MGF-induced proliferation and fibrogenic differentiation of PDLSCs.
In cultured ACL fibroblasts exposed to injurious stretch, MGF improved the expression of cell mobility-relevant molecules, especially ROCK1, at 0 or 24 hours after the injury. ROCK1 protein expression in injured ACL fibroblasts was reduced, and MGF treatment recovered it.
An anti-PEc monoclonal antibody (MAb) was developed targeting the PEc peptide of IGF-1Ec. In SCID mice with prostate cancer tumours, anti-PEc MAb treatment was associated with a significant decrease in tumour size and metastases rate by reversing the tumours' mesenchymal phenotype. In cultured cells, the anti-PEc MAb effects were associated with downregulation of pERK1/2 and vimentin and upregulation of E-Cadherin.
The source groups mechano growth factor (MGF) with the large peptides, which it describes as including analogues of growth hormone releasing hormone, insulin-like growth factor-1 (IGF-1), and MGF. The same source states that IGF-1 analogues are among the large peptides that athletes may use to enhance performance and that are banned by WADA. A separate review lists pegylated mechano growth factor (PEG-MGF) among IGF-1 analogues most commonly encountered in clinical practice and online self-administration protocols.
MGF IGF-Ec, also called mechano growth factor, has been used in two studies to modify tissue engineering scaffolds. In one study, the short peptide MGF was decorated via click chemistry onto silk fibroin layers that had been assembled on an electrospun polycaprolactone fibrous scaffold. The stated goal of that polycaprolactone work was to direct the macrophage phenotype transition and aim to reduce the foreign body response. In a separate study, MGF was loaded as cargo onto a porous titanium alloy scaffold whose two-layer coating of carbon nanotubes and mesoporous silica nanoparticles served as its carrier.
FOR RESEARCH USE ONLY — Products are sold exclusively for in vitro and preclinical laboratory research. Not for human consumption or administration. Not intended for diagnostic or therapeutic use. These statements have not been evaluated by the FDA.