MGF
A mechanically induced IGF-1 splice-variant peptide studied in preclinical muscle and cellular research models.
Quick answers
What is MGF?
MGF is a synthetic peptide (IGF-1Ec C-terminal E-domain, 24 residues) with a molecular weight of ~2,868 g/mol and the formula C121H199N41O40.
How much published research cites MGF?
The Luvaminos MGF record cites 25 published references, dated 1996 to 2022. Each is listed on this page with a link to its source.
Does Luvaminos test MGF, and where is the certificate?
Luvaminos does not currently stock MGF. Every peptide lot Luvaminos sells is tested by Freedom Diagnostics Testing, PLLC, an independent laboratory, and its certificate is published at luvaminos.com/coa under the lot number printed on the vial.
What modifications does MGF carry?
MGF: The synthetic research peptide corresponds to the free-acid 24-residue E-domain.
How is MGF powder stored?
Sealed MGF powder: -20°C (colder for long-term); keep desiccated and frozen until use. Minimize freeze-thaw cycles; protect from light.
How is MGF different from PEG-MGF?
MGF and PEG-MGF are different compounds: MGF has 24 amino acids, a molecular weight of ~2,868 g/mol and formula C121H199N41O40; PEG-MGF has 24 amino acids and a molecular weight of ~2.7 kDa (unPEGylated peptide portion; approximate). MGF: The synthetic research peptide corresponds to the free-acid 24-residue E-domain.
Molecular Profile
- Type
- Synthetic peptide (IGF-1Ec C-terminal E-domain, 24 residues)
- Molecular formula
- C121H199N41O40
- Molecular weight
- ~2,868 g/mol
- Amino acids
- 24
- Sequence
- YQPPSTNKNTKSQRRKGSTFEEHK
- Modification
- The synthetic research peptide corresponds to the free-acid 24-residue E-domain; stabilized analogs substitute D-arginine in the central basic (QRRK) region and amidate the C-terminus to slow proteolysis, and PEGylated forms (PEG-MGF) couple a polyethylene glycol chain to extend circulating half-life.
Mechanism & Target Class
MGF is a synthetic peptide corresponding to the unique C-terminal E-domain of a mechanically inducible IGF-1 splice isoform, a structure generated when inclusion of a short exon-5 insert shifts the reading frame in exon 6 to produce a 24-residue sequence distinct from the predominant systemic isoform. A central, unresolved structural question in the literature is which receptor, if any, this E-domain peptide engages; no dedicated E-peptide binding partner has been definitively identified. The peptide's arginine/lysine-rich polybasic motif has been studied as a potential cell-penetrating and nuclear-localization element, and specific protein interactions (e.g., with 14-3-3 proteins in cardiac cell models) have been characterized.
Storage & Handling
- Lyophilized
- -20°C (colder for long-term); keep desiccated and frozen until use.
- Handling
- Minimize freeze-thaw cycles; protect from light.
Primary Database
References (25)
Reviews
1Vassilakos G, et al. (2014). Hormones (Athens)
- 2
Brisson BK, Barton ER. (2013). Frontiers in Endocrinology
- 3
Matheny RW Jr, Nindl BC, Adamo ML. (2010). Endocrinology
- 4
Goldspink G. (2005). Physiology (Bethesda)
Clinical
5Hameed M, et al. (2004). Journal of Physiology
- 6
Hameed M, et al. (2003). Journal of Physiology
Primary research
7Solís C, et al. (2022). Frontiers in Physiology
- 8
Armakolas A, et al. (2015). Molecular Medicine
- 9
Fornaro M, et al. (2014). American Journal of Physiology-Endocrinology and Metabolism
- 10
Mavrommatis E, Shioura KM, Los T, Goldspink PH. (2013). Molecular and Cellular Biochemistry
- 11
Schlegel W, et al. (2013). PLOS ONE
- 12
Brisson BK, Barton ER. (2012). PLOS ONE
- 13
Deng M, et al. (2011). International Orthopaedics
- 14
Kandalla PK, Goldspink G, Butler-Browne G, Mouly V. (2011). Mechanisms of Ageing and Development
- 15
Armakolas A, et al. (2010). The Prostate
- 16
Stavropoulou A, et al. (2009). Molecular Medicine
- 17
Riddoch-Contreras J, et al. (2009). Experimental Neurology
- 18
Philippou A, et al. (2008). In Vivo
- 19
Carpenter V, et al. (2008). Heart, Lung and Circulation
- 20
Ates K, et al. (2007). FEBS Letters
- 21
Dłużniewska J, et al. (2005). FASEB Journal
- 22
Aperghis M, et al. (2004). Brain Research
- 23
Yang SY, Goldspink G. (2002). FEBS Letters
- 24
McKoy G, et al. (1999). Journal of Physiology
- 25
Yang S, Alnaqeeb M, Simpson H, Goldspink G. (1996). Journal of Muscle Research and Cell Motility
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