PEG-MGF
A PEGylated IGF-1 splice-variant peptide studied in preclinical cellular and skeletal-muscle research models.
Quick answers
What is PEG-MGF?
PEG-MGF is a PEGylated synthetic peptide (IGF-1 splice-variant E-domain, 24 residues) with a molecular weight of ~2.7 kDa (unPEGylated peptide portion; approximate).
How much published research cites PEG-MGF?
The Luvaminos PEG-MGF record cites 29 published references, dated 1996 to 2023. Each is listed on this page with a link to its source.
Does Luvaminos test PEG-MGF, and where is the certificate?
Luvaminos does not currently stock PEG-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 PEG-MGF carry?
PEG-MGF: Covalent polyethylene-glycol conjugation of the 24-residue MGF E-peptide, intended to slow proteolysis and renal filtration of the small peptide; the PEG chain size, linker, and attachment site are not defined in primary sources. The unmodified peptide is the C-terminal E-domain of the IGF-1Ec splice variant (IGF-1Eb in rodents).
How is PEG-MGF powder stored?
Sealed PEG-MGF powder: -20°C; lyophilized powder typically stable months when kept desiccated and protected from light. Protect from light; keep sealed and dry.
How is PEG-MGF different from MGF?
PEG-MGF and MGF are different compounds: PEG-MGF has 24 amino acids and a molecular weight of ~2.7 kDa (unPEGylated peptide portion; approximate); MGF has 24 amino acids, a molecular weight of ~2,868 g/mol and formula C121H199N41O40. MGF: The synthetic research peptide corresponds to the free-acid 24-residue E-domain.
Molecular Profile
- Type
- PEGylated synthetic peptide (IGF-1 splice-variant E-domain, 24 residues)
- Molecular weight
- ~2.7 kDa (unPEGylated peptide portion; approximate)
- Amino acids
- 24
- Sequence
- YQPPSTNKNTKSQRRKGSTFEEHK
- Modification
- Covalent polyethylene-glycol conjugation of the 24-residue MGF E-peptide, intended to slow proteolysis and renal filtration of the small peptide; the PEG chain size, linker, and attachment site are not defined in primary sources. The unmodified peptide is the C-terminal E-domain of the IGF-1Ec splice variant (IGF-1Eb in rodents). Two sequence variants circulate: a synthetic analog ending …FEE-His-Lys (shown above) and the native human E-domain ending …FEE-Arg-Lys.
Mechanism & Target Class
MGF is generated by alternative splicing of the IGF-1 gene: a reading-frame shift in the E-domain-encoding exon produces a unique C-terminal E-peptide that is absent from the more abundant IGF-1Ea isoform. The mature IGF-1 region is identical across the isoforms; the isolated 24-residue E-domain peptide is the entity synthesized as MGF, and PEG-MGF is that peptide conjugated to polyethylene glycol. A defining structural feature of the isolated E-peptide is that it lacks the mature IGF-1 region present in full-length constructs: in receptor-activation bioassays the isolated 24-residue peptide produces no detectable receptor-kinase activation, in contrast to full-length constructs that retain the mature IGF-1 region. This structural distinction is the basis of the long-standing and still-contested characterization of the isolated peptide as a molecule separate from mature IGF-1. The structural rationale offered for PEGylation is that the small (~2.7 kDa) peptide is otherwise rapidly filtered and proteolyzed.
Storage & Handling
- Lyophilized
- -20°C; lyophilized powder typically stable months when kept desiccated and protected from light.
- Handling
- Small water-soluble peptide; protect from light; keep sealed and dry.
Primary Database
References (29)
Reviews
1Zabłocka B, Goldspink PH, Goldspink G, Górecki DC. (2012). Front Endocrinol (Lausanne)
- 2
Matheny RW Jr, Nindl BC, Adamo ML. (2010). Endocrinology
- 3
Velloso CP, Harridge SDR. (2010). Scand J Med Sci Sports
- 4
Goldspink G. (2005). Int J Biochem Cell Biol
- 5
Goldspink G. (2005). Physiology (Bethesda)
- 6
Hill M, Wernig A, Goldspink G. (2003). J Anat
Clinical
7Philippou A, et al. (2009). In Vivo
- 8
Hameed M, et al. (2004). J Physiol
- 9
Hameed M, et al. (2003). J Physiol
Primary research
10medRxiv preprint. (2023). medRxiv
- 11
Mol Brain primary study. (2017). Mol Brain
- 12
Janssen JAMJL, et al. (2016). PLoS One
- 13
Fornaro M, et al. (2014). Am J Physiol Endocrinol Metab
- 14
Schlegel W, Raimann A, Halbauer D, et al. (2013). PLoS One
- 15
Mavrommatis E, Shioura KM, Los T, Goldspink PH. (2013). Mol Cell Biochem
- 16
Kravchenko IV, Furalyov VA, Popov VO. (2012). Mol Cell Biochem
- 17
Esposito S, Deventer K, Van Eenoo P. (2012). Rapid Commun Mass Spectrom
- 18
Kandalla PK, Goldspink G, Butler-Browne G, Mouly V. (2011). Mech Ageing Dev
- 19
Deng M, et al. (2011). Int Orthop
- 20
Stavropoulou A, et al. (2009). Mol Med
- 21
Carpenter V, et al. (2008). Heart Lung Circ
- 22
Mills P, Dominique JC, Lafrenière JF, Bouchentouf M, Tremblay JP. (2007). Am J Transplant
- 23
Ates K, et al. (2007). FEBS Lett
- 24
Dłużniewska J, et al. (2005). FASEB J
- 25
Cheema U, Brown R, Mudera V, Yang SY, McGrouther G, Goldspink G. (2005). J Cell Physiol
- 26
Hill M, Goldspink G. (2003). J Physiol
- 27
Yang SY, Goldspink G. (2002). FEBS Lett
- 28
McKoy G, et al. (1999). J Physiol
- 29
Yang S, Alnaqeeb M, Simpson H, Goldspink G. (1996). J Muscle Res Cell Motil
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