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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.
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.
Lyophilized
20°C
lyophilized powder typically stable months when kept desiccated and protected from light.
Small water-soluble peptide; protect from light; keep sealed and dry.
Reviews
Zabłocka B, Goldspink PH, Goldspink G, Górecki DC. (2012). Front Endocrinol (Lausanne)
Matheny RW Jr, Nindl BC, Adamo ML. (2010). Endocrinology
Reviews
Velloso CP, Harridge SDR. (2010). Scand J Med Sci Sports
Goldspink G. (2005). Int J Biochem Cell Biol
Goldspink G. (2005). Physiology (Bethesda)
Hill M, Wernig A, Goldspink G. (2003). J Anat
Clinical
Philippou A, et al. (2009). In Vivo
Hameed M, et al. (2004). J Physiol
Hameed M, et al. (2003). J Physiol
Primary research
medRxiv preprint. (2023). medRxiv
Mol Brain primary study. (2017). Mol Brain
Janssen JAMJL, et al. (2016). PLoS One
Fornaro M, et al. (2014). Am J Physiol Endocrinol Metab
Schlegel W, Raimann A, Halbauer D, et al. (2013). PLoS One
Mavrommatis E, Shioura KM, Los T, Goldspink PH. (2013). Mol Cell Biochem
Kravchenko IV, Furalyov VA, Popov VO. (2012). Mol Cell Biochem
Esposito S, Deventer K, Van Eenoo P. (2012). Rapid Commun Mass Spectrom
Kandalla PK, Goldspink G, Butler-Browne G, Mouly V. (2011). Mech Ageing Dev
Deng M, et al. (2011). Int Orthop
Stavropoulou A, et al. (2009). Mol Med
Carpenter V, et al. (2008). Heart Lung Circ
Mills P, Dominique JC, Lafrenière JF, Bouchentouf M, Tremblay JP. (2007). Am J Transplant
Ates K, et al. (2007). FEBS Lett
Dłużniewska J, et al. (2005). FASEB J
Cheema U, Brown R, Mudera V, Yang SY, McGrouther G, Goldspink G. (2005). J Cell Physiol
Hill M, Goldspink G. (2003). J Physiol
Yang SY, Goldspink G. (2002). FEBS Lett
McKoy G, et al. (1999). J Physiol
Yang S, Alnaqeeb M, Simpson H, Goldspink G. (1996). J Muscle Res Cell Motil
Also known as: Mechano Growth Factor (PEGylated), MGF E-peptide (PEGylated)
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