IGF-1 Splice Variant Peptide / PEGylated Growth Factor Fragment
PEG-MGF (Pegylated Mechano Growth Factor) Research Peptide
PEG-MGF is a pegylated (polyethylene glycol-conjugated) synthetic analog of the E-domain peptide of Mechano Growth Factor (MGF), a splice variant of the insulin-like growth factor 1 (IGF-1) gene. PEGylation extends the in-vivo stability of the MGF E-peptide — which is highly susceptible to enzymatic degradation in its native form — and has been used in preclinical research to investigate the biological roles of the MGF E-domain beyond the IGF-1 receptor (IGF-1R)-mediated signaling common to all IGF-1 isoforms.
Compound identity
- Name
- PEG-MGF
- Class
- IGF-1 Splice Variant Peptide / PEGylated Growth Factor Fragment
- CAS number
- 387380-41-0
- Molecular formula
- C₁₃₀H₂₁₄N₄₀O₃₄ (E-peptide core; PEG conjugate MW varies by PEG chain)
- Also known as
- Pegylated Mechano Growth Factor, PEGylated MGF, MGF E-peptide PEG
- Sequence
- Tyr-Gln-Pro-Pro-Ser-Thr-Asn-Lys-Asn-Thr-Lys-Ser-Gln-Arg-Arg-Lys-Gly-Ser-Thr-Phe-Glu-Glu-Arg-Lys (24 aa MGF E-domain; MW ~2867 Da core peptide, +PEG2000–PEG5000 for the conjugated form)
Research context
The IGF-1 gene undergoes tissue- and stimulus-specific alternative splicing to produce multiple isoforms distinguished primarily by their C-terminal E-domain sequences. In response to mechanical strain, stretch, or damage — particularly in skeletal muscle — local transcription generates a splice variant designated Mechano Growth Factor (MGF), characterized by a unique 49-nucleotide insert in the E-domain that shifts the reading frame and produces a distinct 24-amino acid C-terminal E-peptide. The MGF E-peptide (CAS 387380-41-0, MW ~2867 Da) is biochemically and functionally separable from the mature IGF-1 domain; research by Goldspink et al., Yang, and colleagues at University College London proposed that the E-peptide has biological activity distinct from IGF-1R activation, potentially involving cell proliferation via a yet-to-be-fully-characterized receptor or co-receptor pathway.
A critical limitation of native MGF E-peptide in research is its rapid enzymatic degradation — a very short plasma half-life measured in minutes. PEGylation (conjugation of polyethylene glycol chains, typically PEG2000–5000, to lysine residues or the N-terminus) substantially increases stability and circulating half-life, enabling once-daily or less frequent dosing in preclinical research protocols. Research using PEG-MGF in rodent models has examined satellite cell activation (muscle stem cells responsible for muscle repair and hypertrophy), myoblast proliferation, and tissue repair after mechanical injury. Studies have sought to dissect the relative contributions of the IGF-1 domain versus the MGF E-peptide to the observed effects of local IGF-1 splice variants. Yang et al. (Journal of Anatomy, multiple publications 2003–2012) and related groups have used PEG-MGF to examine these questions.
As a research reagent, PEG-MGF is used in muscle satellite cell biology, IGF-1 splice variant research, muscle repair and hypertrophy preclinical models, and studies of E-domain-specific signaling distinct from canonical IGF-1R activation. DMV Research supplies PEG-MGF as a lyophilized compound with per-batch Certificate of Analysis confirming identity by mass spectrometry and purity ≥99% by HPLC.
Frequently asked questions
What is PEG-MGF?+
PEG-MGF is the pegylated (polyethylene glycol-conjugated) form of the E-domain peptide of Mechano Growth Factor (MGF), a splice variant of the IGF-1 gene expressed locally in skeletal muscle in response to mechanical loading or damage. PEGylation extends the peptide's half-life (native MGF E-peptide degrades in minutes) to enable preclinical research studies of MGF E-domain biology. The E-domain peptide is 24 amino acids and is distinct from the mature IGF-1 receptor-binding domain shared by all IGF-1 isoforms.
How does PEG-MGF differ from IGF-1 LR3 and regular IGF-1?+
Native IGF-1 and IGF-1 LR3 both act primarily through the IGF-1 receptor (IGF-1R) via the conserved IGF-1 domain. MGF arises from a different splice pattern of the IGF-1 gene, generating a unique C-terminal E-peptide (24 aa) alongside the shared IGF-1 domain. Research has proposed that the MGF E-peptide has distinct biological activities beyond IGF-1R signaling — including proposed effects on satellite cell activation and proliferation. PEG-MGF supplies only the E-domain peptide (not the IGF-1 domain), conjugated to PEG for stability, making it a tool for isolating E-domain-specific biology from IGF-1R-mediated effects. IGF-1 LR3 is an analog of the mature IGF-1 domain with reduced IGFBP binding; PEG-MGF is a stabilized fragment of the distinct E-domain.
What does 'PEGylation' mean for MGF?+
PEGylation is the covalent attachment of polyethylene glycol (PEG) chains to a peptide or protein. For MGF, which is rapidly degraded by enzymes in plasma and tissue (half-life measured in minutes), PEGylation confers steric protection against proteolysis and significantly extends circulating half-life. PEG2000–PEG5000 conjugates are commonly used in PEG-MGF research preparations. The PEG chain also increases molecular weight and hydrodynamic radius, reducing renal filtration. This allows PEG-MGF to be used in once-daily (or less frequent) dosing protocols in preclinical animal research where native MGF E-peptide would require continuous infusion.
Is PEG-MGF approved for human use?+
No. PEG-MGF is not FDA-approved or approved by any regulatory body for human use. As supplied by DMV Research, it is a research peptide for in-vitro and pre-clinical laboratory research purposes only. Not for human consumption.
Research use only
All products are intended for laboratory and research use only (RUO) and are not for human consumption, ingestion, or any in-vivo use.
The statements on this page have not been evaluated by the FDA. PEG-MGF is not intended to diagnose, treat, cure, or prevent any disease. Content is provided for laboratory research reference only.