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MGF without PEG 2mg

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Mechano Growth Factor (MGF) is the alternative splice variant of the insulin-like growth factor 1 (IGF-1) gene, also designated IGF-1Ec, distinguished from the systemic IGF-1Ea isoform by a distinct C-terminal E-domain peptide sequence. Research interest centers on its proposed role in activating satellite cell proliferation in skeletal muscle tissue following mechanical loading, distinct from the growth-promoting signalling of mature IGF-1. Research applications include satellite cell activation pathway studies, IGF-1 splice variant comparative research, and muscle tissue mechanotransduction investigation.

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All SwissChems products are independently third-party tested at a USA-based HPLC-licensed laboratory prior to distribution. Certificates of Analysis (COA) are published on the Independent Test Results page and available at product level. If any independently conducted HPLC test returns a negative result, SwissChems will refund: (1) the cost of the HPLC test, and (2) the full order amount including shipping.
Chemical Formula C121H200N42O39
Synonyms MGF, IGF-1Ec
Molar Mass 2,644.85 g/mol
CAS Number 1565841-06-6
Total Compound Content 2mg per vial
Shelf Life 36 months
MGF is produced via alternative splicing of the IGF-1 gene specifically in response to mechanical loading or damage in skeletal muscle tissue, generating a peptide with a distinct C-terminal E-domain not present in the systemically circulating mature IGF-1 (IGF-1Ea) isoform. Research models investigate MGF's reported capacity to activate quiescent satellite cells (muscle-resident stem cells) and promote their entry into the cell cycle, a function studied as distinct from and potentially complementary to mature IGF-1's role in promoting differentiated myoblast protein synthesis via the PI3K/Akt/mTOR pathway. The unmodified (non-PEGylated) form is used in research protocols requiring native peptide pharmacokinetics rather than the extended half-life conferred by PEGylation. Independently third-party HPLC-tested; COA available per batch.

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How does MGF (IGF-1Ec) functionally differ from mature IGF-1 (IGF-1Ea) in muscle tissue research models?

Both are products of the same IGF-1 gene but result from alternative splicing, producing distinct C-terminal E-domain peptide sequences with reportedly distinct biological roles. Mature IGF-1 (IGF-1Ea) primarily promotes protein synthesis and hypertrophy in already-differentiated myoblasts via PI3K/Akt/mTOR signalling. MGF (IGF-1Ec) is studied for a proposed earlier-stage role: activating quiescent satellite cells to re-enter the cell cycle and begin proliferating, a necessary precursor step before these cells can differentiate and contribute to muscle fiber repair or growth. Research distinguishing these roles typically uses satellite cell proliferation assays (Ki-67, BrdU incorporation) for MGF versus protein synthesis assays (puromycin incorporation, mTOR pathway activation) for mature IGF-1.

What is the significance of using non-PEGylated MGF in pharmacokinetic and mechanistic research?

PEGylation (covalent attachment of polyethylene glycol chains) is a common modification used to extend a peptide's circulating half-life by reducing renal clearance and proteolytic degradation. Non-PEGylated MGF reflects the native peptide's pharmacokinetic profile, which is relevant for research questions about the compound's natural biological half-life and clearance mechanisms, or where the larger PEG moiety might sterically interfere with receptor binding or cellular uptake in a specific experimental model. Researchers should select PEGylated or non-PEGylated formats based on whether their study question concerns native peptide kinetics or extended-exposure pharmacology.

What experimental models are used to study MGF's proposed satellite cell activation mechanism?

Isolated satellite cell cultures (from skeletal muscle biopsy or whole-muscle explant) and ex vivo muscle fiber preparations are standard models for studying MGF's effects on satellite cell quiescence exit and proliferation, typically using cell-cycle markers (Ki-67, PCNA) and proliferation assays (BrdU or EdU incorporation) as primary readouts. Mechanical loading or injury models (such as eccentric contraction protocols in ex vivo muscle preparations) are sometimes used to study endogenous MGF splice variant induction alongside exogenous MGF administration, allowing comparison of native versus exogenous peptide effects on the same satellite cell population.

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