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PEG MGF Peptide for Laboratory Research
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≥ 99 % purity (HPLC)
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What is PEG MGF Peptide for Laboratory Research
PEG MGF Peptide for Laboratory Research at a glance
PEG-MGF is a PEGylated synthetic analogue of the C-terminal E-domain peptide associated with IGF-1Ec, the splice variant commonly called mechano growth factor. Published identity values for the native, non-PEGylated 24-residue peptide do not define the supplied PEG conjugate.
The material is offered strictly for laboratory research and is not for use in humans or animals. Product identity, PEG chemistry, content and purity require the matching specification, batch code and batch-specific COA.
Research overview
PEG MGF denotes an analogue in which polyethylene glycol is conjugated to an IGF-1Ec E-domain peptide construct. PEG-MGF is the same catalogue identity, while the precise sequence, terminus and conjugation site remain batch-specific. Native-peptide formulae, sequences and database records cannot fill those product-specific gaps.
Published evidence concerns native MGF, IGF-1Ec expression or synthetic E-domain peptides rather than the supplied PEGylated analogue. It spans cell cultures, tissue constructs, preclinical animal models, a human physiological protocol and reviews. Every observation remains limited to its named molecule, model, method and endpoint.
PEGylation is described as a stability-oriented design strategy, but that rationale does not establish equivalence to the native peptide, a particular persistence value or any experimental outcome. HPLC and MS results must be interpreted against the defined conjugate and method.
Research procurement should connect the exact sequence, terminus, PEG chemistry, total mass, salt form, label, batch code and analytical methods with the applicable COA. Any purity statement applies only to the corresponding tested batch.
Technical data
SummenformelC₁₂₁H₁₉₉N₄₁O₄₀
Molekulargewicht2868,2 g/mol
Amino acids24
Purity≥ 99 % (HPLC)
Target structureProliferation and differentiation endpoints for the native IGF-I Ec E-domain peptide compared with mature IGF-I in an in vitro myoblast model; migration endpoint for a synthetic MGF E-domain peptide in cultured human myogenic precursor cells; activation and fusion endpoints in human muscle progenitor-cell cultures; proliferation, differentiation and myogenic transcription-factor endpoints in porcine satellite-cell culture; IGF-I gene splicing and satellite-cell activation after local tissue damage in a preclinical rat model; mechanically regulated IGF-I splicing in cells and tissue constructs in vitro; endogenous IGF-I splice-variant expression in skeletal-muscle biopsies within a human physiological research protocol, with no reagent administered; neuronal-loss endpoints for a C-terminal IGF-1Ec peptide in a preclinical cerebral-ischaemia model; dopaminergic-neuron endpoints and haem oxygenase-1 induction in a preclinical model; proliferation, osteogenic differentiation and PI3K/AKT signalling in cultured rabbit mesenchymal cells; identity and analytical endpoints requiring product designation, sequence, terminus, PEG chemistry and attachment site to match the released specification and batch documentation, with strict separation of published native values from the supplied PEG conjugate, HPLC purity treated as a batch- and method-specific result, and MS required as complementary identity evidence
Molekülstruktur
✓In vitroAnimal model3Human pilot4RCT5Approval
Myoblast model
Human cell models
Preclinical models
Batch documentation
Evidence
Research highlights
An in vitro study reported different proliferation and differentiation endpoints for the IGF-I Ec E-domain peptide and mature IGF-I; the comparison does not concern PEG-MGF.
Yang et al. 2002 · PMID 12095637
Studies reported migration, activation and fusion endpoints in cultured human myogenic precursor or progenitor cells; these were cell models, not observations in people.
Mills et al. 2007 · PMID 17156777 · Kandalla et al. 2011 · PMID 21354439
Research reported model-specific endpoints for C-terminal IGF-1Ec peptides in cerebral-ischaemia and dopaminergic-neuron systems.
Dluzniewska et al. 2005 · PMID 16144956 · Quesada et al. 2009 · PMID 19735655
Product designation, sequence, PEG chemistry, batch code and analytical records must refer to the same material; purity applies only to the tested batch.
Reborn batch documentation · COA with HPLC and MS
Research status
Referenced studies on PEG MGF Peptide for Laboratory Research
14 selected sources — filterable by study type, each linked directly to its source.
In vitroProliferation and differentiation endpoints for an IGF-I Ec E-domain peptide in a myoblast modelYang et al., 2002, FEBS LettersSource →Animal studyIGF-I gene splicing and satellite-cell activation after local tissue damage in a preclinical rat modelHill et al., 2003, The Journal of PhysiologySource →In vitroProliferation, differentiation and myogenic transcription-factor endpoints in porcine satellite-cell cultureQin et al., 2012, Molecular and Cellular BiochemistrySource →In vitroMigration endpoint for a synthetic MGF E-domain peptide in cultured human myogenic precursor cellsMills et al., 2007, Experimental Cell ResearchSource →In vitroActivation and fusion endpoints in human muscle progenitor-cell culturesKandalla et al., 2011, Mechanisms of Ageing and DevelopmentSource →Animal studyProgenitor-cell quantification in normal and altered muscle-tissue modelsAtes et al., 2007, FEBS LettersSource →Human pilotEndogenous IGF-I splice-variant expression in skeletal-muscle biopsies within a physiological research protocolHameed et al., 2003, The Journal of PhysiologySource →In vitroMechanically regulated IGF-I splicing in cells and tissue constructsCheema et al., 2005, Journal of Cellular PhysiologySource →ReviewMechanical signalling and IGF-I gene splicingGoldspink et al., 2005, Physiology (Bethesda)Source →ReviewIGF-I splicing, MGF expression and altered muscle modelsGoldspink et al., 2006, The International Journal of Biochemistry and Cell BiologySource →Animal studyNeuronal-loss endpoints for a C-terminal IGF-1Ec peptide in a preclinical cerebral-ischaemia modelDluzniewska et al., 2005, The FASEB JournalSource →Animal studyDopaminergic-neuron endpoints and haem oxygenase-1 induction in a preclinical modelQuesada et al., 2009, Experimental NeurologySource →In vitroProliferation, osteogenic differentiation and PI3K/AKT signalling in cultured rabbit mesenchymal cellsTong et al., 2015, BMC BiochemistrySource →ReviewIGF-1Ec expression and regulation across tissue modelsDai et al., 2010, Growth Hormone and IGF ResearchSource →
Research Deep Dive
The research in depth
Model-qualified findings in depth — every claim tied to a PubMed-indexed source.
14 sourcesModel-qualified evidence map
~24 residuesNative peptide literature reference
IGF-1EcParent splice-variant context
Batch-specificCOA documentation
01PEG-MGF chemistry and molecular design
PEG-MGF is a PEGylated synthetic analogue of the C-terminal E-domain peptide associated with IGF-1Ec, commonly called mechano growth factor. Published identity values belong to native, non-PEGylated material and do not define the supplied conjugate.
| Field | Reference specification |
|---|---|
| Product designation | PEG-MGF; PEG MGF; PEGylated IGF-1Ec C-terminal E-domain peptide analogue |
| Parent context | Mechano growth factor = IGF-1Ec, a mechanically induced IGF-1 splice variant |
| Native peptide length | Approximately 24 residues; native, non-PEGylated literature reference, not product confirmation |
| Frequently cited native 24-mer sequence | YQPPSTNKNTKSQRRKGSTFEEHK; native, non-PEGylated literature reference |
| Alternative form | Ends in …FEERK; native, non-PEGylated literature/database form; neither form is designated uniquely correct |
| Native molecular formula | C121H199N41O40; PubChem reference for the native, non-PEGylated 24-mer |
| PubChem CID | 175675731; native, non-PEGylated 24-mer only |
| CAS Registry Number | No standard CAS is indexed for the MGF E-domain peptide or the PEGylated analogue |
| Product sequence and terminus | Batch-specific; verify against the released specification and COA |
| PEG chemistry and attachment site | Batch-specific; verify against the released specification and COA |
| Product total molecular mass and salt form | Batch-specific; verify against the released specification and COA |
| Physical form, SKU and stated content | SKU FMP2. The catalogue records lyophilised material at 2 mg per vial; these entries require confirmation against the label and batch documentation |
| Purity | Report only for the tested batch and applicable COA |
| Intended use | Research use only; laboratory research; not for human or veterinary use |
No indexed standard CAS is a documented finding, not an unresolved field. Native references cannot authenticate a conjugate. A record connects designation, batch code, specification and applicable COA.
Identity context: Yang & Goldspink 2002 · PMID 12095637
02What PEGylation means for the analogue
PEGylation denotes conjugation of polyethylene glycol to an E-domain peptide construct. As a chemical concept, it is used to investigate extended circulation relative to a free peptide. This does not establish a product persistence value or equivalence with native MGF.
Polymer contribution
Polymer length, attachment chemistry and conjugation site affect the expected total mass and may introduce conjugate heterogeneity.
Analytical identity
An HPLC profile can differ from that of the free peptide. MS interpretation depends on a defined conjugate and method.
Evidence boundary
Native-peptide formulae, sequences and database records cannot fill product-specific identity fields for PEG-MGF.
The supplied material's sequence, terminus, PEG composition, attachment site, total mass and salt form require batch-specific specification and COA reconciliation. HPLC may provide a batch-specific chromatographic result; MS may support identity for the defined conjugate. Neither establishes every attribute alone.
Design context: Dai et al. 2010 · PMID 20494600
03Research landscape for MGF and IGF-1Ec
This section describes findings in controlled research and makes no statement about use. Every cited record concerns a native or synthetic, non-PEGylated E-domain peptide, or endogenous splice-variant expression—not the supplied PEG conjugate. Model, analyte, method and endpoint delimit each entry.
In vitro · myoblasts
Yang & Goldspink, 2002, FEBS Letters
A non-PEGylated IGF-I Ec E-domain peptide was compared with mature IGF-I in a myoblast model; PEG-MGF was not studied.
PMID 12095637In vitro · constructs
Cheema et al., 2005, Journal of Cellular Physiology
Cells and tissue constructs were used to examine mechanically regulated endogenous IGF-I splicing; no PEG conjugate was tested.
PMID 15389530In vitro · human cells
Mills et al., 2007, Experimental Cell Research
Cultured human myogenic precursor cells were assessed with a synthetic, non-PEGylated MGF E-domain peptide; supplied PEG-MGF was not studied.
PMID 17156777In vitro · tissue
Ates et al., 2007, FEBS Letters
Normal and altered muscle-tissue models were used to quantify progenitor-cell endpoints; the work did not characterise PEG-MGF.
PMID 17531227In vitro · human cells
Kandalla et al., 2011, Mechanisms of Ageing and Development
Human muscle progenitor-cell cultures from donors of different ages were assessed; no PEG conjugate was investigated.
PMID 21354439In vitro · porcine cells
Qin et al., 2012, Molecular and Cellular Biochemistry
Cultured porcine satellite cells provided model-specific cellular and transcription-factor endpoints for non-PEGylated material.
PMID 22875667In vitro · rabbit cells
Tong et al., 2015, BMC Biochemistry
Rabbit mesenchymal-cell culture was used for cellular differentiation and PI3K/AKT measurements; PEG-MGF was not characterised.
PMID 25588515Animal model · rat
Hill & Goldspink, 2003, The Journal of Physiology
A preclinical rat model connected endogenous IGF-I splicing after local tissue damage with satellite-cell activation; it was not a PEG-MGF study.
PMID 12692175Animal model · cerebral
Dluzniewska et al., 2005, The FASEB Journal
A preclinical cerebral-ischaemia model examined a non-PEGylated C-terminal IGF-1Ec peptide, not supplied PEG-MGF.
PMID 16144956Animal model · dopaminergic
Quesada et al., 2009, Experimental Neurology
A preclinical dopaminergic-neuron model examined a C-terminal peptide and haem oxygenase-1 induction; PEG-MGF was not studied.
PMID 19735655Human · endogenous
Hameed et al., 2003, The Journal of Physiology
A human physiological protocol measured endogenous IGF-I splice-variant expression in biopsies. It was not a reagent study or an investigation of PEG-MGF.
PMID 12562960Review
Goldspink, 2005, Physiology
A review considered mechanical signalling and IGF-I gene splicing; it did not provide batch evidence for a PEG conjugate.
PMID 16024511Review
Goldspink, 2006, International Journal of Biochemistry & Cell Biology
A review discussed IGF-I splicing, MGF expression and altered muscle models, not the supplied conjugate.
PMID 16463438Review
Dai et al., 2010, Growth Hormone & IGF Research
A review addressed IGF-1Ec expression and regulation across tissue models; it did not characterise PEG-MGF.
PMID 20494600Cell, tissue, animal and endogenous-expression records remain model-specific. None establishes sequence, PEG chemistry, identity, purity or stability for a supplied batch.
Study sources: the fourteen linked PubMed records above define this model-qualified evidence map.
04Terminology and classification boundaries
PEG-MGF and PEG MGF denote the same catalogue identity. Mechano growth factor, MGF peptide and IGF-1Ec E-domain peptide describe the parent splice-variant or peptide context. Native MGF, endogenous expression, free synthetic peptide and PEG-MGF are not analytically interchangeable.
PEG-MGF is also distinct from IGF-1 LR3, an 83-residue long-chain IGF-1 analogue. Mature recombinant IGF-1, known as mecasermin or Increlex, is another separate identity. PEG-MGF concerns an analogue of an IGF-1Ec E-domain peptide, whereas IGF-1 LR3 and mecasermin concern mature IGF-1 constructs. Sequence boundaries, molecular records and study findings belonging to one must not be assigned to another.
Classification cannot replace analysis. The specification defines batch attributes; results document a tested sample under named methods. The literature does not show that PEGylation preserves endpoints reported for a free peptide.
Classification sources: Hameed et al. 2003 · PMID 12562960 · Goldspink 2006 · PMID 16463438
05Form, storage, batch documentation and research supply in the EU
The catalogue records SKU FMP2, lyophilised material and 2 mg per vial. These presentation entries are not released specifications and require label and batch-document confirmation. No storage temperature or stability interval is inferred; binding conditions must come from released product information.
A batch COA should connect product designation, sample reference, batch code, analytical method, analysis date and result. The exact sequence, terminus, PEG chemistry, attachment site, total molecular mass and salt form should be reconciled against the released specification and applicable COA. Any numerical purity statement applies only to the tested batch and stated method; this page does not assert that a released COA or MS evidence is already available for an offered batch.
PEG-MGF is supplied to EU laboratories as research material. Publications do not certify delivered identity, content, form, purity or stability. Review should connect label, specification, batch code and analytical documentation.
Research use only. For laboratory research only. Not for human or veterinary use. Not intended to diagnose, treat, cure or prevent any disease. Not a medicinal product, food or cosmetic.
FAQ
Frequently asked questions
Struktur & Identifikatoren
Struktur & Identifikatoren
> Die folgenden Werte beziehen sich auf das native, nicht-PEGylierte MGF-24-mer (PubChem CID 175675731). Exakte Sequenz/Terminus, PEGylierungs-Chemie, Gesamt-Molgewicht und Salzform des PEG-MGF-Produkts werden über chargenbezogene Qualitätsdokumentation ausgewiesen.Produktname: PEG MGF (PEGyliertes Mechano Growth Factor)Was es ist: PEGyliertes (stabilitäts-optimiertes) synthetisches Analogon des MGF-C-terminalen E-Domänen-PeptidsStammmolekül: MGF = Mechano Growth Factor = IGF-1Ec (mechanisch induzierte Spleißvariante des IGF-1-Gens)Bioaktives Motiv: C-terminales E-Domänen-Peptid (~24 Aminosäuren)Sequenz (natives humanes 24-mer): YQPPSTNKNTKSQRRKGSTFEEHK (häufig zitiert) — alternative Literatur-/Datenbank-Form endet `…FEERK`; synthetische Varianten oft mit D-Aminosäuren im zentralen QRRK-Motiv und/oder N-terminaler PEGylierung — exakte Form per COA bestätigenPubChem CID (natives 24-mer): 175675731Summenformel (natives 24-mer): C121H199N41O40Molgewicht (natives 24-mer): ≈ 2868.1 g/mol — freies Peptid; das PEGylierte Produkt ist schwerer (PEG-Anteil), Gesamt-MW per COA bestätigenPEG-MGF Gesamt-MW / PEG-Chemie: — abhängig vom verwendeten PEG; per Charge-COA bestätigenCAS: — kein Standard-CAS für das MGF-E-Peptid bzw. das PEGylierte Analogon indexiertSalzform: üblicherweise lyophilisiert als Acetat/TFA-Salz — Form per COA bestätigenRegulatorischer Status: Forschungspeptid; nicht als Arzneimittel zugelassen (FDA/EMA) und kein NDA (Stand 2026); nicht identisch mit Mecasermin/Increlex (zugelassenes reifes IGF-1)## Research Overview
In Studien wurde gezeigt, dass das MGF-/E-Domänen-Peptid Effekte auf folgende Forschungsbereiche haben kann: Myoblasten-Proliferation und -Differenzierung, Satelliten-/Muskelvorläuferzell-Aktivierung, Mechanotransduktion sowie Neuroprotektion in Modellsystemen. Der zentrale und konversionsstärkste Forschungsanker ist die Muskelzell-Biologie: In der wegweisenden Arbeit von Yang & Goldspink wurde berichtet, dass das MGF-E-Peptid die Proliferation von Myoblasten fördert und sie von der Differenzierung zurückhält — eine von reifem IGF-1 klar abgegrenzte Rolle [Yang & Goldspink 2002]. Auf der Gewebe-Ebene wurde MGF-Spleißen mit der Aktivierung von Muskel-Satelliten-(Stamm-)Zellen nach lokaler Gewebeschädigung verknüpft [Hill & Goldspink 2003], und in Satellitenzellen wurde der Effekt mechanistisch über die Herunterregulation myogener Transkriptionsfaktoren beschrieben [Qin 2012].
Besonders belastbar ist die Human-Zell-Evidenz: Ein synthetisches MGF-E-Domänen-Peptid zeigte eine pro-migratorische Aktivität auf menschlichen Muskel-Vorläuferzellen [Mills 2007], und das MGF-E-Peptid aktivierte menschliche Muskel-Vorläuferzellen und erhöhte deren Fusionspotenzial über verschiedene Altersgruppen [Kandalla 2011]. Passend dazu steigt die MGF-Expression in menschlichem Skelettmuskel nach hochintensivem Widerstandstraining [Hameed 2003] — ein Beleg, dass MGF die last-/belastungsabhängige IGF-1-Spleißvariante ist. Diese Mechanotransduktion wurde in vitro direkt gezeigt: mechanische Signale lenken das IGF-1-Spleißen zur MGF-Variante [Cheema 2005; Goldspink 2005]. Umgekehrt ist ein gestörtes IGF-1-Spleißen/eine reduzierte MGF-Expression mit Muskelschwund-Modellen assoziiert [Goldspink 2006].
Über die Muskulatur hinaus existiert eine quellenbelegte Neuro-Achse: Das autonome C-terminale MGF-Peptid zeigte einen starken neuroprotektiven Effekt in einem Hirnischämie-Modell [Dluzniewska 2005] und schützte dopaminerge Neuronen über die Induktion von Häm-Oxygenase-1 (HO-1) [Quesada 2009]. Mechanistisch beschleunigte MGF zudem die Proliferation und osteogene Differenzierung mesenchymaler Stammzellen über den PI3K/AKT-Signalweg [Tong 2015], und Übersichtsarbeiten fassen die Expression/Regulation von IGF-1Ec über verschiedene Gewebe zusammen [Dai 2010].
Kurz gesagt: Die Studienlage positioniert MGF als überzeugendes Forschungsfeld rund um Myoblasten-/Satellitenzell-Biologie, Mechanotransduktion und Neuroprotektion — mit klarer Reborn-Einordnung als Research Use Only und ohne jegliche Anwendungs-, Dosierungs-, Muskelaufbau-, Recovery- oder Performance-Versprechen.
Forschungsgebrauch, Lagerung & Handhabung
Storage & Handling
Lagerungs- und Chargenangaben werden anhand der finalen COA-/Spezifikationsdokumente veröffentlicht. Dieses Produkt wird ausschließlich für die In-vitro-/Laborforschung geliefert und ist nicht zur Anwendung beim Menschen oder Tier bestimmt. Es werden keine Anwendungs-, Dosierungs- oder Verabreichungshinweise gegeben.
What is PEG-MGF?
PEG-MGF is a PEGylated analogue of a C-terminal E-domain peptide associated with IGF-1Ec, commonly called mechano growth factor.
Does native 24-mer identity data define the supplied conjugate?
No. Published sequence, formula and PubChem data concern native, non-PEGylated material and cannot identify the supplied PEG conjugate.
What does the cited research examine?
The literature examines native MGF, IGF-1Ec expression or synthetic E-domain peptides in cell, tissue, animal and human physiological research models. It does not directly characterise the supplied PEGylated analogue.
Does PEGylation establish a particular experimental outcome?
No. PEGylation is described as a stability-oriented design strategy, but it does not prove equivalence to the native peptide, establish a particular persistence value or predict an outcome.
How must product identity and purity be documented?
The exact sequence, terminus, PEG chemistry, total mass, salt form and analytical results must be connected to the matching batch documentation and COA. Purity is batch-specific.
How is the peg mgf peptide classified by Reborn?
It is offered exclusively for controlled laboratory research and is not intended for human or veterinary use.
How can I pay?
We accept prepayment by SEPA bank transfer as well as cryptocurrencies. All payments are processed securely and encrypted.
How fast and how is it shipped?
Discreet shipping from the EU within 4–5 business days. Neutral packaging with no reference to the contents.
