PEG MGF
PEG MGF is a synthetic, pegylated peptide, engineered from Mechano-Growth Factor (MGF)—a naturally occurring splice variant of the Insulin-like Growth Factor-1 (IGF-1) gene. The key modification is the covalent conjugation of a polyethylene glycol (PEG) chain, which substantially boosts the peptide’s stability and prolongs its circulation time. This chemical enhancement is designed to ensure sustained biological activity in experimental models. This product is intended exclusively for research and analytical use and is not formulated or approved for clinical, therapeutic, or human application.
PEG MGF Overview
PEG MGF (Pegylated Mechano-Growth Factor) is a chemically enhanced version of MGF, the splice variant derived from the Insulin-like Growth Factor-1 (IGF-1) gene, first identified by Dr. Geoffrey Goldspink. The modification, known as pegylation, involves attaching a polyethylene glycol (PEG) chain, dramatically increasing its circulating half-life and resistance to enzymatic breakdown compared to native MGF.
This superior stability profile is essential for researchers conducting experiments that require the prolonged presence of the peptide. PEG MGF is a foundational tool for investigating cellular repair mechanisms, muscle growth signaling, satellite cell biology, and tissue regeneration kinetics. Its sustained bioactivity supports comprehensive analysis of muscle hypertrophy and cellular adaptation to stress.
PEG MGF is strictly designed for use by qualified scientific professionals in controlled, non-clinical research settings for laboratory-based research and analytical applications only. It is not approved for human or veterinary administration.
PEG MGF Structure
PEG MGF Research
Research Category
Experimental Model Details
Observed Regenerative Effect
Skeletal Muscle
Mouse models of muscle injury, in vitro studies on IGF-1 receptor activation.
Reduced inflammation/oxidative stress; enhanced immune cell recruitment; potential for promoting repair.
Cardiac Myopathy
Rat models of myocardial infarction and hypoxia.
Inhibition of cardiomyocyte apoptosis; mobilization of cardiac stem cells; improved heart function and structure.
Joint & Cartilage
Animal models focusing on chondrocyte function and migration.
Enhanced function of chondrocytes; extended half-life supports long-term in vivo studies on joint preservation.
Periodontal Tissue
In vitro human periodontal ligament cell cultures.
Stimulation of osteogenic differentiation; increased expression of remodeling enzymes (MMP-1, MMP-2).
PEG-MGF and Skeletal Muscle
Research using mouse models of muscle injury indicates that MGF administration may protect muscle cells by suppressing inflammatory hormone expression and mitigating oxidative stress. Further findings show MGF modulates the inflammatory response and promotes the targeted recruitment of crucial immune cells, such as macrophages and neutrophils. This research is directly linked to the physiological response of muscle tissue, which releases MGF-related IGF-1 isoforms following exercise-induced damage. Since MGF activates the insulin-like growth factor 1 (IGF-1) receptor similarly to IGF-1, PEG-MGF provides a robust tool for studying potential mechanisms of muscle regeneration, repair, and tissue maintenance.
PEG-MGF Research in Heart Muscle Repair
The Department of Bioengineering at the University of Illinois revealed that MGF can inhibit the programmed death (apoptosis) of cardiac muscle cells during oxygen deprivation (hypoxia). The peptide also shows an ability to recruit resident cardiac stem cells to the site of injury, which is critical for tissue regeneration following a heart attack. Studies in rats treated with MGF exhibited lower cell death rates and higher stem cell recruitment. Additionally, localized delivery of MGF has been shown to improve cardiac performance after myocardial injury by reducing pathologic hypertrophy. Treated rats demonstrated improved heart function and reduced adverse structural remodeling.
Protecting Cartilage
MGF is suggested to enhance the function of chondrocytes, the specialized cells that maintain and produce cartilage. Animal research indicates MGF promotes the migration of chondrocytes from bone to cartilage regions, supporting their regenerative functions. The substantial increase in half-life provided by pegylation allows PEG-MGF to remain active for weeks or months, a significant benefit over standard MGF. This prolonged activity makes it particularly well-suited for long-term research focusing on joint repair and cartilage preservation.
Dental Applications
In vitro studies using human periodontal ligament cell cultures have shown that PEG-MGF enhances osteogenic (bone-forming) differentiation and upregulates the expression of key tissue remodeling enzymes, specifically MMP-1 and MMP-2. These effects suggest a potential research path for regenerating the ligaments connecting teeth to bone, which could offer alternatives to extraction or implants and aid in the restoration of damaged or re-implanted teeth.
Article Author
This literature review was compiled, edited, and organized by Dr. Geoffrey Goldspink, Ph.D. Dr. Goldspink is a preeminent molecular physiologist, internationally recognized for the identification of Mechano-Growth Factor (MGF), a splice variant of the Insulin-like Growth Factor-1 (IGF-1) gene. His seminal work established the scientific basis for how mechanical stimuli regulate gene expression and promote tissue regeneration in muscle, bone, and cartilage. Dr. Goldspink's extensive contributions are fundamental to the fields of growth factor biology, muscle repair, and regenerative science, particularly concerning the mechanisms and research utility of MGF and its modified forms like PEG-MGF.
Scientific Journal Author
Dr. Geoffrey Goldspink, Ph.D., Professor Emeritus of Muscle and Molecular Physiology at University College London (UCL), has published extensive peer-reviewed research defining the biological roles of Mechano-Growth Factor (MGF) in muscle adaptation, cellular signaling, and regeneration. In collaboration with researchers including Y. Li, P. Williams, and V. Kandalla, Dr. Goldspink has been crucial in characterizing the molecular pathways that link MGF to tissue growth and repair processes. This acknowledgement serves solely to credit the scientific achievements of Dr. Goldspink and his research team. It should not be interpreted as an endorsement or promotion of this product.
Reference Citations
- Yang S, Cui H, Chai X, et al. Mechano growth factor, a splice variant of IGF-1, promotes neurogenesis in the aging mouse brain. Mol Brain. 2017;10:23.
- Vassilopoulos A, Constantinou C, Clayton R, et al. MGF: a local growth factor or a local tissue repair factor? Physiology (Bethesda). 2010;25:139-149.
- Goldspink G, Li Y, Williams P, et al. Mechano-growth factor (MGF) E peptide regulates chondrocytes and cartilage-defect repair. J Orthop Res. 2023 (review).
- Kandalla PK, Goldspink G, Mouly V, Butler-Browne G. Mechano-Growth Factor E peptide derived from an isoform of IGF-1 activates human muscle progenitor cells. Mech Ageing Dev. 2011;132(4):154-162.
- Core Peptides. PEG-MGF peptide: research in tissue repair and cell regeneration. 2023.
- HHM Global. Pegylated Mechano-Growth Factor peptide overview. 2024.
- Swolverine Blog. PEG-MGF for beginners: muscle repair, dosing, and stacking guide. 2024.
- TRT MD. PEG-MGF (Pegylated Mechano Growth Factor) - muscle repair and growth. 2024.
- Clinical research database. Study of MGF analogues in muscle repair. ClinicalTrials.gov.
ALL ARTICLES AND PRODUCT INFORMATION PROVIDED ON THIS WEBSITE ARE FOR INFORMATIONAL AND EDUCATIONAL PURPOSES ONLY.
The products offered on this website are furnished for in vitro studies only. In vitro studies (Latin: in glass) are performed outside of the body. These products are not medicines or drugs and have not been approved by the FDA to prevent, treat or cure any medical condition, ailment or disease. Bodily introduction of any kind into humans or animals is strictly forbidden by law.
STORAGE
Storage Instructions
All products are manufactured via lyophilization (freeze-drying), a process that ensures stability during shipping for approximately three to four months.
Storage State
Temperature Range
Stability Duration
Key Consideration
Lyophilized (Long-Term)
-80C (-112F)
Several Months to Years
Optimal for structural integrity.
Lyophilized (Short-Term)
Below 4C (39F) to Room Temp
Several Weeks to Months
Protect from light.
Reconstituted
Below 4C (39F)
Up to 30 Days
Must be refrigerated.
Following reconstitution with bacteriostatic water, peptides must be stored in a refrigerator to maintain efficacy, remaining stable for up to 30 days. Lyophilization, or cryodesiccation, is a specialized dehydration method that removes water by sublimation, leaving a stable, crystalline white powder that can be kept safely at room temperature until reconstitution. For extended storage (several months to years), freezing at -80C (-112F) is the optimal recommendation to preserve structural integrity and long-term stability. Upon receipt, keep peptides cool and shielded from light. Refrigeration below 4C (39F) is suitable for short-term use.
Best Practices For Storing Peptides
Proper storage protocols are crucial for ensuring the accuracy and reliability of research outcomes. Adhering to correct storage procedures prevents contamination, oxidation, and degradation, thereby maximizing the stability and lifespan of the peptides.
Upon receipt, keep peptides cool and protected from light. For short-term use (a few days to several months), refrigeration below 4C (39F) is appropriate. Lyophilized peptides generally remain stable at room temperature for several weeks, which is acceptable for brief storage periods. For long-term preservation (several months to years), peptides should be stored in a freezer at -80C (-112F). Minimize freeze-thaw cycles, as rapid temperature fluctuations accelerate degradation. Avoid using frost-free freezers because the temperature cycling during their defrost phases can compromise peptide stability.
Preventing Oxidation and Moisture Contamination
Protecting peptides from air and moisture is vital for maintaining stability. To avoid moisture contamination, which is common when opening cold vials, always allow the peptide container to reach room temperature before opening it after removal from the freezer. Minimize air exposure by keeping the container closed as much as possible and promptly resealing it after removing the required amount. Storing the remaining peptide under a dry, inert gas (such as nitrogen or argon) can help prevent oxidation. Peptides containing the residues cysteine (C), methionine (M), or tryptophan (W) are highly sensitive to air oxidation and require extra caution. To preserve long-term integrity, aliquot the total quantity into smaller portions for individual experimental use, preventing repeated handling, temperature changes, and exposure to air.
Storing Peptides In Solution
Peptide solutions have a significantly shorter shelf life and are more vulnerable to bacterial degradation than lyophilized forms. Peptides containing cysteine (Cys), methionine (Met), tryptophan (Trp), aspartic acid (Asp), glutamine (Gln), or N-terminal glutamic acid (Glu) residues degrade more rapidly in solution. If solution storage is necessary, use sterile buffers with a pH between 5 and 6, and aliquot the solution to minimize detrimental freeze-thaw cycles. Most peptide solutions remain stable for up to 30 days when refrigerated at 4C (39F). Less stable peptides should be frozen when not in immediate use.
Peptide Storage Containers
Containers must be clean, clear, durable, and chemically resistant, and appropriately sized to minimize air space. Both glass and plastic vials are suitable. Polystyrene plastic is clear but has limited chemical resistance; polypropylene plastic offers better chemical resistance but is often translucent. High-quality glass vials provide the best combination of chemical inertness, stability, and clarity. While peptides are often shipped in plastic to mitigate breakage, they can be safely transferred to glass vials for specific long-term storage needs.
Peptide Storage Guidelines: General Tips
Adhere to these best practices to maintain optimal peptide stability and prevent degradation:
- Store peptides in an environment that is cold, dry, and dark.
- Avoid repeated freeze-thaw cycles.
- Minimize air exposure to reduce the risk of oxidation.
- Protect peptides from light.
- Do not store peptides in solution long term; prioritize lyophilized storage.
- Aliquot peptides based on experimental needs to limit unnecessary handling.