MGF (C-terminal) 5mg
Is a powerful peptide derived from the Insulin-Like Growth Factor 1 (IGF-1), specifically the Mechano Growth Factor (MGF) splice variant. MGF, also known as IGF-1 Ec in humans, is expressed in muscle tissues in response to mechanical overload or muscle damage, playing a critical role in muscle repair and growth. This peptide is known for its ability to promote tissue regeneration and muscle hypertrophy through its unique mechanism of action.
Key Benefits of MGF (C-terminal) 5mg:
Muscle Repair and Regeneration:
MGF is highly effective in stimulating muscle repair and regeneration. It is released in response to muscle stress, such as intense physical training, and plays a vital role in muscle tissue regeneration. This makes it an ideal peptide for accelerating recovery after workouts or injuries, promoting faster healing and reducing downtime.Promotes Muscle Hypertrophy:
As a variant of IGF-1, MGF stimulates the growth of new muscle fibers and enhances muscle hypertrophy (growth). It achieves this by activating satellite cells in muscle tissues, which are responsible for repairing and building muscle fibers. This results in increased lean muscle mass and improved strength.Improved Muscle Recovery:
MGF aids in faster muscle recovery by enhancing protein synthesis and promoting the repair of damaged muscle tissues. This reduces muscle soreness and allows for more intense and frequent training sessions, making it highly beneficial for athletes or bodybuilders looking to maximize their gains.Enhanced Performance and Endurance:
By accelerating muscle repair and growth, MGF helps improve overall performance and endurance. With quicker recovery times and enhanced muscle strength, users can push through more demanding workouts, resulting in better performance in both strength and endurance sports.Support for Injury Healing:
MGF's role in tissue repair extends beyond just muscle growth. It is also beneficial for healing injuries, particularly those affecting muscle tissues, tendons, and ligaments. Its regenerative properties can assist in reducing recovery time from injuries and minimizing the long-term effects of muscle strain.No Significant Side Effects:
MGF (C-terminal) 5mg is known for its targeted action in muscle tissues, and unlike some other peptides, it does not induce significant systemic side effects. This makes it a safe and effective option for individuals looking to enhance muscle growth and recovery without the risks associated with other performance-enhancing compounds.Increased Satellite Cell Activity:
MGF activates satellite cells, which are critical for muscle growth and repair. This increased activity of satellite cells helps facilitate muscle regeneration, making it particularly useful for individuals seeking to recover from muscle strain or injury and for those engaging in heavy resistance training.
Conclusion:
MGF (C-terminal) 5mg is a highly effective peptide designed to stimulate muscle regeneration, enhance hypertrophy, and improve recovery times. Its unique ability to activate satellite cells and promote tissue repair makes it an invaluable tool for athletes, bodybuilders, and anyone seeking to improve their muscle growth and recovery. With its targeted action and minimal side effects, MGF provides a safe and efficient solution for muscle recovery, performance enhancement, and overall muscle health.
MGF (C-terminal) 5mg
Mechano growth factor (MGF) is a novel splice variant of the Insulin-Like Growth Factor-1 (IGF-1), also known as IGF-1 Ec in humans and IGF-1Eb in rodents. It is actually originally called MGF because the RNA form of it is expressed in muscle tissues in response to the overload or/and damage of muscle growth tissue. The C-terminal peptide of the mechano growth factor (MGF) is a crucial region for the alternative splicing of the peptide. The alternative splicing in the MGF is brought about by the shift in the reading frame in which a specific C-terminal sequence (E-domain) is encoded by exon 5 and the first part of the exon 6. Another interesting point in MGF is that, because of the E domain it contains, MGF can act on muscles independently from the rest of the molecule. Furthermore, MGF can elicit very different effects with mGF promoting satellite cells proliferation and IGF-1 inducing differentiation (Dluzniewska et al. 2005).
Age Related Muscle Loss and MGF
MGF was suggested to play a number of physiological roles because the failure in its expression may result to age-related loss of skeletal function. Included in its functions is its ability to become a potent neuroprotective as supported by the study that has shown functional copies of the MGF cDNA to be expressed in a plasmid vector which then protected facial neurons after nerve damage (Dluzniewska et al. 2005). One such failure is called sarcopenia. It would also appear that with regards to age, the young have a better ability to respond to MGF (4), and that the elderly experience a decreased response to MGF which results in a decreased ability to stimulate the growth of new muscle tissue.
How does Mechano Growth Factor work? - Muscle Growth!
When mechanical overload is introduced to a muscle (as by weight training), the IGF-1 gene is released and is differentially spliced during the bodies response. Initially, it it is spliced to produce predominantly IGF-1Ec (called the MGF splice variant of IGF-1). This early splicing stimulates satellite cells into activation. Which in turn allows the activation of extra undamaged nuclei to grow new muscle fiber and tissue. The appearance of MGF also initiates the upregulation of new protein synthesis. After this initial splicing of IGF-1 into MGF, production then switches towards producing a systemic release of IGF-1Ea from the liver, which also upregulates protein synthesis as well. The expression of IGF-1 splice variants, over the course of the healing and regrowth phase of muscle repair is thought to be the primary mechanism by which the body produces new muscle tissue.
Recent Research and Studies Involving Mechano Growth Factor
Insulin like growth factor-1 (IGF-1) expression is implicated in myocardial pathophysiology, and two IGF-1 mRNA splice variants have been detected in rodents, IGF-1Ea and mechano-growth factor (MGF). Recent research has shown that the expression pattern of IGF-1 gene transcripts in rat myocardium from 1 h up to 8 wks after myocardial infarction induced by left anterior descending coronary artery ligation. In addition, we characterized IGF-1 and MGF E peptide action and their respective signaling in H9C2 myocardial-like cells in vitro. IGF-1Ea and MGF expression were significantly increased, both at transcriptional and translational levels, during the late postinfarction period (4 and 8 wks) in infarcted rat myocardium. Measurements of serum IGF-1 levels in infarcted rats were initially decreased (24 h up to 1 wk) but remained unaltered throughout the late experimental phase (4 to 8 wks) compared with sham-operated rats. Furthermore, specific anti–IGF-1R neutralizing antibody failed to block the synthetic MGF E peptide action, whereas it completely blocked IGF-1 action on the proliferation of H9C2 cells. Moreover, this synthetic MGF E peptide did not activate Akt phosphorylation, whereas it activated ERK1/2 in H9C2 rat myocardial cells. These data support the role of IGF-1 expression in the myocardial repair process and suggest that synthetic MGF E peptide actions may be mediated via an IGF-1R independent pathway in rat myocardial cells, as suggested by in vitro experiments.
Recent studies have also discovered two clones of the hybridonoma secreting monoclonal antibodies to the mechano-growth factor have been developed by cell fusion technique. The monoclonal antibody of one clone recognizes the human MGF peptide that is absent in insulin-like growth factor-1 (IGF-1) which comprised mostly of amino acids from 87-111. Enzyme-linked immunosorbent assay (ELISA) has further shown that there is a high affinity binding constants with the full length of the MGF and the 87-111 fragments of the clones. These can then be used for the quantitation of the MGF through sandwich type assay (Kravchenko et al. 2006).