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PEG MGF

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$19.99$37.99

Concentration
2 mg per vial

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Properties

Physical Appearance Fine White Lyophilized Powder
Residue Sequence PEG-Tyr-Gln-Pro-Pro-Ser-Thr-Asn-Lys-Asn-Thr-Lys-Ser-Gln-Arg-Arg-Lys-Gly-Ser-Thr-Phe-Glu-Glu-Arg-Lys-NH2
Solubility 100 μg/mL sterile diluent (distilled de-ionized water)
Source Biosynthetic production
Stability Lyophilized protein is to be stored at -20°C. It is recommended to aliquot the reconstituted (dissolved) protein into several discrete vials in order to avoid repeated freezing and thawing. Reconstituted protein can be stored at 4°C.
Molar Mass 2867.2 g/mol
Molecular Formula C121H200N42O39

Description

Polyethylene Glycol (PEG) Mechano Growth Factor (MGF) is an isoform of Insulin Like Growth Factor 1 (IGF-1) comprised of 24 amino acid residues that is stabilized by a biocompatible polymer coating (PEG). The C-terminal residue sequence of MGF infers the characteristics that make this peptide unique from IGF-11.

A natural form of MGF is expressed in muscle tissues in response to the overburdening or damage of these cells2. MGF has been found to induce the stimulation of repair, regrowth, and the formation of new cells in response to stress3. This process is called hypertrophy (or hyperplasia) and is crucial in the gaining of muscle mass.

The natural production of MGF stimulates the recruitment of undamaged cells to give rise to new muscle tissues, while a liver-derived variant of this agent (IGF-1Ea) initiates the upregulation – or positive feedback control – of protein synthesis4. Through these biochemical pathways, MGF is thought to be the primary mechanism by which the body naturally produces new muscle tissue.

Animal studies have shown MGF as an active neuroprotective agent5 and a promoter of conserved skeletal health6. Also, reinforcing its functionality as an agent of muscle tissue repair, MGF has been found to be active in coordinating the repair of heart muscle tissue following myocardial infarction (heart attack)7.

Product Comparison

Though IGF-1 and MGF are very similar in origin and in (partial) structure, the two agents have very different mechanisms of action. Researchers have expressed that these two agents show great synergy and have observed enhanced rates in muscle growth while both IGF-1 LR3 (or IGF-1 DES) and MGF have been administrated together in animal subjects.

PEG MGF is much more stable than unprotected MGF, which infers a much longer residence time in the bloodstream. Preference for MGF’s ‘burst’ profile or PEG MGF’s sustained profile of activity must be determined by the research intent.

Synonyms:

Pegylated MGF, PEG IGF-1 Ec; Pegylated MGF Splice Variant of IGF-;


Peer-Reviewed Sources:

  1. Hill, M., & Goldspink, G. (2003). Expression and Splicing of the Insulin‐Like Growth Factor Gene in Rodent Muscle is Associated with Muscle Satellite (stem) Cell Activation following Local Tissue Damage. The Journal of physiology, 549(2), 409-418. ↩︎
  2. Matheny Jr, R. W., Nindl, B. C., & Adamo, M. L. (2010). Minireview: Mechano-growth factor: a putative product of IGF-I gene expression involved in tissue repair and regeneration. Endocrinology, 151(3), 865-875. ↩︎
  3. Iida, K., Itoh, E., Kim, D. S., Del Rincon, J. P., Coschigano, K. T., Kopchick, J. J., & Thorner, M. O. (2004). Muscle mechano growth factor is preferentially induced by growth hormone in growth hormone‐deficient lit/lit mice. The Journal of physiology, 560(2), 341-349. ↩︎
  4. Goldspink, G. (1999). Changes in muscle mass and phenotype and the expression of autocrine and systemic growth factors by muscle in response to stretch and overload. Journal of anatomy, 194(03), 323-334. ↩︎
  5. Quesada, A., Micevych, P., & Handforth, A. (2009). C-terminal mechano growth factor protects dopamine neurons: a novel peptide that induces heme oxygenase-1. Experimental neurology, 220(2), 255-266. ↩︎
  6. Barton-Davis, E. R., Shoturma, D. I., Musaro, A., Rosenthal, N., & Sweeney, H. L. (1998). Viral mediated expression of insulin-like growth factor I blocks the aging-related loss of skeletal muscle function. Proceedings of the National Academy of Sciences, 95(26), 15603-15607. ↩︎
  7. Carpenter, V., Matthews, K., Devlin, G., Stuart, S., Jensen, J., Conaglen, J., & McMahon, C. (2008). Mechano-growth factor reduces loss of cardiac function in acute myocardial infarction. Heart, lung and circulation, 17(1), 33-39. ↩︎

All literature, information, and data, provided on this website are for informational and educational purposes only.

Accurate research is our priority.

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