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|Physical Appearance||Fine White Lyophilized Powder|
|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|
IGF-1 is a key factor in mediating the growth-promoting effects of growth hormone (GH) 5. This particular IGF-1 species was developed in order to avoid interaction with IGFBPs (Insulin Like Growth Factor Binding Proteins), which are known to hinder the activity of native IGF-1 over time6. By avoiding this interplay, IGF-1 LR3 is capable of achieving a very long half-life, which leads to its utility as a long-acting, extremely active facilitator of GH-stimulated anabolic activity.
Compared to IGF-1 DES, IGF-1 LR3 is considered to be less active as a stimulant of acute hyperplasia. This said, IGF-1 LR3 with its sustained in vivo activity is able to induce hypertrophic activity over long periods of time, whereas native IGF-1 and IGF-1 DES lack this functionality7.
IGF-1 LR3 and IGF-1 DES have both been demonstrated as more active biological agents relative to native IGF-1 when it comes to stimulating new cell growth in animal trials.
Studies investigating the effects of concurrent IGF-1 species and GH (or GH secretagogue) administration have identified their synergy5 in promoting the development of lean body mass and reduction of fat stores in test subjects.
Insulin Like Growth Factor-1 LR3; IGF-1 Long R3; IGF-1 Long Arg3;
Somatomedin C analogue; Itropin
- Musarò, A., McCullagh, K., Paul, A., Houghton, L., Dobrowolny, G., Molinaro, M., & Rosenthal, N. (2001). Localized Igf-1 transgene expression sustains hypertrophy and regeneration in senescent skeletal muscle. Nature genetics, 27(2), 195-200.
- Wangsa-Wirawan, N. D., Colby, C. B., O’Neill, B. K., & Middelberg, A. P. J. (2000). The Characteristics of Protein Inclusion Bodies: Physicochemical Properties of an Insulin-like Growth Factor Analog-Long-R3-IGF-1.
- Tavakkol, A., Elder, J. T., Griffiths, C. E., Cooper, K. D., Talwar, H., Fisher, G. J., & Voorhees, J. J. (1992). Expression of growth hormone receptor, insulin-like growth factor 1 (IGF-1) and IGF-1 receptor mRNA and proteins in human skin. Journal of Investigative Dermatology, 99(3), 343-349.
- LeRoith, D., & Yakar, S. (2007). Mechanisms of disease: metabolic effects of growth hormone and insulin-like growth factor 1. Nature Clinical Practice Endocrinology & Metabolism, 3(3), 302-310.
- Berryman, D. E., Christiansen, J. S., Johannsson, G., Thorner, M. O., & Kopchick, J. J. (2008). Role of the GH/IGF-1 axis in lifespan and healthspan: lessons from animal models. Growth Hormone & IGF Research, 18(6), 455-471.
- Francis, G. L., Ross, M., Ballard, F. J., Milner, S. J., Senn, C., McNeil, K. A., & Wells, J. R. E. (1992). Novel recombinant fusion protein analogues of insulin-like growth factor (IGF)-I indicate the relative importance of IGF-binding protein and receptor binding for enhanced biological potency. Journal of molecular endocrinology, 8(3), 213-223.
- Ding, H. U., Gao, X. L., Hirschberg, R., Vadgama, J. V., & Kopple, J. D. (1996). Impaired actions of insulin-like growth factor 1 on protein Synthesis and degradation in skeletal muscle of rats with chronic renal failure. Evidence for a postreceptor defect. Journal of Clinical Investigation, 97(4), 1064.
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