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IGF-1 LR3

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$79.99$99.99

Concentration
1 mg per vial

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Properties

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

Identifiers

CAS 143045-27-6

Description

Insulin Like Growth Factor (IGF)-1 LR3 is an 83 amino acid residue analogue of native IGF-1, which has been documented as an agent for inducing hyperplasia and stimulating cellular proliferation1. By modifying the original IGF-1 polypeptide – a 70 amino acid residue sequence – with a 13 amino acid b-terminus extension and a substitution of Arg for Glu at position 3 (hence the synonym Long Arg3)2, IGF-1 LR3 introduces enhancements to IGF-1’s biological activity while improving its structural stability, and therefore, residence time, in vivo.

Animal studies have demonstrated the ability of IGF-1 LR3 to bind directly to natural IGF receptors and stimulate new tissue formation, while inhibiting apoptosis (programmed cell death) in existing tissues3. Especially at muscle cell sites, IGF-1 species are noted to enhance amino acid recruitment, augment the synthesis of new proteins while minimizing the digestion of intracellular protein as a fuel source. Instead, fat deposits are used as energy sources while IGF-1 species are biochemically active4.

Product Comparison

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.

Synonyms:

Insulin Like Growth Factor-1 LR3; IGF-1 Long R3; IGF-1 Long Arg3;

Somatomedin C analogue; Itropin


Peer-Reviewed Sources:

  1. 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. ↩︎
  2. 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. ↩︎
  3. 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. ↩︎
  4. 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. ↩︎
  5. 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. ↩︎
  6. 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. ↩︎
  7. 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. ↩︎

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

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