IGF‑1 LR3 – Advanced Research Peptide
This product is not intended for weight loss, human consumption, or veterinary use. It is sold for research purposes only. Please handle with care and follow all safety guidelines for the specific chemicals involved.
Musculoskeletal & Bone Research
In musculoskeletal studies, IGF-1 peptides have been shown to accelerate muscle regeneration. Rat models demonstrate that IGF‑1 LR3 treatment post-injury promotes satellite cell proliferation, enhances muscle strength, and speeds recovery. Additionally, IGF‑1 administration in rats with bone fractures has been associated with improved bone formation and faster healing, highlighting its potential in bone regeneration studies.
Neuroprotection & Cognitive Research
Research on IGF‑1 LR3 1mg peptide reveals neuroprotective benefits in rat models of brain injury. Administration of IGF‑1 peptides improves cognitive function and reduces neuronal damage, indicating potential applications in the study of neurodegenerative diseases and traumatic brain injury.
Synergistic Research Applications
IGF‑1 has been studied in combination with other growth factors, such as VEGF, to enhance tissue repair and angiogenesis. These findings suggest IGF-1 LR3 can be utilized in complex experimental designs investigating combinatory regenerative therapies.
Research Use & Compliance
All IGF-1 LR3 peptides sold on our platform are strictly for laboratory, analytical, or research purposes. This product is not intended for human or veterinary use, and all studies should comply with relevant research regulations and safety guidelines.
References:
Gawri, R., et al. “Synergistic Effect of IGF-1 and VEGF in Wound Healing.” Journal of Wound Care, vol. 26, no. 7, 2017, pp. 413-419. https://www.jwc.com/
Ma, X., et al. “The Role of IGF-1 in Bone Fracture Healing in Rats.” Bone Research, vol. 6, no. 1, 2018, pp. 15-24. https://www.boneresearchjournal.com/
Schwabe, C., et al. “Insulin-Like Growth Factor 1 and Muscle Regeneration in Rats.” Journal of Muscle Research and Cell Motility, vol. 21, no. 3, 2000, pp. 163-173. https://link.springer.com/
Xie, J., et al. “Neuroprotective Effects of IGF-1 in Traumatic Brain Injury in Rats.” Neuroscience Letters, vol. 551, 2013, pp. 11-16. https://www.journals.elsevier.com/neuroscience-letters
Zhu, X., et al. “IGF-1 and Its Role in Tissue Repair in Rat Models.” Endocrinology, vol. 159, no. 4, 2018, pp. 1527-1535. https://academic.oup.com/endo
NuScience Peptides sells research products only, they are not for human consumption.
Synonyms:
Insulin Like Growth Factor-1 LR3; IGF-1 Long R3; IGF-1 Long Arg3;
Somatomedin C analogue; Itropin
Peer-Reviewed Sources:
- 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.
ALL LITERATURE, INFORMATION, AND DATA, PROVIDED ON THIS WEBSITE ARE FOR INFORMATIONAL AND EDUCATIONAL PURPOSES ONLY.
Properties
| Molecular Formula |
C400H625N111O115S9 |
|---|---|
| Molecular Weight | 9117.60 |
| Monoisotopic Mass | n/a |
| Polar Area | n/a |
| Complexity | n/a |
| XLogP | n/a |
| Heavy Atom Count | n/a |
| Hydrogen Bond Donor Count | n/a |
| Hydrogen Bond Acceptor Count | n/a |
| Rotatable Bond Count | n/a |
| 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 |
| PubChem LCSS |
IGF1-lr2 Laboratory Chemical Safety Summary |
Identifiers
| CID | |
|---|---|
| CAS | 143045-27-6 |
| InChI | |
| InChIKey | |
| Isomeric SMILES | |
| Canonical SMILES | |
| IUPAC Name |
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