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IGF-1 LR3 (1mg)
IGF-1 LR3 peptides are Synthesized and Lyophilized in the USA.
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What is the IGF-1 LR3 Peptide?
IGF-1 LR3 is an altered variant of insulin-like growth factor-1; the complete name of the peptide is insulin-like growth factor-1 long arginine 3. IGF-1 derivatives have played important roles in research studies on cell proliferation, cell division, and cell-to-cell communication. Despite showing physiological effects similar to the parent protein, IGF-1 LR3 does not interact with IGF binding proteins as strongly as IGF-1. Hence, it appears to stay in the bloodstream for longer durations (about 120 times longer) as compared to native IGF-1. The structural modifications in IGF-1 LR3 may have contributed to its increased half-life in the blood. The peptide is created by the inclusion of 13 amino acids to the N-terminus of native IGF-1 and by replacing the glutamic acid at position 3 to arginine.
Molecular Formula: C400H625N111O115S9
Molecular Weight: 9117.60 g/mol
Sequence: MFPAMPLSSL FVNGPRTLCG AELVDALQFV CGDRGFYFNK PTGYGSSSRR APQTGIVDEC CFRSCDLRRL EMYCAPLKPA KSA
CAS Number: 946870-92-4
IGF-1 LR3 and Cell Division
Like IGF-1, research suggests that IGF-1 LR3 may act as a stimulus for cell division and proliferation, primarily affecting connective tissues of the muscle and bone and cell division in the liver, kidney, skin, lung, nerve, and blood tissues. IGF-1 is best considered to be a maturation hormone because of its apparent influence in cell proliferation, differentiation, and maturation, helping them to carry out their specialized functions. The longer life span of IGF-1 LR3 in the blood makes it a more potent molecule as compared to IGF-1. A single dose of IGF-1 LR3 appears to provide about three times as much cellular activation compared to a similar dose of IGF-1. Researchers report that “The response with LR3IGF-I was particularly striking because this peptide binds 3-fold less well than IGF-I to the type 1 IGF receptor.“ It is important to remember that IGF-1 LR3 peptide and every IGF-1 derivative have not been observed to mediate cellular enlargement (hypertrophy), and instead may participate in cell division and proliferation (hyperplasia). For instance, in the case of muscle, studies suggest IGF-1 LR3 would not cause enlargement of muscle cells, rather simply increasing the total number of muscle cells.
IGF-1 LR3 and Myostatin
Myostatin (also known as growth differentiation factor 8) is a muscle protein that primarily suppresses the growth and differentiation of muscle cells. Myostatin is, thus crucial in protection from unregulated hypertrophy and proper healing post-injury. However, some situations that demand inhibition of myosin. Blocking of myosin can be helpful in conditions like Duchenne Muscular Dystrophy (DMD) or in people who suffer from loss of muscle due to prolonged immobility. In such cases, blocking the natural enzyme could help slow down muscle breakdown, maintain strength, and avoid morbidity. Studies conducted in mouse models of DMD have suggested that IGF-1 LR3 and other IGF-1 derivatives may overcome the adverse effects of Myostatin to protect muscle cells and prevent apoptosis. The scientists note that “results together suggest that myostatin suppresses both basal and IGF-1-stimulated proliferation of both WAT and BAT preadipocytes, actions that are again similar to those in muscle satellite cells”. IGF-1 LR3, due to its long stability, may be effective in counteracting Myostatin by activating MyoD, a muscle protein that is normally triggered by exercise (e.g., weight lifting).
IGF-1 LR3 and Metabolism, Diabetes
Researchers suggest that IGF-1 LR3 indirectly boosts fat burning by associating with the IGF-1R receptor and the insulin receptor. These interactions may improve glucose uptake from the blood by muscle, nerve, and liver cells. This potential would result in an overall reduction in blood sugar levels, which then trigger adipose tissue as well as the liver to initiate catabolism of glycogen and triglycerides. Overall, this leads to a decrease in adipose tissue and net energy consumption (i.e. net catabolism). Given its role in controlling blood sugar levels, IGF-1 LR3 may reduce insulin levels and the need for exogenous insulin in diabetes. In a majority of the patients, this brings about a 10% reduction in insulin requirements to maintain the same blood sugar levels. IGF-1 LR3 thus helps understand insulin regulation in patients with decreased insulin sensitivity. It also highlights possible ways to prevent type 2 diabetes.
IGF-1 LR3 and Longevity Research
Studies observe that IGF-1 LR3 may promote tissue repair and upkeep of the body, making it a protective molecule against cellular damage and the effects of aging. Research in cows and pigs indicate that IGF-1 LR3 administration may overcome the effects of aging, prolong life and reduce disability. Ongoing research in mice has focused on the potential of IGF-1 LR3 in preventing the progression of a wide range of conditions such as muscle atrophy, dementia, and kidney disease.
IGF-1 LR3 and Glucocorticoid Signaling
Glucocorticoids, produced essentially from the adrenal glands, also act as important clinical medications which help to control pain and decrease inflammation in autoimmune diseases, cancer, and neurological injuries, to name a few. However, glucocorticoids have numerous undesirable side effects, such as muscle wasting, fat gain, and deterioration of bone density. Thus, IGF-1 LR3 is being explored as an option to reduce the side effects of glucocorticoids and thereby mediate a more effective therapy. Studies have shown minimal to moderate side effects, low oral bioavailability, and excellent subcutaneous bioavailability in mice. Per kg dosage in mice does not scale up to the dosage which can be required for humans.
- Assefa B, Mahmoud AM, Pfeiffer AFH, Birkenfeld AL, Spranger J, Arafat AM. Insulin-Like Growth Factor (IGF) Binding Protein-2, Independently of IGF-1, Induces GLUT-4 Translocation and Glucose Uptake in 3T3-L1 Adipocytes. Oxid Med Cell Longev. 2017;2017:3035184. doi: 10.1155/2017/3035184. Epub 2017 Dec 20. PMID: 29422987; PMCID: PMC5750484.
- Tomas FM, Knowles SE, Owens PC, Chandler CS, Francis GL, Read LC, Ballard FJ. Insulin-like growth factor-I (IGF-I) and especially IGF-I variants are anabolic in dexamethasone-treated rats. Biochem J. 1992 Feb 15;282 ( Pt 1)(Pt 1):91-7. doi: 10.1042/bj2820091. PMID: 1371669; PMCID: PMC1130894.
- Li N, Yang Q, Walker RG, Thompson TB, Du M, Rodgers BD. Myostatin Attenuation In Vivo Reduces Adiposity, but Activates Adipogenesis. Endocrinology. 2016 Jan;157(1):282-91. doi: 10.1210/en.2015-1546. Epub 2015 Nov 18. PMID: 26580671; PMCID: PMC4701895.
- Bailes J, Soloviev M. Insulin-Like Growth Factor-1 (IGF-1) and Its Monitoring in Medical Diagnostic and in Sports. Biomolecules. 2021 Feb 4;11(2):217. doi: 10.3390/biom11020217. PMID: 33557137; PMCID: PMC7913862.
- AsghariHanjani N, Vafa M. The role of IGF-1 in obesity, cardiovascular disease, and cancer. Med J Islam Repub Iran. 2019 Jun 17;33:56. doi: 10.34171/mjiri.33.56. PMID: 31456980; PMCID: PMC6708115.
- Philippou A, Barton ER. Optimizing IGF-I for skeletal muscle therapeutics. Growth Horm IGF Res. 2014 Oct;24(5):157-63. doi: 10.1016/j.ghir.2014.06.003. Epub 2014 Jun 19. PMID: 25002025; PMCID: PMC4665094.
Dr. Usman (BSc, MBBS, MaRCP) completed his studies in medicine at the Royal College of Physicians, London. He is an avid researcher with more than 30 publications in internationally recognized peer-reviewed journals. Dr. Usman has worked as a researcher and a medical consultant for reputable pharmaceutical companies such as Johnson & Johnson and Sanofi.
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