Advance Your Research with the addition of pure, tested IGF1-LR3 peptide.
$129.99
IGF1 LR3, available through Research Chemical, is a notable research compound. IGF1-LR3 is an analogue of insulin-like growth factor 1 (IGF1). It is a protein that is involved in cell growth and proliferation. IGF1-LR3 has a very low affinity towards IGFBPs as compared to IGF-1.
In the study, IGF1-LR3 was administered to fetal sheep to stimulate heart growth. The results showed that IGF1-LR3 increased both myocardial and coronary growth. This suggests that IGF1-LR3 may be a potential therapeutic intervention to increase healthy fetal cardiomyocyte endowment.
The mechanism of action of Insulin-like Growth Factor 1 Long R3 (IGF-1 lr3) represents a focal point of investigation in cellular physiology and therapeutic research. As a synthetic analog of the naturally occurring peptide IGF-1, IGF-1 lr3 is distinguished by structural modifications that confer an extended half-life.
Specifically, research explores the selective engagement of IGF-1 lr3 with the IGF-1 receptor on the cell membrane, showcasing the molecular events that ensue and distinguishing its action from the shorter-lived IGF-1 counterpart. Emphasis is placed on elucidating the avoidance of insulin receptor binding, directing IGF-1 lr3 towards the activation of growth-promoting pathways. IGF1-LR3 plays a role on cellular proliferation, protein synthesis, and anabolism.
Insulin-like growth factor 1 Long R3 (IGF1-LR3), a synthetic analog of insulin-like growth factor 1 (IGF-1), has emerged as a promising therapeutic agent with a wide range of potential applications. Its unique properties, including a longer half-life and lower binding affinity for IGF binding proteins (IGFBPs), make it more effective and durable than its natural counterpart. IGF1-LR3 has demonstrated remarkable potential in various areas of medicine, including:
IGF1-LR3 plays a pivotal role in muscle growth and regeneration. It stimulates muscle protein synthesis, promotes satellite cell proliferation, and enhances muscle fiber differentiation. This makes it a promising therapeutic option for treating muscle wasting conditions such as sarcopenia, cachexia, and muscle injuries.
IGF1-LR3 has shown remarkable efficacy in accelerating tissue repair and wound healing. It promotes cell proliferation, angiogenesis, and collagen synthesis, essential processes for tissue regeneration. This property holds promise for treating a variety of conditions, including surgical incisions, burns, and diabetic ulcers.
IGF1-LR3 may play a beneficial role in diabetes management by improving glucose control and insulin sensitivity. It enhances glucose uptake by cells and modulates insulin signaling pathways, potentially offering a novel approach to diabetes treatment.
IGF1-LR3 has been shown to slow down the aging process and delay the onset of age-related diseases. It promotes cellular repair, reduces oxidative stress, and enhances mitochondrial function, potentially contributing to longevity and healthy aging.
IGF-1 LR3 is a synthetic analog of IGF-1, a naturally occurring hormone. While IGF-1 LR3 has some similar effects to IGF-1, it is important to note that it is a different substance with its own unique properties. More research is needed to fully understand the long-term effects of IGF-1 LR3 in humans.
IGF-1 LR3 is still considered an investigational compound, meaning it is not yet approved by the FDA for any medical use. This means that there is limited information available about its safety and efficacy.
Advance Your Research with the addition of pure, tested IGF1-LR3 peptide.
IGF1-LR3 is not a human growth hormone. Instead, it is a synthetic analog of IGF-1, a naturally occurring hormone that plays a role in growth and development. IGF1-LR3 differs from IGF-1 in two main ways:
Half-life: IGF1-LR3 has a longer half-life than IGF-1, which means that it stays in the body for a longer period of time. This makes it more effective for research purposes, as it allows for sustained signaling and a more consistent effect on cells.
Binding affinity: IGF1-LR3 has a lower binding affinity for IGF binding proteins than IGF-1. IGF binding proteins are proteins that bind to IGF-1 and regulate its activity. The lower binding affinity of IGF1-LR3 means that it is less likely to be bound by IGF binding proteins and can therefore exert its effects more effectively.
IGF1-LR3 is being studied for its potential applications in a variety of research areas, including:
Muscle growth and regeneration: IGF1-LR3 has been shown to promote muscle growth and regeneration in animal models. This suggests that it may have potential applications for treating muscle wasting conditions, such as sarcopenia and muscle injuries.
Tissue repair: IGF1-LR3 has also been shown to promote tissue repair in animal models. This suggests that it may have potential applications for treating conditions such as wounds and burns.
Diabetes: IGF1-LR3 is being studied for its potential use in the treatment of diabetes. Early research suggests that it may help to improve glucose control and insulin sensitivity.
IGF1-LR3 is a potent growth factor, and there is some concern that it could have negative side effects, such as:
Tumor growth: IGF1-LR3 has been shown to promote the growth of some types of cancer cells in vitro. More research is needed to determine whether it has the same effect in vivo as it did not affect the rate of tumor growth in a recent study.
Hypoglycemia: IGF1-LR3 can lower blood sugar levels. This could be beneficial for people with diabetes, but it could also lead to hypoglycemia if not carefully monitored.
There are several limitations to current IGF1-LR3 research, including:
A lack of long-term safety data: Most studies of IGF1-LR3 have been small and short-term. More research is needed to determine the long-term safety of this compound.
A lack of understanding of its mechanism of action: While researchers know that IGF1-LR3 promotes growth and regeneration, they do not fully understand how it works. This makes it difficult to predict its potential side effects and to develop effective treatment protocols.
The need for more clinical trials: There is a need for more clinical trials to evaluate the safety and efficacy of IGF1-LR3 in mammals.
IGF1-LR3 is a promising new research tool with the potential to improve the treatment of a variety of conditions. However, more research is needed to fully understand its safety and efficacy. If further research confirms the potential benefits of IGF1-LR3, it could become a valuable tool for treating disease in the future.
If you are searching for where to buy IGF-LR3 online, you will come across many options. Several companies offer peptides, but unfortunately, not all prioritize quality assurance.
Research Chemical stands out in this landscape. We’re committed to delivering only the finest IGF-LR3 for sale online. When you buy peptides from us, rest assured, you’re opting for top-tier quality.
Our peptides undergo rigorous testing, verified by esteemed American third-party laboratories—labs that welcome phone or email inquiries to confirm their certificate’s authenticity. Our peptides are preserved in lyophilized form inside glass containers and maintained in cool conditions to uphold their potency.
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1. Jonker, S. S., Giraud, G. D., Chang, E. I., & Louey, S. (2019). Chronic Fetal IGF1 Administration Matches Coronary Growth to Myocardial Growth. The FASEB Journal, 33(S1), 689-3.
2. Assefa, B., Mahmoud, A. M., Pfeiffer, A. F., Birkenfeld, A. L., Spranger, J., & Arafat, A. M. (2017). Insulin-like growth factor (IGF) binding protein-2, independently of IGF-1, induces GLUT-4 translocation and glucose uptake in 3T3-L1 adipocytes. Oxidative Medicine and Cellular Longevity, 2017.
3. Gehmert, S., Wenzel, C., Loibl, M., Brockhoff, G., Huber, M., Krutsch, W., … & Gehmert, S. (2014). Adipose tissue-derived stem cell secreted IGF-1 protects myoblasts from the negative effect of myostatin. BioMed research international, 2014.
4. Li, N., Yang, Q., Walker, R. G., Thompson, T. B., Du, M., & Rodgers, B. D. (2016). Myostatin attenuation in vivo reduces adiposity, but activates adipogenesis. Endocrinology, 157(1), 282-291.
5. White, A., Stremming, J., Boehmer, B. H., Chang, E. I., Jonker, S. S., Wesolowski, S. R., … & Rozance, P. J. (2021). Reduced glucose-stimulated insulin secretion following a 1-wk IGF-1 infusion in late gestation fetal sheep is due to an intrinsic islet defect. American Journal of Physiology-Endocrinology and Metabolism, 320(6), E1138-E1147.
6. Sarem, Z., Bumke-Vogt, C., Mahmoud, A. M., Assefa, B., Weickert, M. O., Adamidou, A., … & Arafat, A. M. (2017). Glucagon decreases IGF-1 bioactivity in humans, independently of insulin, by modulating its binding proteins. The Journal of Clinical Endocrinology & Metabolism, 102(9), 3480-3490.
7. Sundgren, N. C., Giraud, G. D., Schultz, J. M., Lasarev, M. R., Stork, P. J., & Thornburg, K. L. (2003). Extracellular signal-regulated kinase and phosphoinositol-3 kinase mediate IGF-1 induced proliferation of fetal sheep cardiomyocytes. American Journal of Physiology-Regulatory, Integrative and Comparative Physiology, 285(6), R1481-R1489.
8. Kyle, A. H., Baker, J. H., & Minchinton, A. I. (2012). Targeting quiescent tumor cells via oxygen and IGF-I supplementation. Cancer research, 72(3), 801-809.
9. Tomas, F. M., Knowles, S. E., Owens, P. C., Chandler, C. S., Francis, G. L., & Ballard, F. J. (1993). Insulin-like growth factor-I and more potent variants restore growth of diabetic rats without inducing all characteristic insulin effects. Biochemical Journal, 291(3), 781-786.
Please note that the above references provide evidence for the potential benefits of PEG MGF Peptide as stated in the product description. For more in-depth information, kindly refer to these scholarly works.
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