IGF-1 LR3 1MG

IGF-1 LR3 1MG

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The IGF-1 LR3 1MG for sale here are intended for laboratory and research use only, unless otherwise explicitly stated. They are not intended for human ingestion or for use in products that may be ingested.
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What Is IGF-1 LR3 1MG?

IGF-1 LR3, also known as insulin-like growth hormone long arginine 3, is a synthetic peptide derived from IGF-1. IGF-1 is produced in response to the stimulation of growth hormone by liver. It promotes cell differentiation and proliferation, protein synthesis and muscle growth.

The difference between the two lies in their structure. IGF-1 consists of 70 amino acids while IGF-1 LR3 has 83 amino acids as it contains an additional 13 amino acids at the N terminus. Further, it has a substitution of arginine for glutamic acid at the third position.

These subtle changes contribute to the longer half-life, prolonged duration of action and potency of IGF-1 LR3. Due to its beneficial properties, it gained the attention of various scientists and researchers. On our website, IGF-1 LR3 for sale is available for research and educational purposes.

Structure Of IGF-1 LR3 1MG

structure

Synonyms: Insulin-like growth factor long chain R3, Long-(arg3)insulin-like growth factor-i
Molecular Formula: C400H625N111O115S9
Molecular Weight: 9117.60 g/mol
Sequence: MFPAMPLSSL FVNGPRTLCG AELVDALQFV CGDRGFYFNK PTGYGSSSRR APQTGIVDEC CFRSCDLRRL EMYCAPLKPA KSA
CAS Number: 143045-27-6
PubChem SID: 381123731

IGF-1 LR3 1MG Uses In Research

1. IGF-1 LR3 and Muscle Healing

Insulin-like growth hormone is involved in muscle regeneration and healing. It stimulates the proliferation and differentiation of myoblast. One study found that direct recombinant IGF-1 LR3 administration at days 2, 5, and 7 accelerated muscle healing in mice with strain-injured muscles [1].

Another study replicated the results when researchers evaluated the IGF-1 effects on muscle damage in mice. They found an increase in muscle regeneration and healing in terms of fast twitching in mice treated with IGF-1 compared to the control group. Moreover, IGF-1 was observed to be associated with an increased number of regenerating myofibres on the treated site [2]. Muscle mass and strength decrease with advancing age, and so does the ability to regenerate. The research shows that IGF-1 treatment in the elderly can preserve lean muscle mass [3].

2. IGF-1LR3 and Hypertrophy

Myostatin, also known as growth differentiation factor 8, is an important protein that regulates muscle growth and development. It negatively impacts muscle mass by inhibiting muscle growth and protein synthesis. It prevents unwanted hypertrophy and promotes muscle healing following injury.

Insulin-like growth factor 1, as an inhibitor of myostatin, prevents muscle breakdown in conditions like muscular dystrophy [4, 5]. Further, IGF-1 stimulates the proliferation of myoblast, thus causing an increase in the number of muscle cells (hyperplasia). IGF-1 LR3 due to its increased potency has a much greater effect on cell proliferation compared to IGF-1 [6].

3. IGF-1 LR3 and Diabetes

IGF-1 has a significant effect on glucose regulation. It binds to IGF-1 and insulin receptors that mediate glucose uptake from blood to the liver and muscle cells. This results in decreased blood sugar levels. Research shows that IGF-LR3 is associated with a significant increase in glucose uptake and decrease blood glucose levels [7, 8].

In one study, IGF-1 administration in rats with diabetic cardiomyopathy decreased myocardial apoptosis, oxidative stress, inflammation, interstitial fibrosis and metabolic abnormalities. Further, it caused an increase in the activation of the Akt/GSK-3β pathway, indicating that IGF-1 could be a potential therapy for diabetic cardiomyocytes [9].

4. IGF-1 LR3 and Bone Health

Insulin-like growth hormone is a critical mediator of bone health. In a cross-sectional study, 482 postmenopausal women with diabetes and 482 postmenopausal without diabetes were recruited in a bone health survey. The researchers found that IGF-1 levels were lower in diabetic women with vertebral fractures, suggesting IGF-1 as a marker for the severity of vertebral fractures [10].

A review of 39 clinical studies found that IGF-1 and growth hormone administration showed increased bone resorption and bone formation. Furthermore, IGF-1 enhanced bone healing and promoted rapid improvement in patients with Tibia and hip fractures [11].

5. IGF-1LR3 and Cognition

Research shows that IGF-1 protect the loss of neurons by stimulating cellular process that promotes cell survival. In one study, long-term IGF-1 administration in old age animals increased neurogenesis, vascular density and glucose utilization in brain parts responsible for memory and learning [12].

One study conducted on rats found IGF-1 administration to increase excitatory synaptic transmission in CA1 by 40%. It also found that the increased post-synaptic mechanism was due to the involvement of α-amino-3-hydroxyl-5-methyl-4-isoxazolepropionate (AMPA) receptors. Further, it revealed that PI3k inhibitors blocked the enhanced post-synaptic transmission, suggesting this effect might be dependent on PI3k activation [13].

6. Summary:

GF-LR3 is a synthetic analog of insulin-like growth hormone. Due to the structural difference, it has a longer half-life and prolonged duration of action. It might be involved in muscle healing, bone health and improving insulin sensitivity. Further research is needed to confirm these effects. At Element Sarms, IGF-LR3 purchase is available for research purposes. Only buy IGF-LR3 if you are a licensed researcher.

Referenced Citations

  1. Laumonier, T. and J. Menetrey, Muscle injuries and strategies for improving their repair. Journal of Experimental Orthopaedics, 2016. 3.
  2. Kasemkijwattana, C., et al., Use of Growth Factors to Improve Muscle Healing After Strain Injury. Clinical Orthopaedics and Related Research®, 2000. 370.
  3. Cappola, A.R., et al., Association of IGF-I levels with muscle strength and mobility in older women. J Clin Endocrinol Metab, 2001. 86(9): p. 4139-46.
  4. Schiaffino, S. and C. Mammucari, Regulation of skeletal muscle growth by the IGF1-Akt/PKB pathway: insights from genetic models. Skelet Muscle, 2011. 1(1): p. 4.
  5. Li, N., et al., Myostatin Attenuation In Vivo Reduces Adiposity, but Activates Adipogenesis. Endocrinology, 2016. 157(1): p. 282-91.
  6. Tomas, F.M., A.B. Lemmey, L.C. Read, and F.J. Ballard, Superior potency of infused IGF-I analogues which bind poorly to IGF-binding proteins is maintained when administered by injection. J Endocrinol, 1996. 150(1): p. 77-84.
  7. Assefa, B., et al., 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. 2017: p. 3035184.
  8. White, A., et al., 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, 2021. 320(6): p. E1138-E1147.
  9. Wang, C.Y., X.D. Li, Z.H. Hao, and D. Xu, Insulin-like growth factor-1 improves diabetic cardiomyopathy through antioxidative and anti-inflammatory processes along with modulation of Akt/GSK-3β signaling in rats. kjpp, 2016. 20(6): p. 613-619.
  10. Ardawi, M.-S.M., et al., Increased serum sclerostin and decreased serum IGF-1 are associated with vertebral fractures among postmenopausal women with type-2 diabetes. Bone, 2013. 56(2): p. 355-362.
  11. Locatelli, V. and V.E. Bianchi, Effect of GH/IGF-1 on Bone Metabolism and Osteoporsosis. Int J Endocrinol, 2014. 2014: p. 235060.
  12. Sonntag, W.E., M. Ramsey, and C.S. Carter, Growth hormone and insulin-like growth factor-1 (IGF-1) and their influence on cognitive aging. Ageing Research Reviews, 2005. 4(2): p. 195-212.
  13. Ramsey, M.M., et al., Functional Characterization of Des-IGF-1 Action at Excitatory Synapses in the CA1 Region of Rat Hippocampus. Journal of Neurophysiology, 2005. 94(1): p. 247-254.

Certificate of Analysis (COA)

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High Performance Liquid Chromatography (HPLC)

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Mass Spectrometry (MS)

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IGF1 LR3 allows for many of the growth-promoting effects of growth hormone insulin-like growth factors also know as IGF's. IGF-1 LR3 comprises a family of peptides (protiens) that play important roles in mammalian growth and development. IGF1 LR3 is also known as Long R3 IGF-1 or Insulin-Like Growth Factor-I Long Arg3. The Long R3 IGF-1 version is significantly more potent than regular IGF-1. The enhanced potency is due to the decreased binding of IGF1 LR3 to all known IGF binding proteins. These binding proteins normally inhibit the biological actions of IGF's therefore IG-1 LR3 has been shown to have increased efficacy and function . This IGF-1 LR3 analog of IGF-1 has been created with the purpose of increasing the biological activity of the IGF peptide. IGF1 LR3 is also known as Long R3 IGF-1 or Insulin-Like Growth Factor-I Long Arg3. This is a human recombinant, single, non-glycosylated, polypeptide chain containing 83 amino acids and having a molecular mass of 9200 Daltons. IGF1 mediates many of the growth-promoting effects of growth hormone (GH; MIM 139250). The LR3 is a long-term analog of human IGF-1, specifically designed and manufactured for mammalian cell culture to support large-scale manufacturing of recombinant biopharmaceuticals. Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin'. IGF-1 LR3 is the primary protein involved in responses of cells to growth hormone (GH): that is, IGF-I is produced in response to GH and then induces cellular activities. One such example is muscle growth or hyperplasia. This compound also makes the human body more sensitive to insulin. It is the most potent growth factor found in the human body. IGF-1 causes muscle cell hyperplasia, which is an actual splitting and forming of new muscle cells. The most effective form of IGF-1 is considered to be IGF-1 LR3. This formula has been chemically altered to avoid binding to proteins in the human body, and to increase the half life, approximately 20-30 hours.
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