IGF-1 LR3 vs IGF-1 DES: Structural Differences in Research

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INTRODUCTION TO INSULIN-LIKE GROWTH FACTOR (IGF-1)

VARIANTS OF IGF-1: IGF-1 LR3 AND IGF DES 1,3

IGF-1 exists in two main variants: IGF-1 LR3 and IGF DES 1,3. IGF-1 LR3 is a modified IGF-1 with an extended amino acid sequence that has 13 additional amino acids at the N-terminus and a substitution of arginine for glutamic acid at position 3. IGF DES 1,3 is a truncated IGF-1 that is missing the first 3 amino acids at the N-terminus.

IGF-1 LR3 VS IGF DES 1,3 REVIEW

Although functionally related, IGF-1 LR3 and IGF DES 1,3 are two different compounds with different structures and degree of actions. This article will try to explore the thin line that separates these closely related compounds so we can identify them uniquely for further research.

Additional information will be posted on where to buy them for any biological engineering or research purpose.

Key Differences Between IGF-1 LR3 and IGF-1 DES

IGF-1 LR3 stands for Insulin-like Growth Factor-1, Long Arginine 3. The compound is a non-natural or artificial protein. It is a longer version of Insulin-like Growth Factor-1 (IGF-1). Structurally IGF-1 LR3 is different from its patent compound because of the presence of Arginine instead of glutamic acid at the 3rd position of its amino acid sequence and 13 extra amino acids at the N-terminus. This makes it loosely bound to Insulin-like Growth Factor Binding Proteins (IGFBPs). IGF-1 LR3 and IGF DES 1,3 are two groups of IGF-1 variants, each with distinct structural and functional properties.

The significance of this weak binding to IGFBPs is that the compound can exert more pharmacological action in animal subjects since IGFBPs decrease the pharmacological activity of hormones that are strongly bound to it. IGF-1 LR3 has a longer half-life compared to the base form of IGF-1, allowing for a longer duration of activity in the body.

IGF DES 1,3 stands for Insulin-like Growth Factor Desamino 1,3. It is a natural variant of IGF-1 and extracted from human brain, porcine uterus and bovine colostrum. The compound lacks the first 3 amino acids at the N-terminus which are present in the parent compound.

IGF-1 LR3 VS IGF DES 1,3 MOA (MECHANISM OF ACTION) AND HALF LIFE

IGF-1 LR3 Mechanism of Action & Half-Life

To get even better results than their parent IGF-1, IGF DES 1,3 and IGF-1 LR3 were used separately on animal subjects for trials. It was observed that they bind to Insulin-like Growth Factor Binding Protein (IGFBP) in varying degree. IGF-1 LR3 stays in the host’s body for 20-30 hours. That’s a long half-life, it can exert its pharmacological actions in the host’s body for the same duration.

IGF Des 1, 3 on the other hand binds to receptors of cells that are already deteriorated due to production of lactic acid during exercise. That means they can be used and can quickly bind to these receptors of worn-out cells and trigger cellular division and hyperplasia during exercise.

IGF-1 LR3 AND IGF DES 1,3 EFFECTS

Effects of IGF-1 LR3

The effects of IGF-1 LR3 and IGF DES 1,3 are different due to their structural variations and half-lives.

IGF-1 DES Mechanism of Action & Half-Life

IGF-1 LR3 vs IGF-1 DES: Key Differences at a Glance

The following table summarizes the primary structural, pharmacokinetic, and research application differences between IGF-1 LR3 and IGF-1 DES:

Property IGF-1 LR3 IGF-1 DES
Structure +13 amino acids at N-terminus; Arg substitution at position 3 Missing first 3 N-terminal amino acids (Gly-Pro-Glu deletion)
Half-Life 20–30 hours (systemic, extended) 20–30 minutes (localized, rapid)
IGFBP Binding Reduced β€” circulates freely longer Significantly reduced β€” high local bioavailability
Receptor Affinity Standard IGF-1 receptor binding
Primary Research Use
Signaling Pathway PI3K/Akt/mTOR; sustained systemic activation PI3K/Akt/mTOR + MAPK; rapid localized activation
Administration (Research)

All compounds are for in-vitro and preclinical laboratory research use only (RUO). Not for human or veterinary use.

IGF DES 1,3 VS IGF-1 LR3 RESULTS

IGF-1 LR3 Research Results

Specific muscles of the rats were dosed with a measured vial of the compound.

Effects of IGF-1 DES

IGF-1 Des 1,3 was administered locally to a part of the body for development of only that part, IGF-1 LR3 was administered to a part of an animal subject for overall body effect or development. Also IGF-1 LR3 lasts more than 20 hours in the host’s body while IGF Des 1,3 has 30 minutes half life.

Low blood sugar was recorded after serial administrations of IGF Des 1,3 to animal subjects. Both compounds also enhanced proliferation of cancerous cells in rats with cancerous tumours. IGF Des 1,3 caused reversed testicular atrophy in male Rats with withered testicles.

IGF-1 is also linked to atherosclerosis and vascular aging, studies have shown its role in modulating glutathione peroxidase expression and activity in vascular endothelial cells. But misuse of IGF-1 in sports is a big concern and we need to develop effective detection methods to prevent abuse and ensure fair competition.

WHERE TO BUY IGF DES 1,3 and IGF-1 LR3

IGF-1 LR3 and IGF DES 1,3 are available at Loti Labs for in-vitro and preclinical research use. Purchase IGF-1 LR3 from Loti Labs β€” supplied in 1mg vials, β‰₯98% purity verified by HPLC.

References

  1. Philippou, A., Maridaki, M., Halapas, A., & Koutsilieris, M. (2014). Journal of Muscle Research and Cell Motility, 35(1), 1-10. https://doi.org/10.1007/s10974-013-9371-8
  2. Le Roith, D., Bondy, C., Yakar, S., Liu, J.-L., & Butler, A. A. (2001). The somatomedin hypothesis: 2001. Endocrine Reviews, 22(1), 53-74. https://doi.org/10.1210/edrv.22.1.0428
  3. Philippou, A., Halapas, A., Maridaki, M., & Koutsilieris, M. (2007). IGF-1 and exercise: A review of the current evidence of the effects of exercise on IGF-1 levels and actions. Hormones, 6(2), 87-95. https://doi.org/10.14310/horm.2002.10804. Clemmons, D. R. (2004). IGF-binding proteins: Regulators of IGF actions. Journal of Molecular Endocrinology, 32(1), 13-24. https://doi.org/10.1677/jme.1.01578
  4. Musaro, A. (2013). Biochemical Society Transactions, 41(6), 1451-1456. https://doi.org/10.1042/BST20130135
  5. Le Roith, D. (2003). IGFs. The New England Journal of Medicine, 336(9), 633-640. https://doi.org/10.1056/NEJM199702273360906
  6. Philippou, A., Maridaki, M., & Koutsilieris, M. (2010). Cell Communication and Signaling, 8, 15. https://doi.org/10.1186/1478-811X-8-15
  7. World Anti-Doping Agency. (2024). Prohibited List. Retrieved from https://www.wada-ama.org/en/prohibited-list
  8. Lu, H., Huang, D., Saederup, N., Charo, I. F., Ransohoff, R. M., & Zhou, L. (2011). FASEB Journal, 25(1), 358-369. https://doi.org/10.1096/fj.10-171579
  9. Scavo, L. M., Karas, M., Murray, M., & Leroith, D. (2004). IGF-I stimulates both cell growth and lipogenesis during differentiation of human mesenchymal stem cells into adipocytes. Journal of Clinical Endocrinology & Metabolism, 89(7), 3543-3553. https://doi.org/10.1210/jc.2003-031842

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