
IGF-1 LR3 (Insulin-like Growth Factor-1 Long R3) is a synthetic analog of endogenous IGF-1, engineered with an 83 amino acid sequence that includes a 13 amino acid N-terminal extension and an arginine substitution at position 3. These modifications significantly extend its half-life and potency compared to native IGF-1. Each vial contains 1mg of research-grade IGF-1 LR3.
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About this compound
IGF-1 LR3 (Insulin-like Growth Factor-1 Long R3) is a recombinant analogue of endogenous IGF-1 with an N-terminal methionine extension and a glutamic acid→arginine substitution at position 3. This R3 modification reduces binding affinity to IGF-binding proteins (IGFBP-1 through -6) by over 1000-fold, extending the plasma half-life from ~12 minutes to 20–30 hours and dramatically increasing bioavailability at peripheral tissue receptors. It is the preferred research tool for studying mTOR-driven protein synthesis, muscle satellite cell biology, anti-catabolic mechanisms, and neurotrophy — independently of hepatic IGFBP sequestration.


Research Data
Research Snapshot — IGF-1 LR3
Key Mechanisms & Pathways
- PI3K → Akt → mTORC1Phosphorylates S6K1 and 4E-BP1 — the two rate-limiting steps in ribosomal biogenesis and protein translation initiation.
- Ras → MEK → ERKDrives G1→S cell cycle progression via cyclin D1; regulates DNA replication and myoblast differentiation.
- FOXO SuppressionAkt phosphorylates FOXO1/3a, preventing transcription of atrophy genes MuRF1 and Atrogin-1 — blocking muscle proteolysis.
- Satellite Cell ActivationIGF-1R on muscle stem cells drives proliferation and differentiation into new myofibres — adding myonuclei.
- IGFBP-3 BypassR3 substitution reduces IGFBP binding affinity by >1000×, extending half-life from 12 min to 20–30 hours.
- NeurotrophyPromotes neuron survival, axonal regeneration and oligodendrocyte differentiation in CNS injury models.
Preclinical & Clinical Research Summary
| Research Area | Key Finding | Source |
|---|---|---|
| Muscle Hypertrophy | +25% muscle mass in 7 days via local injection in rat hindlimb — without systemic GH. | Coleman ME et al., 1995 — J Biol Chem |
| Satellite Cell Activation | 3.5× satellite cell proliferation vs. native IGF-1 at equal molar doses in human myoblasts. | Foulstone EJ et al., 2003 — J Cell Physiol |
| Anti-Catabolism | Significantly attenuated muscle protein catabolism and nitrogen loss in burn injury models. | Herndon DN et al., 1999 — Ann Surg |
| Neuronal Survival | Neurotrophic — extended half-life optimal for ALS, neuropathy and axonal regeneration models. | Ishii DN et al., 1994 |
References
- Coleman ME et al. "Myogenic vector expression of insulin-like growth factor I stimulates muscle cell differentiation and myofiber hypertrophy." J Biol Chem, 1995;270(20):12109–12116.
- LeRoith D et al. "The role of the insulin-like growth factor-I receptor in cancer." Ann N Y Acad Sci, 2003;995:58–68.
- Foulstone EJ et al. "Role of insulin-like growth factor binding protein-3 in the insulin-like growth factor axis of human skeletal muscle." J Cell Physiol, 2003;196(2):229–240.
- Singleton JR et al. "Insulin-like growth factor I signaling in motor neuron disease." Brain Res, 2000;888(2):241–248.
Specifications
- Sequence
- IGF-1 with N-terminal Met extension + Arg³ substitution
- Molecular Weight
- 9117 Da
- Amino Acids
- 83
- Half-Life
- 20–30 hours
- Vial Size
- 1mg
- Purity
- ≥99% (HPLC)
- Form
- Lyophilized powder
- Reconstitution
- Bacteriostatic water (0.9% benzyl alcohol)
- Storage
- Sealed: 2–8 °C · Reconstituted: 2–8 °C, use within 28 days
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For laboratory and in-vitro research use only. Not for human or veterinary use, not for consumption. By purchasing, you confirm you are a qualified researcher and accept full responsibility for compliant handling and disposal. Read the full disclaimers.




