IGF-LR3
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About IGF-LR3
IGF-1 LR3 (Long R3 Insulin-like Growth Factor 1) is a synthetic 83-amino acid analog of human IGF-1 with an arginine substitution at position 3 and a 13-amino acid N-terminal extension. These modifications reduce IGF binding protein (IGFBP) affinity, resulting in significantly enhanced bioavailability and a prolonged half-life compared to native IGF-1. Extensively studied for cell proliferation, muscle hypertrophy, and anti-apoptotic signaling in preclinical models.
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Published Study Findings on IGF-LR3
Detailed Research & Citations
In-depth findings from peer-reviewed preclinical and clinical studies
IGF-1 LR3 (Long R3 Insulin-like Growth Factor 1) is a synthetic 83-amino acid analog of human IGF-1 featuring an arginine substitution at position 3 and a 13-amino acid N-terminal extension peptide. These structural modifications dramatically reduce binding to IGF binding proteins (IGFBPs), resulting in 2-3x greater potency and significantly prolonged bioavailability compared to native IGF-1. It is one of the most extensively studied growth factor analogs in preclinical research.
Enhanced IGF-1 Receptor Activation
IGF-LR3 binds the IGF-1 receptor with similar affinity to native IGF-1 but with dramatically reduced IGFBP sequestration, resulting in a much larger fraction of free, biologically active peptide. This drives sustained PI3K/Akt and MAPK/ERK signaling cascades critical for cell survival, proliferation, and differentiation.
European Journal of Biochemistry (1990)Skeletal Muscle Growth & Satellite Cell Activation
IGF-LR3 is a potent stimulator of skeletal muscle hypertrophy, promoting myoblast proliferation, satellite cell activation, and myofiber protein synthesis. In preclinical models, systemic and local IGF-LR3 administration produced significant increases in muscle mass and cross-sectional fiber area.
Proceedings of the National Academy of Sciences (1998)Cell Survival & Anti-Apoptotic Signaling
Through sustained PI3K/Akt pathway activation, IGF-LR3 phosphorylates and inactivates pro-apoptotic factors including BAD, caspase-9, and Forkhead transcription factors. This provides robust anti-apoptotic protection to multiple cell types including neurons, cardiomyocytes, and pancreatic beta cells.
European Journal of Biochemistry (1990)Extended Bioavailability
The Arg3 substitution and 13-amino acid N-terminal extension reduce IGFBP binding by >100-fold compared to native IGF-1, dramatically increasing the circulating free fraction. This yields an effective half-life of approximately 20-30 hours versus ~15 minutes for native IGF-1.
European Journal of Biochemistry (1990)Wound Healing & Tissue Regeneration
IGF-LR3 accelerates wound healing by stimulating fibroblast proliferation, collagen synthesis, and keratinocyte migration. It promotes angiogenesis through VEGF upregulation and has demonstrated enhanced bone fracture repair in preclinical models.
Growth Hormone & IGF Research (1996)Glucose Uptake & Metabolic Effects
IGF-LR3 stimulates glucose uptake in skeletal muscle through GLUT4 translocation via PI3K/Akt signaling, independent of insulin receptor activation. It also promotes amino acid uptake and net protein synthesis while inhibiting protein degradation.
European Journal of Biochemistry (1990)View All 3 Sources
All findings above are sourced from peer-reviewed journals for educational reference. This product is for research purposes only — not for human consumption. Preclinical results may not translate to human outcomes.
Chemical Identity
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