IGF-1 LR3 is a recombinant analogue of insulin-like growth factor-1 engineered with a 13-amino acid N-terminal extension and an arginine substitution at position 3. These modifications reduce binding to IGF-binding proteins and extend its half-life to approximately 20 hours, making it a powerful tool for growth factor signaling research.
IGF-1 LR3 contains a 13-amino acid N-terminal extension and an arginine substitution at position 3 that together reduce binding to IGF-binding proteins (IGFBPs) by ~1000-fold. This dramatically increases free, bioactive IGF-1 available to activate IGF-1 receptors.
Reduced IGFBP binding extends the half-life from ~10 minutes (native IGF-1) to ~20–30 hours. IGF-1 receptor activation triggers PI3K/Akt and MAPK/ERK cascades promoting cell proliferation, survival, protein synthesis, and glucose uptake. LR3's sustained receptor occupancy makes it a powerful tool for anabolic signaling research.
Muscle cell studies demonstrate enhanced protein synthesis, satellite cell activation, and myofibrillar hypertrophy vs native IGF-1. Animal studies document significant increases in lean mass and improved regeneration after injury. LR3 is a key tool for studying unbound IGF-1 biology.
Store lyophilized at -20°C. Reconstitute with 1% acetic acid (not bacteriostatic water) for optimal solubility. Reconstituted solution stable 28 days at 2–8°C.
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