// Insulin-Like Growth Factor Research
IGF-1 and its variants — LR3, DES, and MGF — are among the most studied peptides in growth and recovery research. A comprehensive guide to the science.
This site is for research and educational purposes only. IGF-1 variants are not approved by the FDA for human use outside specific medical conditions. Nothing here constitutes medical advice. Consult a licensed physician.
// IGF-1 Variants
A modified analog with an arginine substitution at position 3 and an N-terminal extension. The extension significantly reduces binding to IGF-binding proteins, dramatically extending half-life and bioavailability compared to native IGF-1.
A truncated form of IGF-1 lacking the first three amino acids of the N-terminus. This truncation paradoxically increases receptor binding affinity 10-fold over native IGF-1, making it the most potent variant — but with a much shorter half-life.
A splice variant of IGF-1 produced locally in muscle tissue in response to mechanical stress and damage. MGF activates satellite cells (muscle stem cells) and plays a key role in muscle repair and hypertrophy signaling.
// Signaling Pathway
// Research Areas
IGF-1, LR3, DES, and MGF each occupy a different niche within the same signaling system. Understanding their distinct half-lives, binding properties, and tissue selectivity is key to understanding the research literature.
PubMed Research →