An extended analogue of insulin-like growth factor-1 with enhanced stability and reduced IGF binding protein affinity. It is studied in research on cell proliferation, receptor binding kinetics, and metabolic signaling with prolonged bioactivity compared to native IGF-1.
IGF-1 LR3, also known as Long R3 IGF-1, is an 83-amino-acid analogue of insulin-like growth factor 1. It differs from native IGF-1 by an arginine substitution at position 3 and a 13-amino-acid N-terminal extension, changes that have been used in research to study altered receptor interaction, reduced binding to IGF-binding proteins, and extended activity in experimental systems.
IGF-1 LR3 is studied for its activity at the IGF-1 receptor, where receptor engagement is used to examine intracellular signaling related to growth, survival, and metabolic regulation. Because this analogue has reduced affinity for IGF-binding proteins compared with native IGF-1, it is commonly used in research involving receptor signaling duration, cell growth pathways, anabolic signaling models, and IGF-axis biology.
Research on IGF-1 LR3 developed from broader work on insulin-like growth factor biology and the role of IGF-binding proteins in regulating peptide availability. Longer-chain analogues such as LR3 were designed to help researchers study how structural modifications change receptor activity, binding-protein interaction, and functional persistence in laboratory models.
For research use only. Not for human or veterinary use. Detailed storage guidelines →