IGF-1 LR3 is a synthetic analog of human insulin-like growth factor-1 engineered with a 13-amino-acid N-terminal extension and a glutamic acid substitution at position 3. These modifications significantly reduce its binding affinity to IGF binding proteins.
This modification extends the peptide’s half-life from the minutes observed with native IGF-1 to several hours and increases systemic bioavailability.
The extended circulation time allows once-daily administration protocols to be studied in research settings. Unlike native IGF-1, which requires more frequent administration, IGF-1 LR3 can maintain more stable plasma levels throughout the day.
The peptide exhibits anabolic and metabolic activity through interaction with the IGF-1 receptor.
Studies of IGF-1 and its analogs have demonstrated effects related to cellular growth, protein synthesis, and metabolic regulation. Due to its insulin-like properties, particular attention should be paid to blood glucose during initial research and tolerance-assessment phases.