IGF-1 LR3

Overview

IGF-1 LR3 is a recombinant analog of human IGF-1 with two key modifications: an arginine substitution at position 3 (R3) and a 13–amino acid N-terminal extension (Long, derived from methionyl porcine GH). These changes reduce binding affinity for the IGF binding proteins (IGFBPs), which extends free, bioavailable IGF-1 in research systems.

Research Background

IGF-1 LR3 has been studied in research on cellular proliferation, muscle and tendon biology, and somatotropic axis pharmacology. Its altered IGFBP binding profile makes it a useful tool for studying IGF-1 receptor activation independent of binding-protein dynamics.

Storage & Handling

Store lyophilized peptide at -20°C for long-term stability. Once reconstituted with bacteriostatic water, store at 2–8°C and use within recommended timeframes. Handle under sterile laboratory conditions and avoid repeated freeze-thaw cycles.

Disclaimer:
This product is for laboratory research use only. It is not intended for human or animal consumption or for use in any diagnostic, therapeutic, or clinical applications.

IGF-1 LR3 binds the IGF-1 receptor (IGF-1R), a receptor tyrosine kinase, with affinity comparable to native IGF-1. Receptor activation triggers PI3K/Akt and Ras/MAPK signaling, driving anabolic and proliferative responses. The reduced affinity for IGFBP-1, -3, -5 and -6 means more peptide remains free in solution and available to bind IGF-1R in research conditions, producing prolonged signaling compared with native IGF-1.

IGF-1 LR3 is studied in research on muscle and tendon biology, cellular proliferation, IGF-1 receptor pharmacology, and somatotropic axis signaling. It is a reference analog in IGF-axis research.