Molecular Structure of IGF-1 LR3 Peptide
IGF-1 LR3 peptide is a synthetic, 83-amino-acid recombinant analog of human Insulin-like Growth Factor-1. The sequence incorporates a critical substitution of Arginine for Glutamic acid at position 3, alongside a 13-amino-acid N-terminal extension peptide. This specific structural reconfiguration significantly reduces its affinity for IGF-binding proteins (IGFBPs). As a result, the active presence of IGF-1 LR3 peptide in cell culture models and receptor assays is markedly prolonged compared to native IGF-1, extending its effective analytical half-life to 20–30 hours.
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In vitro testing requires precise vehicle selection to prevent aggregation. Lyophilized IGF-1 LR3 peptide dissolves efficiently in sterile 0.1M acetic acid or dilute hydrochloric acid (10 mM HCl) to yield concentrations ranging between 0.1 mg/mL and 1.0 mg/mL. Maintaining a slightly acidic pH environment ensures stable molecular dispersion, preventing precipitation during automated micro-pipetting, liquid handling, or downstream cellular exposure assays.
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The lyophilized solid remains stable for short-term handling at controlled ambient laboratory temperatures ($15^\circ\text{C}$ to $25^\circ\text{C}$). For extended storage, the dry powder must be held at $-20^\circ\text{C}$ or $-80^\circ\text{C}$ in a desiccated environment protected from light exposure. Post-reconstitution, liquid aliquots should be refrigerated at $2^\circ\text{C}$ to $8^\circ\text{C}$ and used within defined experimental timelines to avoid hydrolytic cleavage.
Laboratory Compliance for IGF-1 LR3 Peptide
When sourcing IGF-1 LR3 peptide from AU Peptides Store, research institutions receive reference-grade reagents synthesized strictly for in vitro cellular study and analytical testing. Every batch undergoes third-party verification via high-performance liquid chromatography (HPLC) and mass spectrometry to confirm mass accuracy, amino acid alignment, and complete removal of synthetic byproducts. All shipments include a complete Certificate of Analysis (COA).
