IGF-1 LR3 — Long Arg3 Insulin-like Growth Factor-1 Research Compound

Catalog ID: IGF1 | CAS: 946870-92-4 | Sequence: Gly-Pro-Ala-Met-Arg-Gly-Phe-Tyr-Pro-Ser-Ser-Ser-Arg-Leu-Tyr-Ala-Leu-Val-Asp-Ala-Leu-Glu-Gln-Leu-Ala-Gln-Phe-Val-Cys-Gly-Asp-Arg-Gly-Phe-Tyr-Phe-Ser-Arg-Lys-Asn-Val-Asp-Gln-Cys-Cys-Phe-Arg-Ser-Cys-Asn-Gly-Tyr-Arg-Gly-Ser-Ser-Ser-Arg-Arg-Gly-Phe-Tyr-Ser-Phe-Ser-Thr-Pro-Ser-Lys |

Molecular Formula: C₄₀₀H₆₂₅N₁₁₁O₁₁₅S₉

Compound Overview

IGF-1 LR3 is a recombinant synthetic analog of human insulin-like growth factor-1 (IGF-1), modified to extend biological half-life and reduce binding affinity to IGF-binding proteins (IGFBPs).
The analog features a **13-amino-acid N-terminal extension** and a **substitution of arginine for glutamic acid at position 3**, enhancing its research stability in cell-culture conditions.
For laboratory research use only — not for human consumption or therapeutic application.

Molecular Characteristics

• Synonyms: Long Arg3 IGF-1; IGF-1 LR³; Insulin-like Growth Factor Analog
• CAS Number: 946870-92-4
• Sequence: Modified IGF-1 peptide (83 amino acids, with Arg³ substitution and N-terminal extension)
• Molecular Formula: C₄₀₀H₆₂₅N₁₁₁O₁₁₅S₉
• Molecular Weight: ≈ 9117.9 g/mol
• Purity: ≥ 98% (HPLC verified)
• Formulation: Lyophilized peptide powder

Physical Properties

• Appearance: White to off-white lyophilized powder
• Solubility: Sterile water, PBS, or acetic acid (for research use only)
• Container: Sterile sealed vial

Storage & Stability

• Unreconstituted: Store at −20 °C, protected from light and moisture.
• Reconstituted: Aliquot and store at −20 °C; avoid repeated freeze–thaw cycles.

Research Context

IGF-1 LR3 is used in controlled in vitro and in vivo experiments exploring **cell proliferation**, **metabolic signaling**, and **IGF receptor interactions**.
It has been a key research analog in studies examining **insulin-like growth factor receptor (IGF-1R) binding dynamics**, **Akt/PI3K pathway activation**, and **cell growth mechanisms**.
Its structure makes it less susceptible to binding protein inhibition, allowing researchers to study **direct peptide-receptor signaling** and **extended receptor occupancy models**.