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What Is the Molecular Structure of IGF-1 LR3?

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Published 2026-07-11 · REVIVE Peptides Research Desk · 2 min read
Short answer: IGF-1 LR3 is an 83-amino-acid synthetic analog of the 70-amino-acid native human IGF-1 molecule. The extra length comes from a 13-amino-acid N-terminal extension combined with a substitution of arginine for glutamic acid at position 3 (Arg3) — the modification that gives the compound its "Long Arg3" name.

Native IGF-1 is a compact, 70-amino-acid single-chain polypeptide folded by three internal disulfide bonds into a structure similar to proinsulin. IGF-1 LR3 keeps that same core folded structure but adds a 13-residue extension to the N-terminal end of the chain, bringing the total residue count to 83, and replaces the glutamic acid normally found at position 3 with arginine.

Neither modification changes the region of the molecule that binds the IGF-1 receptor, which is why IGF-1 LR3 retains receptor-binding activity comparable to native IGF-1 in published in-vitro research. What the structural changes do alter is the molecule's surface chemistry near the N-terminus, which is the region primarily responsible for binding to IGF-binding proteins (IGFBPs) in circulation.

This structural summary reflects general, well-established peptide chemistry and is provided for research-education purposes only. IGF-1 LR3 is listed on revivelab.ae as the IGF-1 LR3 pack (1 mg); this page describes the compound and gives no guidance on its use.

IGF-1 LR3 Pack 1 mg — REVIVE LAB UAE
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