Peptide · Research Monograph · 83-amino-acid IGF-1 analog (70-aa IGF-1 + 13-residue N-terminal extension, Arg3 substitution)

IGF-1 LR3

A growth factor studied for muscle growth and recovery

IGF-1 LR3 is a long-acting form of insulin-like growth factor 1, a key driver of growth and repair — researched for muscle growth, recovery, and cell regeneration.

For laboratory research use only — not for human or animal use

Available in the Eon catalog — IGF-1 LR3 from $70.00 Certificate of analysis (PDF)

Molecular data

Molecular formulaC400H625N111O115S9
Molecular weight9117.6 Da
Sequence83 amino acids — human IGF-1(1-70) plus 13-residue N-terminal extension; Arg3 substitution
Sequence length83 residues
CAS / identifier946870-92-4
Physical formLyophilized powder
Available sizes1mg

How it works

IGF-1R Agonism

Insulin-Like Growth Factor Receptor Activation

IGF-1 LR3 (Long R3 IGF-1) is an 83-amino-acid analog of human IGF-1, carrying a 13-residue N-terminal extension and an arginine-for-glutamate substitution at position 3. It binds and activates the type 1 IGF receptor (IGF-1R), a receptor tyrosine kinase, triggering downstream PI3K/Akt and MAPK/ERK signaling.

  • Retains near-native affinity for IGF-1R
  • Activates PI3K/Akt/mTOR protein-synthesis signaling
  • Engages MAPK/ERK proliferation pathways
Reduced IGFBP Binding

Extended Bioavailability

The N-terminal extension and Arg3 substitution lower the analog's affinity for IGF-binding proteins (IGFBPs) by roughly 100- to 1,000-fold relative to native IGF-1. With less of the molecule sequestered by IGFBPs, more remains free to engage IGF-1R, giving a markedly longer functional half-life in culture systems.

  • ~100–1,000× lower IGFBP affinity
  • Greater free fraction available to the receptor
  • Longer-lasting signaling than native IGF-1
Anabolic Signaling

Protein Synthesis & Cell Survival

Through Akt activation, IGF-1 signaling stimulates mTOR/p70S6K-driven protein synthesis, inhibits GSK3β, and suppresses FoxO-mediated protein degradation — a cascade extensively characterized in skeletal-muscle and cell-culture research models.

  • Activates mTOR–p70S6K translation
  • Inhibits proteasomal/FoxO degradation
  • Promotes anti-apoptotic cell survival

What the research shows

Bioprocessing

Serum-Free Cell Culture

Long R3 IGF-1 sustains growth, viability and recombinant-protein productivity of serum-free CHO cell lines, outperforming insulin under production conditions.

Morris & Schmid 2000

Bioproduction Potency

More Potent Than Insulin

In serum-free HEK293 culture, LONG R3 IGF-I acts as a more potent growth and survival factor than insulin or native IGF-I, effective at far lower concentrations.

Voorhamme & Yandell 2006

Anabolic Signaling

Myotube Hypertrophy Pathways

IGF-1 drives skeletal myotube hypertrophy via PI(3)K/Akt/mTOR and PI(3)K/Akt/GSK3 signaling — a foundational model for anabolic growth research.

Rommel et al. 2001

Muscle Growth

IGF1–Akt/PKB Regulation

The IGF1-Akt/PKB axis controls skeletal-muscle protein synthesis and degradation, as established across transgenic and knockout genetic models.

Schiaffino & Mammucari 2011

Specification

Chemical NameLong R3 Insulin-Like Growth Factor-1 (IGF-1 LR3)
Sequence83 amino acids — human IGF-1(1-70) plus 13-residue N-terminal extension; Arg³
Molecular Weight9,117.6 Da
Molecular FormulaC₄₀₀H₆₂₅N₁₁₁O₁₁₅S₉
CAS Number946870-92-4
FormLyophilized powder
Purity≥99% (HPLC verified)
TestingThird-party HPLC, Mass Spec, Endotoxin
Storage (lyophilized)-20°C for long-term stability
Storage (reconstituted)2–8°C, use within 14 days
SolubilitySterile acidified water or bacteriostatic water
COAIncluded with every order

Frequently asked questions

What is IGF-1 LR3 and how does it differ from native IGF-1?

IGF-1 LR3 (Long R3 IGF-1) is an engineered 83-amino-acid analog of human insulin-like growth factor 1. It adds a 13-residue N-terminal peptide extension and replaces the glutamic acid at position 3 with arginine. These changes dramatically reduce binding to IGF-binding proteins (IGFBPs) while preserving affinity for the IGF-1 receptor, so it stays active far longer than native IGF-1 in culture.

Why is IGF-1 LR3 used in cell culture?

Because it resists IGFBP sequestration and signals potently through IGF-1R, IGF-1 LR3 is a widely used serum-free media supplement. Studies show it supports growth, viability and recombinant-protein productivity of CHO and HEK293 cell lines at concentrations far below those required for insulin.

What signaling pathways does IGF-1 LR3 activate?

By activating the IGF-1 receptor tyrosine kinase, it engages the PI3K/Akt/mTOR pathway (protein synthesis and cell survival) and the MAPK/ERK pathway (proliferation). In skeletal-muscle models, the IGF1-Akt axis also suppresses protein degradation via FoxO and GSK3β.

How should IGF-1 LR3 be stored and reconstituted?

Store the lyophilized powder at -20°C, protected from moisture and light. Reconstitute with sterile acidified water or bacteriostatic water; once in solution, keep at 2–8°C and use within roughly two weeks. Avoid repeated freeze–thaw cycles to preserve activity.

Is this product intended for human use?

No. Research-grade IGF-1 LR3 sold here is strictly for in vitro laboratory research and analytical applications. It is not a drug and is not intended for human or veterinary use, consumption, or any clinical application.

Literature

  • PubMed Effects of insulin and LongR(3) on serum-free Chinese hamster ovary cell cultures expressing two recombinant proteins 2000 — Morris AE, Schmid J
  • PubMed LONG R3IGF-I as a more potent alternative to insulin in serum-free culture of HEK293 cells 2006 — Voorhamme D, Yandell CA
  • PubMed Mediation of IGF-1-induced skeletal myotube hypertrophy by PI(3)K/Akt/mTOR and PI(3)K/Akt/GSK3 pathways 2001 — Rommel C et al.
  • PubMed Regulation of skeletal muscle growth by the IGF1-Akt/PKB pathway: insights from genetic models 2011 — Schiaffino S, Mammucari C

For laboratory research use only. Not a drug, supplement, or medical product; not for human or animal use. All findings referenced are from published preclinical/laboratory research.