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

IGF-1 LR3

IGF-1 analog · serum-free culture supplement

Also known as Long R3 IGF-1 · LR3 IGF-1

IGF-1 LR3 is a modified version of insulin-like growth factor 1. It is 13 amino acids longer than the natural version and has one amino acid swapped at position 3. That swap keeps it from binding the carrier proteins that normally hold IGF-1 in check, which makes it last much longer. Studies have measured cell growth signaling and protein production in culture.

Formula
C400H625N111O115S9
Mol. weight
9117.6 Da
Length
83 residues
CAS
946870-92-4

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

IGF-1 LR3 vial from the Eon Peptides research catalog
IGF-1 LR3 · 1mg · catalog photograph

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

  1. Receptor Binding

    Activation of the Type 1 IGF Receptor

    Long R3 IGF-1 (IGF-1 LR3) is a human IGF-1 analog of 83 amino acids. Two modifications define it: a 13-residue extension at the N-terminus and arginine replacing glutamate at position 3. Its target, the type 1 IGF receptor (IGF-1R), is a receptor tyrosine kinase; activation sets off PI3K/Akt and MAPK/ERK signaling downstream.

    • Affinity for IGF-1R stays close to native
    • Protein-synthesis signaling through PI3K/Akt/mTOR is switched on
    • Proliferation pathways of the MAPK/ERK type are engaged
  2. IGFBP Evasion

    Weak Binding-Protein Affinity and Prolonged Activity

    Relative to native IGF-1, the analog binds IGF-binding proteins (IGFBPs) with roughly 100- to 1,000-fold lower affinity, a consequence of the Arg3 substitution and the N-terminal extension. IGFBPs therefore sequester less of the molecule, a larger share stays free to engage IGF-1R, and in culture systems the functional half-life is markedly longer.

    • IGFBP affinity reduced ~100-1,000×
    • A larger free fraction can reach the receptor
    • Signaling persists longer than with native IGF-1
  3. Akt Cascade

    Translation, Degradation Control and Cell Survival

    Acting through Akt, IGF-1 signalling engages protein synthesis driven by mTOR/p70S6K and regulates GSK3β and FoxO-mediated protein degradation. Skeletal-muscle and cell-culture research models have characterised the cascade extensively.

    • Translation via mTOR-p70S6K is activated
    • Proteasomal/FoxO degradation is inhibited
    • Anti-apoptotic cell survival has been measured

What the research shows

  1. CHO Bioproduction

    Growth Factor for Serum-Free CHO Lines

    In serum-free CHO cell lines, Long R3 IGF-1 is reported to maintain viability, growth and recombinant-protein productivity, outperforming insulin in production conditions.

  2. HEK293 Potency

    Comparison With Insulin and Native IGF-I

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

  3. Hypertrophy Signaling

    Pathways of Myotube Hypertrophy

    Skeletal myotube hypertrophy is driven by IGF-1 through two signaling routes, PI(3)K/Akt/mTOR and PI(3)K/Akt/GSK3, a foundational model in anabolic growth research.

  4. Muscle Genetics

    Regulation by the IGF1-Akt/PKB Axis

    Transgenic and knockout genetic models have established that skeletal-muscle protein synthesis and degradation are both controlled by the IGF1-Akt/PKB axis.

How it's tested

Every lot of IGF-1 LR3 released to the catalog carries a third-party certificate of analysis. 1 documented lot is on file for this compound, with reported HPLC purity from 99.67% to 99.67% (mean 99.67%), issued by Freedom Diagnostics. 1 of 1 certificates record identity as confirmed.

Documented lots
1
Reported purity
99.67% to 99.67%
Mean purity
99.67%
Issuing labs
Freedom Diagnostics

All certificates in the COA library →

Frequently asked questions

How is IGF-1 LR3 structured, and what distinguishes it from the native growth factor?

Long R3 IGF-1 (IGF-1 LR3) is an engineered analog of human insulin-like growth factor 1, 83 amino acids in length. Arginine replaces the glutamic acid at position 3, and a 13-residue peptide extension is added at the N-terminus. Affinity for the IGF-1 receptor is preserved, whereas binding to IGF-binding proteins (IGFBPs) is substantially reduced. In culture, its activity therefore outlasts that of native IGF-1.

What role does IGF-1 LR3 play in serum-free cell culture systems?

IGF-1 LR3 is widely used as an additive in serum-free media, for two reasons: it signals potently through IGF-1R, and it resists sequestration by IGFBPs. According to published studies, CHO and HEK293 cell lines show supported viability, growth and recombinant-protein productivity with it, at concentrations far lower than insulin requires.

Which intracellular signaling cascades lie downstream of IGF-1 LR3?

The compound activates the IGF-1 receptor tyrosine kinase. Two pathways follow: PI3K/Akt/mTOR, linked to cell survival and protein synthesis, and MAPK/ERK, linked to proliferation. Skeletal-muscle models further show that protein degradation is suppressed by the IGF1-Akt axis, acting via FoxO and GSK3β.

What storage conditions preserve the activity of lyophilized IGF-1 LR3?

Lyophilized powder is kept at -20°C, shielded from light and moisture. Repeated freeze-thaw cycling is avoided, which preserves activity.

What is the intended scope of use for research-grade IGF-1 LR3?

Research-grade IGF-1 LR3 is restricted to analytical applications and in vitro laboratory research. It is not a drug. Human use, veterinary use and clinical application of any kind all fall outside its intended scope.

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.