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IGF-1 LR3
Specialty Peptides

IGF-1 LR3

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Long R3 Insulin-like Growth Factor-1 is an 83 amino acid analog of IGF-1. The LR3 modification provides enhanced stability and potency for research applications.

Purity

99%+

Size

1mg

1
COA Available
Lab Verified
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For Research Use Only (RUO)

This product is intended for in-vitro research applications only. Not for human or animal consumption, cosmetic use, or as a dietary supplement. All customers must be at least 21 years of age. It is the researcher's responsibility to handle materials in accordance with their institution's safety protocols and all applicable laws.

Specifications

Molecular Weight9,111 Da
Sequence83 Amino Acids
AppearanceWhite lyophilized powder
StorageStore at -20°C
SolubilitySoluble in sterile water

Certificate of Analysis

Each batch of IGF-1 LR3 undergoes rigorous third-party testing to ensure purity and identity verification. Download your COA instantly.

HPLC Purity Analysis
Mass Spectrometry Verification
Lot-Specific Documentation

Extended Research Applications & Mechanisms

Overview

IGF-1 LR3 (Long R3 Insulin-like Growth Factor-1) is an 83-amino acid synthetic analog of human IGF-1 featuring an arginine substitution at position 3 and a 13-amino acid N-terminal extension peptide. These modifications dramatically reduce binding to IGF binding proteins (IGFBPs), resulting in enhanced bioavailability and prolonged biological activity. IGF-1 LR3 is utilized in laboratory research to study growth factor signaling, muscle biology, and cell proliferation mechanisms. All discussion herein is limited to experimental research contexts and does not imply applied, therapeutic, or physiological use.

Biochemical Characteristics

Sequence: 83 amino acids (N-terminal extension + Arg3 substitution)
Molecular Formula: C₄₀₀H₆₂₅N₁₁₁O₁₁₅S₉
Molecular Weight: 9117.5 g/mol
CAS Number: 946870-92-4

IGF-1 LR3 contains a 13-amino acid extension at the N-terminus and an arginine-for-glutamic acid substitution at position 3. These modifications reduce IGFBP affinity by over 500-fold while maintaining full IGF-1 receptor binding in experimental models.

Research Applications

IGF-1 LR3 is employed in laboratory research to study IGF-1 receptor signaling and anabolic pathways. Common experimental applications include muscle protein synthesis assays, cell proliferation studies, and growth factor pathway investigations. Research protocols utilize IGF-1 LR3 to investigate the effects of sustained IGF-1R activation without the confounding influence of IGFBP modulation, enabling clearer interpretation of direct receptor-mediated effects.

Pathway / Mechanistic Context

Mechanistically, IGF-1 LR3 activates the IGF-1 receptor (IGF-1R), triggering autophosphorylation and recruitment of IRS-1/2 adaptor proteins. This leads to activation of two major downstream pathways: the PI3K/Akt pathway promoting cell survival and protein synthesis, and the Ras/MAPK pathway supporting proliferation. The PI3K/Akt pathway activates mTORC1, which stimulates ribosomal biogenesis and translation initiation through phosphorylation of S6K1 and 4E-BP1. Simultaneously, Akt phosphorylates and inactivates GSK-3β, promoting glycogen synthesis and additional anabolic responses.

Preclinical Research Summary

Preclinical investigations of IGF-1 LR3 include in-vitro cell culture studies and in-vivo animal models evaluating muscle growth, cell proliferation, and metabolic effects. Reported findings include enhanced muscle protein synthesis, increased satellite cell activation, and promoted cellular growth in various tissue types. Animal studies further explore effects on body composition and tissue regeneration, demonstrating the potent anabolic properties of IGFBP-resistant IGF-1 analogs. All findings are interpreted strictly within the context of laboratory research models.

Form & Analytical Testing

IGF-1 LR3 is supplied as a synthetic research-grade lyophilized peptide. Identity and purity are confirmed through analytical methodologies including high-performance liquid chromatography (HPLC) and mass spectrometry (MS). Batch-specific documentation includes certificate of analysis data supporting molecular identity and purity metrics ≥98%.

Mechanisms of Action

1

IGF-1 Receptor Activation - High-affinity binding to IGF-1R with full agonist activity

2

IGFBP Resistance - Dramatically reduced binding to IGF binding proteins (>500-fold reduction)

3

PI3K/Akt Signaling - Activates phosphoinositide 3-kinase and downstream Akt pathway for cell survival

4

Extended Half-Life - Prolonged biological activity due to reduced IGFBP sequestration and clearance

Research Applications

1Muscle Biology Research

Studies on muscle growth, protein synthesis, and regeneration.

Key Research Findings
  • Potent stimulator of muscle protein synthesis via mTORC1 activation
  • Promotes satellite cell activation and myoblast proliferation
  • Enhances muscle fiber hypertrophy in research models
  • Supports muscle regeneration and repair pathway studies

2Cell Proliferation & Survival Studies

Research on growth factor signaling and cell biology.

Key Research Findings
  • Activates IGF-1R with full agonist efficacy
  • Promotes cell survival through PI3K/Akt pathway
  • Stimulates cell division through MAPK signaling
  • Extended half-life enables sustained receptor activation

3IGFBP-Independent Signaling Studies

Investigation of direct IGF-1R effects without IGFBP modulation.

Key Research Findings
  • Over 500-fold reduced IGFBP binding affinity
  • Enables study of direct IGF-1R-mediated effects
  • Prolonged bioavailability compared to native IGF-1
  • Useful for structure-activity relationship studies

Supporting Research & Bibliography

The following peer-reviewed publications support the research applications described above. References are provided for informational purposes to assist researchers in their literature review.

1

Novel recombinant fusion protein analogues of insulin-like growth factor (IGF)-I indicate the relative importance of IGF-binding protein and receptor binding for enhanced biological potency

Francis GL, Ross M, Ballard FJ, et al.

Journal of Molecular Endocrinology1992;8:213-223DOIPubMed
2

Increased weight gain, nitrogen retention and muscle protein synthesis following treatment of diabetic rats with insulin-like growth factor (IGF)-I and des(1-3)IGF-I

Tomas FM, Knowles SE, Owens PC, et al.

Biochemical Journal1991;276:547-554DOIPubMed
3

Natural and synthetic forms of insulin-like growth factor-1 (IGF-1) and the potent derivative, destripeptide IGF-1: biological activities and receptor binding

Ballard FJ, Francis GL, Ross M, et al.

Biochemical and Biophysical Research Communications1987;149:398-404DOIPubMed
4

Effects of full-length and truncated insulin-like growth factor-I on nitrogen balance and muscle protein metabolism in nitrogen-restricted rats

Tomas FM, Knowles SE, Owens PC, et al.

Journal of Endocrinology1992;135:193-206DOIPubMed

Total references: 4

Note: The information provided is for research reference only. All research applications are based on in-vitro and animal studies. This product is intended for laboratory research purposes only. Not for human or veterinary use.

Research Use Only: This product is intended for laboratory research purposes only. Not for human or veterinary use. By purchasing, you confirm that you are a qualified researcher and will use this product in accordance with all applicable regulations.

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