Molecular Profile
What Is IGF-1 LR3?
- Type
- Synthetic IGF-1 analog
- CAS Number
- 143045-27-6
- Molecular Weight
- 9,117.60 g/mol
- Amino Acids
- 83
- Formula
- C400H625N111O115S9
- Sequence
- MFPAMPLSSL FVNGPRTLCG…
Research Peptides
IGF-1 LR3
≥99% purityLyophilized powderThird-party COA
IGF-1 LR3 is supplied as a sterile lyophilized powder in a sealed glass vial, manufactured to ≥99% purity. Every batch is verified by independent third-party analysis and ships with a Certificate of Analysis.
$69.99
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Certificate of analysis
The report for the current batch is available on request. Request it here.
IGF-1 LR3 is supplied as a sterile lyophilized powder in a sealed glass vial, manufactured to ≥99% purity. Every batch is verified by independent third-party analysis and ships with a Certificate of Analysis.
⚠ Research use only. This product is intended solely for in-vitro laboratory research by qualified professionals. Not for human or veterinary use.
Research overview
About IGF-1 LR3
IGF-1 LR3 (Insulin-like Growth Factor-1 Long R3) is a synthetic, modified version of the naturally occurring IGF-1 peptide with an extended half-life and enhanced potency.
It acts as a potent growth factor that promotes cell proliferation, differentiation, and survival. In research settings, IGF-1 LR3 is studied for its ability to stimulate muscle growth (hypertrophy), support tissue repair, enhance nutrient uptake, and promote anabolic processes through activation of the IGF-1 receptor pathway.
Key Research Areas
- Muscle growth and hypertrophy models
- Tissue repair and regeneration
- Cellular proliferation and anti-aging research
- Metabolic regulation and nutrient partitioning
- Recovery from injury and performance studies
Structural Modifications
How It Differs from Native IGF-1
Mohan & Baylink, 2002
- N-terminal extension
- +13 amino acids (MFPAMPLLSLFVN)
- Position 3 substitution
- Glu → Arg
- Total length
- 83 vs 70 amino acids
- IGFBP affinity
- Dramatically reduced
- IGF-1R affinity
- Retained
Sources & references5 peer-reviewed publications and databases
Biochemical Journal
Tomas FM, Knowles SE, Owens PC et al.
1992 · DOI: 10.1042/bj2820091 · PMID: 1371669
Journal of Endocrinology
Tomas FM, Lemmey AB, Read LC, Ballard FJ
1996 · DOI: 10.1677/joe.0.1500077 · PMID: 8708565
Journal of Endocrinology
IGF-binding proteins are multifunctional and act via IGF-dependent and -independent mechanisms
Mohan S, Baylink DJ
2002 · DOI: 10.1677/joe.0.1750019 · PMID: 12379487
American Journal of Pathology
von der Thüsen JH, Borensztajn KS, Moimas S et al.
2011 · DOI: 10.1016/j.ajpath.2010.10.007 · PMID: 21281823
Journal of Endocrinology
Conlon MA, Tomas FM, Owens PC et al.
1995 · DOI: 10.1677/joe.0.1460247 · PMID: 7561636
Research summaries and references are drawn from published, peer-reviewed literature and are provided for educational reference only. They are not product claims or medical advice. This product is sold strictly for laboratory research and is not for human or veterinary use.
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