IGF-1 LR3
IGF-1R Agonism Studies
$90.00
- FormatLyophilized powder, single-use vial
- StorageStore lyophilized vial frozen; refer to COA for lot-specific stability data
50 in stock
About IGF-1 LR3
IGF-1 LR3 is an 83-amino-acid recombinant analog of insulin-like growth factor 1. It is derived from the native 70-amino-acid IGF-1 sequence through the addition of a 13-residue N-terminal extension and substitution of arginine at position 3. These structural modifications significantly reduce binding affinity for IGF-binding proteins, increasing its persistence and biological activity in experimental systems.
Full Specification
| Molecular Formula | C400H625N111O115S9 |
| Molecular Weight | 9117.6 g/mol |
| Purity | ≥99% HPLC |
| Appearance | White to off-white lyophilized powder |
| Storage | Store lyophilized vial frozen; refer to COA for lot-specific stability data |
| Format | Lyophilized powder, single-use vial |
The IGF-1 LR3 Molecule
An illustrative representation generated from the compound's molecular formula, alongside its logged molecular data. This figure is schematic — not a measured conformation.
How IGF-1 LR3 Works
The pathways IGF-1 LR3 acts on — and what each one does. The animation traces its signal outward from the compound to every target it engages.
Signalling pathways studied in preclinical models · illustrative
Insulin-Like Growth Factor Receptor Activation
IGF-1R AgonismIGF-1 LR3 (Long R3 IGF-1) is an 83-amino-acid analog of human IGF-1, modified with a 13-residue N-terminal extension and an arginine substitution for glutamate at position 3. It binds to and activates the type 1 insulin-like growth factor receptor (IGF-1R), a receptor tyrosine kinase, initiating downstream signaling through pathways including PI3K/Akt and MAPK/ERK.
Extended Bioavailability, Reduced IGFBP Binding
PharmacokineticsThe N-terminal extension and Arg3 substitution substantially reduce IGF-1 LR3's affinity for insulin-like growth factor binding proteins (IGFBPs), by approximately 100- to 1,000-fold compared with native IGF-1. Because less of the analog is bound and sequestered by IGFBPs, a greater proportion remains available to interact with IGF-1R, contributing to its prolonged functional activity and extended persistence in cell-culture systems.
Protein Synthesis & Cell Survival
Anabolic SignalingThrough Akt activation, IGF-1 signalling engages mTOR/p70S6K-driven protein synthesis and GSK3β/FoxO-mediated protein degradation — a cascade extensively characterised in skeletal-muscle and cell-culture research models.
What IGF-1 LR3 Is Researched For
Serum-Free Cell Culture
Studied as a growth-supporting factor in serum-free CHO cell culture, including its ability to maintain cell growth and viability while supporting recombinant-protein production, with comparisons against insulin-based culture systems.
Growth Activity Compared With Insulin
In serum-free HEK293 cell models, it has demonstrated strong growth- and survival-promoting activity at substantially lower concentrations than insulin, with activity also compared against native IGF-1.
Myotube Growth Pathways
In cultured myotubes, activation of PI3K/Akt signaling can influence downstream pathways including mTOR and GSK3, both involved in regulating protein synthesis and cellular growth.
IGF-1/Akt-PKB Regulation
The IGF-1/Akt-PKB signaling axis has been extensively investigated in skeletal-muscle research, with genetic, transgenic, and knockout models helping establish its role in balancing muscle protein synthesis and breakdown.
Common Questions About IGF-1 LR3
An 83-amino-acid recombinant analog of insulin-like growth factor 1, modified to reduce binding to IGF-binding proteins and extend its activity in experimental systems.
A 13-residue N-terminal extension and an arginine substitution at position 3 give it substantially reduced IGFBP affinity compared with the native 70-amino-acid hormone.