This product is also referenced in the literature under the following terms: Long R3 IGF-1, IGF-1 LR3 research peptide, IGFBP-resistant IGF-1 analog, recombinant IGF-1 LR3.
Mechanism of Action (Research Context)
Published peer-reviewed research describes IGF-1 LR3 as a high-affinity agonist of the type-1 IGF receptor (IGF-1R) with substantially reduced affinity for IGFBP-1 through IGFBP-6. This binding-protein resistance results in extended bioactive half-life in research models compared to native IGF-1. Investigators commonly use this compound in laboratory studies exploring PI3K/Akt/mTOR signaling, MAPK pathway activation, satellite-cell proliferation, and protein-synthesis pathways. Researchers should consult primary literature for current mechanistic understanding.
Product Specifications
- CAS Number: 946870-92-4
- Molecular Formula: C₄₀₀H₆₂₅N₁₁₁O₁₁₅S₉
- Molecular Weight: 9111.5 g/mol
- Sequence: 83-amino-acid recombinant analog (70-aa native IGF-1 + 13-aa N-terminal extension; Arg substitution at position 3)
- Form: Lyophilized
- Endotoxin: <1.0 EU/μg (research-grade specification)
- Purity: Refer to lot-specific Certificate of Analysis
Research Applications
IGF-1 LR3 is referenced in laboratory research focused on IGF-1 receptor signaling, cell proliferation, myogenic differentiation, and anabolic pathway studies. Typical study designs include in-vitro receptor-binding assays, cell-based proliferation and protein-synthesis assays (C2C12 myoblasts, fibroblast cultures), Western-blot analysis of Akt and S6K phosphorylation, and analytical method development. This product is supplied as a reference standard only and is not formulated, labeled, or packaged for any in-vivo or therapeutic application.
Storage & Handling
Store lyophilized powder at -20°C, protected from light. Reconstituted solution should be stored at 2–8°C and used within the validated stability window. For long-term storage of reconstituted material, aliquot and freeze at -80°C to avoid repeated freeze-thaw cycles. Always handle in accordance with standard laboratory safety practices. Refer to the lot-specific Certificate of Analysis for stability data and recommended handling.
Quality & Documentation
Each lot is supplied with a Certificate of Analysis (COA) referencing identity, purity, and applicable analytical results (HPLC purity, mass-spectrometry confirmation, endotoxin testing). The COA is the authoritative source for lot-specific data and supersedes any general product description.
Frequently Asked Questions
What is IGF-1 LR3? IGF-1 LR3 (Long R3 IGF-1) is a recombinant 83-amino-acid analog of human IGF-1 supplied as a research reference compound for in-vitro laboratory investigation in growth-factor and anabolic-signaling research.
How does IGF-1 LR3 differ from native IGF-1? Two structural modifications: a 13-amino-acid N-terminal extension and an arginine residue substituted for glutamic acid at position 3. These changes drastically reduce binding-protein affinity, resulting in extended bioactive half-life in research models while retaining full IGF-1R agonist activity.
Why is the binding-protein resistance significant in research? In native systems, the majority of circulating IGF-1 is bound to IGFBPs, which modulates its bioavailability. Researchers use IGF-1 LR3 when they need a consistent, IGFBP-independent agonist to isolate receptor-level signaling effects in cell culture.
Is this product intended for human use? No. This is a research reference material only and is not formulated, labeled, or packaged for human or veterinary use, diagnostic use, food, cosmetic, or therapeutic application.
What documentation is included? A lot-specific Certificate of Analysis (COA) covering identity, purity, mass-spectrometry confirmation, and endotoxin testing.
Research Use Only. This product is intended exclusively for in-vitro laboratory and research applications. Not for human or veterinary consumption, diagnostic use, food, cosmetic, or therapeutic purposes. Handling should be performed only by qualified researchers in an appropriate laboratory setting.
