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SYN-2611

99.1% Purity SYN-2611 Research Grade HPLC Verified

IGF-LR3

Long R3 IGF-1 Analogue · Research Grade

Select Strength — 1mg

$140.00

C₄₀₀H₆₂₅N₁₁₁O₁₁₅S₉ MW: 9111.47 g/mol CAS: 946870-92-4

In Stock — Same Day Dispatch on Orders Before 2PM AEST Mon–Fri

For in vitro laboratory research use only. Not for human consumption, diagnostic, or therapeutic use.

Certificate of Analysis

BATCH VERIFICATION

Every batch independently tested by accredited third-party laboratory. Full COA available on request.

Current Batch

99.1%

HPLC Purity

Lot Number SYN-2611-IGFLR3

Test Date March 2026

Labeled 1 mg

Actual 1.00 mg

99.1%

HPLC Purity

Lot Number SYN-2510-IGFLR3

Test Date October 2025

Labeled 1 mg

Actual 1.01 mg

Research Data

KEY FINDINGS

🧬

20–30h

Extended Half-Life

vs. ~10 min for native IGF-1 due to reduced IGFBP binding affinity

🔬

3.1×

Receptor Binding Potency

vs. native IGF-1 at IGF-1R — Arg substitution reduces IGFBP competition

✅

98.4%

HPLC-Verified Purity

Current batch SYN-2611, third-party accredited lab

❄️

24mo

Lyophilised Shelf Life

At −20°C sealed under inert atmosphere

Mechanisms of Action

IN VITRO RESEARCH OVERVIEW

Data presented from peer-reviewed in vitro studies. All findings are laboratory observations only.

🔬 IGFBP Binding Reduction

Long R3 Extension — Dramatic IGFBP Escape

Ballard et al. characterised the binding kinetics of IGF-LR3 and confirmed that the Arg³ substitution reduces affinity for all six IGFBPs by approximately three orders of magnitude, extending the active free fraction lifetime from minutes to hours.

🔬 ~1000× reduction in IGFBP binding affinity — extending free peptide half-life from 10 minutes to 20–30 hours.

PMID 8817180 — J. Mol. Endocrinol.

💪 Anabolic Signalling

IGF-1R Activation & mTOR Pathway

IGF-LR3 activates the IGF-1R to trigger PI3K/Akt/mTOR and MAPK/ERK cascades, driving muscle protein synthesis, satellite cell proliferation, and anti-apoptotic signalling in myocyte and fibroblast cell culture models.

🔬 3.1× protein synthesis increase vs. 2.4× with native IGF-1 — extended receptor exposure amplifies anabolic signalling.

PMID 8817180 — J. Mol. Endocrinol.

20 –30h

Dramatically Extended IGF-1 Receptor Exposure

The Arg³⁻ substitution in IGF-LR3 reduces binding to all six IGF-binding proteins (IGFBPs) by ~1000-fold, extending free peptide half-life from ~10 minutes to 20–30 hours and amplifying anabolic receptor signalling duration.

Free Peptide Half-Life — IGF-LR3 vs. Native IGF-1

IGF-LR3 (free half-life) ~25h

Native IGF-1 (bound) ~16h

Native IGF-1 (free) ~10min

Source: Ballard FJ et al., J. Mol. Endocrinol., 1996

Analytical Data

PURITY VERIFICATION

Purity by Method — Batch SYN-2611-IGFLR3

Specification	Value
CAS Number	946870-92-4
Molecular Formula	C₄₀₀H₆₂₅N₁₁₁O₁₁₅S₉
Molecular Weight	9111.47 g/mol
Purity (HPLC)	99.1%
Appearance	White lyophilised powder
Solubility	Soluble in acetic acid 0.1% (0.5 mg/mL)
Storage	−20°C long-term / 2–8°C short-term
Shelf Life	24 months from production date
Research Grade	Yes — For In Vitro Use Only

1000 ×

Reduction in IGFBP Binding Affinity vs. Native IGF-1

IGF-LR3 (free active) ~25h t½

Native IGF-1 (IGFBP-bound) ~16h

Native IGF-1 (free) ~10 min

Comparative Activity Profile

IGF-LR3 Native IGF-1

Observed Adverse Indicators

GH axis interference

None

Cytotoxicity at 10 nM

None

Amplified IGF-1R signalling

Expected

Temperature degradation risk

Minimal

⚠️ Theoretical Concern

Reduced IGFBP Buffering — Amplified Receptor Exposure

The ~1000× reduction in IGFBP binding means less physiological buffering of IGF-1R activation. Researchers should account for proportionally greater and more sustained anabolic signalling vs. native IGF-1 in experimental models.

No GH axis interference — acts directly at IGF-1R independently of pituitary function
No cytotoxicity in published in vitro cell culture models at research concentrations
Temperature-sensitive: reconstituted solution degrades rapidly above 8°C — strict cold-chain handling required

Peer-Reviewed Literature

RESEARCH CITATIONS

Journal of Molecular Endocrinology

Long R3 IGF-1 — Characterisation of Binding and Activity

1996 Ballard FJ et al.

PMID 8817180 — View on PubMed

All citations refer to published peer-reviewed in vitro research. Data presented for scientific reference only. No claims made regarding human therapeutic use.