IGF-1 LR3

About IGF-1 LR3

IGF-1 LR3 is a modified version of insulin-like growth factor-1 with extended half-life, used in research studying growth factor pathways.

This research peptide is supplied as a lyophilized powder that requires reconstitution before use in laboratory applications. It is provided at research-grade purity for in-vitro studies only.

Research Applications: IGF-1 LR3 is used exclusively for laboratory research purposes. It is not intended for human consumption, medical treatment, or any form of in-vivo application.

Storage: Store lyophilized powder at -20°C. After reconstitution, store at 2-8°C and use within the timeframe specified by the manufacturer.

Detailed Research Information

IGF-1 LR3 (Long R3 Insulin-like Growth Factor-1) is a synthetic analog of insulin-like growth factor-1 extensively studied in cellular growth and metabolism research. As a research compound, IGF-1 LR3 is investigated for its extended half-life, reduced binding protein affinity, and enhanced bioavailability compared to native IGF-1.

Key Research Applications

Cell Culture Research: IGF-1 LR3 is utilized in cell proliferation studies, examining growth factor signaling in various cell lines, and optimizing media formulations for tissue culture applications.

Anabolic Signaling Studies: Research applications include investigation of protein synthesis pathways, mTOR activation mechanisms, and anabolic cellular responses to IGF-1 receptor stimulation.

Metabolism Research: IGF-1 LR3 is employed in studies exploring glucose uptake mechanisms, glycogen synthesis pathways, and insulin-like metabolic effects in muscle and adipose tissue models.

Binding Protein Studies: Research utilizes IGF-1 LR3 to examine IGF binding protein (IGFBP) interactions, free versus bound IGF-1 activity, and mechanisms of reduced IGFBP affinity.

Mechanism of Action

IGF-1 LR3 functions through activation of IGF-1 receptors while exhibiting dramatically reduced affinity for insulin-like growth factor binding proteins (IGFBPs). The peptide contains an N-terminal 13 amino acid extension and a glutamic acid substitution at position 3, which together prevent IGFBP binding while maintaining receptor activation capacity. Research demonstrates that this modification extends the half-life from minutes to hours and increases bioavailability, making it particularly valuable for sustained research applications.

Product Specifications

All listed research peptides are supplied in lyophilized (freeze-dried) powder form and require reconstitution with bacteriostatic water or sterile water before use in laboratory applications. Products are intended exclusively for in vitro research and are not for human consumption.