IGF-1 LR3 is a synthetic protein and lengthened analogue of human insulin-like growth factor 1 (IGF-1).
CAT No: 10-101-260
CAS No:946870-92-4
Synonyms/Alias:946870-92-4;CAMELLIA SINENSIS LEAF OIL;2-[4-[2-[3-[bis[(9Z,12Z)-2-hydroxyoctadeca-9,12-dienyl]amino]propyldisulfanyl]ethyl]piperazin-1-yl]ethyl 5-[bis(2-hydroxytetradecyl)amino]pentanoate;
IGF-1 LR3 (Insulin-like Growth Factor 1 Long Arg3) is a synthetic peptide analog of human IGF-1, engineered to possess an extended amino acid sequence featuring a substitution of arginine for glutamic acid at position 3 and an additional 13 amino acids at the N-terminus. These modifications significantly enhance its biological stability and reduce binding affinity to IGF-binding proteins, resulting in a markedly prolonged half-life and increased bioavailability in vitro. IGF-1 LR3 is widely recognized in biochemical research for its potent mitogenic and anabolic properties, making it a valuable tool in studies of cellular growth, differentiation, and metabolic regulation. Its unique structural and functional attributes have established it as a preferred reagent in a variety of experimental paradigms involving peptide-mediated signaling pathways.
Cellular proliferation studies: IGF-1 LR3 is extensively utilized to investigate mechanisms of cell growth and proliferation across diverse mammalian cell lines. By binding to the IGF-1 receptor and activating downstream signaling cascades such as the PI3K/Akt and MAPK pathways, it enables researchers to dissect the molecular underpinnings of mitogenesis and survival. Its enhanced resistance to IGF-binding proteins ensures sustained receptor engagement, providing robust and reproducible stimulation in cell culture models. This property is particularly advantageous in experiments aiming to elucidate the roles of growth factors in tissue development, cancer biology, and regenerative processes.
Signal transduction research: The peptide's capacity to activate IGF-1 receptor-mediated signaling makes it an indispensable reagent for probing intracellular pathways involved in metabolism, apoptosis, and gene expression. IGF-1 LR3 is frequently employed to delineate the differential effects of IGF-1 analogs on downstream effectors, offering insights into receptor specificity, ligand-receptor dynamics, and cross-talk with other hormonal or growth factor systems. These studies are crucial for advancing the understanding of cellular communication networks and their implications in health and disease.
Protein synthesis assays: Owing to its potent anabolic activity, IGF-1 LR3 serves as a key stimulant in assays designed to quantify protein synthesis and turnover in vitro. By promoting translational initiation and elongation, it facilitates investigations into the regulation of muscle cell hypertrophy, differentiation, and atrophy. Researchers leverage its bioactivity to model physiological and pathological states characterized by altered protein metabolism, thereby enabling the development of novel strategies for tissue engineering and metabolic research.
Peptide receptor interaction studies: As a structurally modified peptide, IGF-1 LR3 is instrumental in studies examining ligand-receptor interactions, receptor binding kinetics, and affinity profiling. Its distinct sequence modifications allow for comparative analyses with native IGF-1, shedding light on the structural determinants of receptor activation and the impact of specific amino acid substitutions. Such research informs the rational design of next-generation peptide therapeutics and enhances the understanding of peptide-receptor pharmacology.
Cell culture supplementation: IGF-1 LR3 is widely adopted as a supplement in serum-free or low-serum cell culture systems to support cell viability, proliferation, and differentiation. Its prolonged activity and reduced degradation in culture conditions make it a reliable alternative to native IGF-1 for maintaining optimal cellular function over extended experimental timelines. This application is particularly valuable in the expansion of primary cells, stem cells, and specialized cell types where consistent growth factor signaling is essential for experimental reproducibility and success.
2. The spatiotemporal control of signalling and trafficking of the GLP-1R
3. High fat diet and GLP-1 drugs induce pancreatic injury in mice
5. Cell-based adhesion assays for isolation of snake venom’s integrin antagonists
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