IGF-1-LR3

IGF-1-LR3

Price range: $20.00 through $79.00

Research Use Only

All products are intended solely for laboratory research and are not for human or animal consumption. By purchasing, the buyer agrees to use these products in compliance with all applicable laws.

IGF-1 LR3 Overview

IGF-1 LR3 is an 83-amino acid synthetic polypeptide engineered to overcome limitations of native IGF-1 through two strategic modifications: glutamic acid-to-arginine substitution at position 3 and addition of a 13-residue N-terminal extension (MFPAMPLSSLFVN). These alterations reduce binding affinity for IGFBPs by approximately 100-fold while maintaining full target receptor activation capacity, resulting in increased bioavailability and extended half-life compared to native IGF-1. Research models examine its activation of tyrosine kinase signaling, downstream PI3K-Akt and Ras-MAPK pathways, effects on substrate uptake in experimental models, protein synthesis stimulation, and molecular proliferation in laboratory settings.

Francis et al. (1992). Castellino et al. (1992).

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SKU: SKU-IGF-1-LR3 Category:

Research Findings

IGF-1 LR3 has been extensively studied in molecular signaling and pathway research, with investigations focusing on receptor-mediated signaling cascades, anabolic dynamics, substrate utilization, and molecular remodeling in various experimental models. Studies examine both its enhanced pharmacokinetic properties and downstream molecular responses.

Key Areas of Research:

  • Signaling: PI3K-Akt, MAPK-ERK, tyrosine kinase

  • Substrate: Uptake dynamics, lipid pathways, amino acid

  • Anabolic: Protein synthesis, proliferation, nitrogen

  • Molecular: Differentiation, survival signaling, viability

Together, these investigations demonstrate IGF-1 LR3’s potent activation of signaling pathways. As a modified IGF-1 analog with reduced IGFBP binding, LR3 provides a research framework for examining target receptor biology, anabolic signaling mechanisms, and downstream pathway characterization in diverse experimental systems.

Francis et al., Journal of Molecular Endocrinology, 1992

Castellino et al., Biochemical and Biophysical Research Communications, 1992

Lu et al., Protein Expression and Purication, 2009

References

Francis G.L. et al. (1992). Novel recombinant fusion protein analogues of insulin-like growth factor (IGF)-I indicate the relative importance of IGF-binding protein and receptor binding for enhanced biological potency. Journal of Molecular Endocrinology, 8(3):213-223.

Castellino F.J. et al. (1992). Receptor binding and mitogenic potency of insulin-like growth factor I analogues modied at position 3. Biochemical and Biophysical Research Communications, 189(3):1641-1648.

Lu Z. et al. (2009). Expression and purification of recombinant human long-R3 insulin-like growth factor-I in Pichia pastoris. Protein Expression and Purification, 67(1):38-43.

Size

0.1mg, 1mg

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