Product Usage: This PRODUCT IS INTENDED AS A RESEARCH CHEMICAL ONLY. This designation allows the use of research chemicals strictly for in vitro testing and laboratory experimentation only.All product information available on this website is for educational purposes only. Bodily introduction of any kind into humans or animals is strictly forbidden by law. This product should only be handled by licensed, qualified professionals. This product is not a drug, food, or cosmetic and may not be misbranded, misused or mislabeled as a drug, food or cosmetic.

Long Arginine 3-IGF-1_1MG

IGF-1 LR3

IGF-1 LR3 (Insulin-Like Growth Factor-1 Long Arg3) is a recombinant analog of human IGF-1 engineered with an Arginine substitution at position 3 and an N-terminal extension of 13 amino acids. These structural modifications have been widely studied in research settings for their effects on protein stability, receptor interaction, and binding affinity to IGF binding proteins (IGFBPs).*

In laboratory research, IGF-1 LR3 is used as a molecular research tool to study IGF-1 receptor signaling, cell growth pathways, and comparative structure–function relationships between native IGF-1 and modified analogs in controlled experimental systems.*

  • Protein Name: IGF-1 LR3
  • Protein Class: Insulin-like growth factor analog
  • Amino Acid Length: 83 amino acids
  • Modification: Arg3 substitution with N-terminal extension
  • Form: Lyophilized powder
  • Purity: ≥99% (HPLC verified)
  • Quantity: 1 mg per vial
  • Analytical Verification: HPLC and Mass Spectrometry (MS)
  • Manufacturing: Recombinant expression and in-house purification
  • Designation: For Research Use Only (RUO)

$88.00

18 in stock

Products will arrive in a lyophilized (powder) form for maximum stability.

Free domestic shipping on orders over $300

IGF-1 LR3

Scientific & Research Context

IGF-1 LR3 has been examined in published research for its interaction with the IGF-1 receptor (IGF-1R) and downstream signaling cascades involved in cellular growth, differentiation, and metabolic regulation in experimental models.* Compared to native IGF-1, the LR3 modification has been investigated for altered binding dynamics with IGFBPs and extended activity profiles in vitro.*

Within laboratory research environments, IGF-1 LR3 has been studied in relation to:*

  • IGF-1 receptor binding and activation assays*

  • Intracellular signaling pathways such as PI3K/Akt and MAPK*

  • Cell proliferation and differentiation models*

  • Protein–protein interaction and binding affinity studies*

  • Comparative analyses between native IGF-1 and IGF-1 analogs*

Its modified structure makes IGF-1 LR3 a frequently referenced compound in cell biology, biochemistry, and molecular signaling research.*

Quality & Analytical Assurance

Each batch of IGF-1 LR3 undergoes comprehensive analytical testing to confirm molecular identity, sequence integrity, and purity. Verification using validated HPLC and MS methodologies ensures batch-to-batch consistency, reliability, and reproducibility for research applications.

Storage & Handling

IGF-1 LR3 is supplied in lyophilized form to enhance stability during storage and transport. Store unopened vials in a cool, dry environment protected from light. Reconstitution and subsequent handling should follow established protein research and laboratory best practices to preserve molecular integrity.

For further information on proper storage techniques, click the button…

Storage Instructions

Referenced Scientific Literature
Provided for informational and educational purposes only

  • Rinderknecht E, Humbel RE. The amino acid sequence of human insulin-like growth factor I and its structural homology with proinsulin. Journal of Biological Chemistry, 1978; 253(8): 2769–2776.
  • Le Roith D, Bondy C, Yakar S, Liu JL, Butler A. The somatomedin hypothesis: 2001. Endocrine Reviews, 2001; 22(1): 53–74.
  • Jones JI, Clemmons DR. Insulin-like growth factors and their binding proteins: biological actions. Endocrine Reviews, 1995; 16(1): 3–34.
  • Firth SM, Baxter RC. Cellular actions of the insulin-like growth factor binding proteins. Endocrine Reviews, 2002; 23(6): 824–854.
  • Baxter RC. IGF binding proteins in cancer: mechanistic and clinical insights. Nature Reviews Cancer, 2014; 14(5): 329–341.
  • Holly JMP, Perks CM. Insulin-like growth factor physiology: what we have learned from human studies. Endocrine, 2012; 42(2): 205–213.
  • De Meyts P. The insulin receptor and its signal transduction network. Endocrine Reviews, 2004; 25(6): 817–835.
  • Dupont J, Le Roith D. Insulin and insulin-like growth factor I receptors: similarities and differences in signal transduction. Hormone Research, 2001; 55(Suppl 2): 22–26.
  • Butler AA, Le Roith D. Control of growth by the somatotropic axis. Annual Review of Physiology, 2001; 63: 141–164.
  • Yakar S, et al. Circulating levels of IGF-1 directly regulate bone growth and density. Journal of Clinical Investigation, 2002; 110(6): 771–781.
  • Adipose tissue-derived stem cell secreted IGF-1 protects myoblasts from the negative effect of myostatin. BioMed Research International, 2014; Article ID 129048.
  • Li N, Yang Q, Walker RG, Thompson TB, Du M, Rodgers BD. Myostatin attenuation in vivo reduces adiposity but activates adipogenesis. Endocrinology, 2016; 157(1): 282–291.
  • Corpas E, Harman SM, Blackman MR. Human growth hormone and human aging. Endocrine Reviews, 1993; 14(1): 20–39.
  • Sonntag WE, Csiszar A, de Cabo R, Ferrucci L, Ungvari Z. Diverse roles of growth hormone and IGF-1 in mammalian aging. Journal of Gerontology: Biological Sciences, 2012; 67(6): 587–598.
  • IGF-I/IGFBP system: metabolism outline and physical exercise. PubMed, 2012.
  • Hanaoka BY, Peterson CA, Horbinski C, Crofford LJ. Implications of glucocorticoid therapy in idiopathic inflammatory myopathies. Nature Reviews Rheumatology, 2012; 8(8): 448–457.
  • Philippou A, Halapas A, Maridaki M, Koutsilieris M. Growth hormone/IGF-1 axis in skeletal muscle physiology. Journal of Musculoskeletal & Neuronal Interactions, 2007.
  • Philippou A, Papageorgiou E, Bogdanis G, Halapas A, et al. Expression of IGF-1 isoforms in skeletal muscle. In Vivo, 2009; 23(4): 567–575.

ALL ARTICLES AND PRODUCT INFORMATION PROVIDED ON THIS WEBSITE ARE FOR INFORMATIONAL AND EDUCATIONAL PURPOSES ONLY. The products offered on this website are furnished for in-vitro studies only. In-vitro studies (Latin: in glass) are performed outside of the body. These products are not medicines or drugs and have not been approved by the FDA to prevent, treat or cure any medical condition, ailment or disease. Bodily introduction of any kind into humans or animals is strictly forbidden by law.