Receptor Grade IGF-1 LR3 peptide, a polypeptide amino acid also known as Long arginine 3 IGF-1, or LR3-IGF-1, has been suggested to exhibit potential action in lipolysis, protein synthesis, and muscular recovery. (1) Insulin-like Growth factor-1, or IGF-1, is a naturally produced protein composed of 70 amino acids. Structurally similar to insulin, this Receptor Grade IGF-1 LR3 has the potential primarily in regulating cell tissue and body growth and development. There are two synthetic variations of IGF-1; firstly, the synthetic IGF-1, which was developed with the intention of identically mimicking to the natural protein and possibly stimulating similar effects as IGF-1; and second, is Receptor Grade IGF-1 LR3, which is also synthetic in nature, but may exhibit higher efficacy than the natural protein.
Receptor Grade IGF-1 LR3 is a synthetic variant of the naturally occurring IGF-1, which contains an extended N-terminal structure and arginine acid at residue 3. Hence, it is named IGF-1 Long R3. Owing to the altered structure, Receptor Grade IGF-1 LR3 has been suggested to bind poorly with type 1 IGF-1 receptors, potentially increasing blood plasma concentration of the IGF binding proteins.
During the years 1940 to 1950, a growth hormone somatotropin was identified and researched, with scientists eventually positing that it had potential to increase in the sulfate uptake in normal control rat serum. This ‘sulfate factor’ was isolated from the rat serum and named ‘somatomedin.’ An independent study was also conducted to examine the components producing insulin-like activity. During this study, it was suggested that these components were in fact the ‘somatomedins,’ resulting in naming these compounds ‘insulin-like growth factors’.
Further mutations of the insulin-like growth factors were carried out using gene targeting approaches to potentially increase bioavailability and potency potential. During these mutation studies, Receptor Grade IGF-1 LR3 was synthesized with an additional arginine acid and an extended structure at the N-terminal, producing a protein composed of 80+ amino acids, as opposed to 70 amino acids found in natural IGF-1
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