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Insulin-Like Growth Factor (IGF-1)1 min readJanuary 28, 2026
What is IGF-1 and How Does it Work
## What is IGF-1? Insulin-like Growth Factor-1 (IGF-1), also known as Somatomedin-C, is a polypeptide growth factor that is a member of the insulin family of peptides. IGF-1 includes 70 amino acids with a molecular weight of 7649 Daltons. Similar to insulin, which has 51 amino acids, IGF-1 has an A and B chain connected by 3 disulfide bonds in a single chain. The main source of IGF-1 for adults is the liver. The Insulin-like growth factors (IGFs)
What is IGF-1? Insulin-like Growth Factor-1 (IGF-1), also known as Somatomedin-C, is a polypeptide growth factor that is a member of the insulin family of peptides. IGF-1 includes 70 amino acids with a molecular weight of 7649 Daltons. Similar to insulin, which has 51 amino acids, IGF-1 has an A and B chain connected by 3 disulfide bonds in a single chain. The main source of IGF-1 for adults is the liver. The Insulin-like growth factors (IGFs)
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GH ReleasersInsulin-Like Growth Factor (IGF-1)Stem Cell Research
Scientific research has examined age-associated variations in IGF-1 signaling and their correlation with cellular growth, tissue remodeling, and metabolic regulation across experimental models.
IGF1 LR3 (insulin-like growth factor-1 Long R3) is a non-glycosylated, recombinant polypeptide chain made up of 83 amino acids. IGF1 LR3 is the recombinant form of human IGF-1, and as such it contains the entire native amino acid sequence but with two major modifications: substitution of arginine (abbreviated R or arg) at position 3 with glutamic acid (abbreviated E or Glu) hence the label _R3_; and the extension of the N-terminus of th
## What is Follistatin? Follistatin was first identified in the late 1980s, when researchers discovered that it could block the activity of myostatin, a protein that regulates muscle growth. This finding sparked a great deal of interest in the scientific community, and over the next several years, researchers began to uncover more information about the protein's structure and function. One of the key breakthroughs came in 1997, when scientists discovered that a genetic mutation in a bree