For laboratory research use only. Not for human consumption. Not for clinical or therapeutic use. Not evaluated by the FDA.
For laboratory research use only. Not for human consumption. Not for clinical or therapeutic use. Not evaluated by the FDA.
Also known as: IGF-1, IGF1, Insulin-like growth factor 1, somatomedin C
IGF-1 is a peptide hormone structurally homologous to insulin that mediates many of growth hormone’s downstream cellular effects. It is produced primarily by the liver following GH-receptor activation and signals through the IGF-1 receptor.
IGF-1 is the principal downstream effector of the growth hormone (GH) axis: GH released by the pituitary stimulates the liver to synthesize and secrete IGF-1, which then acts through the IGF-1 receptor to influence cell proliferation, differentiation, and protein synthesis. This GH–IGF-1 pathway is a central topic in endocrinology and metabolic research.
In vitro, IGF-1 is used as a reference ligand in cell-proliferation and receptor-binding assays studying the GH/IGF-1 signaling axis, including research on GHRH analogs and secretagogues that act upstream of IGF-1 release.
A widely used research analog is IGF-1 LR3 (Long R3 IGF-1) — an engineered variant with a position-3 arginine substitution and a 13-amino-acid N-terminal extension that extend its half-life and reduce binding to IGF-binding proteins, making it a practical tool for receptor and signaling studies.
Structurally, IGF-1 is a 70-amino-acid single-chain polypeptide with roughly 50% homology to insulin, so correct molecular weight and sequence identity matter when verifying a research reagent — closely related growth factors and engineered analogs can otherwise be confused. In circulation most IGF-1 is not free but bound to a family of six IGF-binding proteins (IGFBP-1 through IGFBP-6) that regulate its half-life and how much ligand reaches the receptor, a key consideration when IGF-1 is added to serum-containing culture media.
At the receptor, IGF-1 activates the IGF-1 receptor tyrosine kinase and its two principal downstream cascades — PI3K/Akt, associated with cell survival and protein synthesis, and Ras/MAPK, associated with proliferation — which is why it remains such a widely used reference ligand in signaling and cell-proliferation research.
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