IGF-DES is a truncated IGF-1 lacking the first 3 amino acids. Virtually no IGFBP binding — the most potent IGF-1 form available for studying isolated receptor activation without binding protein interference.
Des(1-3) IGF-1, commonly known as IGF-DES, is a 67-amino acid truncated variant of human Insulin-like Growth Factor-1 in which the N-terminal tripeptide Gly-Pro-Glu has been removed. This truncation is the most impactful possible modification for IGFBP interaction: the Gly-Pro-Glu tripeptide is the critical determinant for high-affinity IGFBP binding, and its removal virtually eliminates interaction with all six IGF binding proteins. As a result, IGF-DES exists almost entirely in the free, bioavailable form in any research system — making it approximately 10-fold more potent than native IGF-1 in receptor activation assays.
Des(1-3) IGF-1 is not purely a synthetic construct — it has been identified as an endogenous bioactive form in human brain tissue, where it is generated by acid protease-mediated N-terminal processing. The brain-derived form is thought to act in a paracrine/autocrine manner on neural progenitor cells and neurons without IGFBP sequestration, enabling rapid, localized IGF signaling. This endogenous context provides biological validation for the research utility of the truncated form.
IGF-DES retains full agonist activity at both the IGF-1 receptor (IGF1R) and the insulin receptor isoform A (IR-A) at higher concentrations. Research applications include studies requiring maximal IGF1R activation without IGFBP confounding (cell proliferation dose-response curves, receptor phosphorylation kinetics, downstream signaling mapping), comparison studies with IGF-1 LR3 and native IGF-1 for dissecting IGFBP contribution to signaling, and neural progenitor cell biology research.
Supplied as a lyophilized powder with ≥99% purity. Store at -20°C. For growth factor signaling research only.
