IGF-1 DES Research Overview

IGF-1 DES Research Overview

IGF-1 DES, also written DES(1-3)IGF-1, is a 67-amino-acid variant formed by removal of the first three N-terminal residues from native IGF-1. The truncation changes its interaction with IGF-binding proteins and makes DES a distinct reference material for controlled short-window and localized IGF-signalling research.

The IGF-1 DES research material page lists the DES-specific specifications, available format, and batch-documentation pathway.

Structural identity

Native IGF-1 contains 70 amino acids. DES lacks the N-terminal Gly-Pro-Glu sequence, leaving 67 amino acids. This identity is distinct from IGF-1 LR3, which instead has an N-terminal extension and an Arg3 substitution for a total of 83 amino acids.

IGFBP interaction

The N-terminal region contributes to IGF-binding-protein interactions. Removing residues 1–3 reduces DES affinity for several IGFBPs in experimental systems. Research designs use this difference to examine receptor access and localized signalling while controlling for matrix, cell type, and observation window.

Receptor and pathway endpoints

DES engages the IGF-1 receptor. Laboratory studies measure receptor phosphorylation, PI3K-AKT-mTOR and RAS-MAPK pathway signals, and cellular-proliferation or differentiation endpoints. Short observation windows and spatially constrained models help distinguish DES-focused questions from longer-duration LR3 studies.

DES compared with LR3

DES and LR3 are not interchangeable. DES is a truncated 67-amino-acid variant associated with short-window and localized-signalling experiments. LR3 is an extended 83-amino-acid analog with reduced IGFBP affinity and a longer signalling window in research models.

Analytical verification

Compound-specific documentation should identify DES(1-3)IGF-1 rather than a generic IGF-1 label. HPLC can characterize purity, while mass spectrometry can support molecular-identity assessment. Researchers should match documentation to the batch identifier printed on the vial.

Research scope

This material is described solely for controlled laboratory studies of IGF-1R binding, IGFBP interactions, localized signalling, and cellular endpoints. Its scope is limited to laboratory receptor, binding-protein, pathway, and cellular-endpoint research.

References

• Ballard FJ et al. Des(1-3)IGF-I: a truncated form of insulin-like growth factor-I. International Journal of Biochemistry & Cell Biology. 1996.
• Russo VC et al. DES(1-3)IGF-I in organ-culture growth-factor research. Growth Factors. 1994.
• Mongongu C et al. Detection of Long R3 and DES(1-3) IGF-I using immunopurification and high-resolution mass spectrometry. Drug Testing and Analysis. 2021.

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