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IGF-1 DES

Hormonal & Endocrine · ['DES(1-3) IGF-1', 'IGF-1 DES(1-3)', 'Des-N-(1-3)-IGF-1']

A naturally occurring and synthetically produced truncated form of IGF-1 lacking the first three N-terminal amino acids (Gly-Pro-Glu), a deletion that sharply reduces IGF binding protein affinity and is studied as a highly potent IGF-1R agonist in vitro.

🔬 Research use only — not for human or veterinary use. K4 Elite does not provide dosing instructions.
Molecular Weight
~7371 Da g/mol
Research Level
Well Researched
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IGF-1 DES, more precisely DES(1-3)IGF-1, is a truncated variant of insulin-like growth factor 1 that lacks the first three amino acids (glycine-proline-glutamate) at the N-terminus. This form occurs naturally in some tissues and is also produced synthetically for research. The missing tripeptide is the region responsible for a substantial portion of IGF-1's interaction with its binding proteins.

Removal of these residues greatly reduces the molecule's affinity for IGFBPs, which in laboratory studies increases the fraction free to engage the IGF-1 receptor. As a result, DES(1-3)IGF-1 is frequently reported in the literature as more potent than intact IGF-1 in cell-based assays.

It is handled exclusively as a research reagent for in vitro and preclinical study of insulin-like growth factor signaling.

Like intact IGF-1, DES(1-3)IGF-1 signals through the IGF-1 receptor tyrosine kinase, activating PI3K/Akt and Ras/MAPK cascades associated with proliferation and survival signaling in experimental cell systems.

Its defining property is markedly reduced IGFBP binding due to the absent N-terminal tripeptide. Because IGFBPs normally sequester IGF-1 and limit receptor access, the truncated analog shows enhanced apparent potency in cultures containing binding proteins, making it a useful tool for dissecting IGFBP-dependent versus receptor-dependent effects.

  • IGF-1 receptor signaling potency compared with intact IGF-1 in IGFBP-rich cultures
  • Neuronal survival and neurotrophic signaling in cell-based and animal models
  • Skeletal muscle and connective-tissue cell proliferation studies
  • Intestinal and epithelial growth research in preclinical models
  • Structure-function analysis of the IGF-1 N-terminal domain and IGFBP interaction
📋 How published studies were conducted — a research reference summarizing study designs from the literature. This is not usage, dosing, or administration guidance. K4 Elite does not provide dosing instructions; determining any research protocol is the sole responsibility of the qualified researcher.

The following describe published experimental studies for reporting purposes only; they are not usage directions.

Ballard, Francis and colleagues characterized DES(1-3)IGF-1 as several-fold more potent than intact IGF-1 in stimulating cell growth in cultures containing IGF binding proteins, attributing the difference to reduced IGFBP sequestration (Ballard et al., 1987–1991 series).

Preclinical neuroscience studies have reported DES(1-3)IGF-1 as a neurotrophic factor in animal models of neuronal injury, where investigators administered the peptide and measured markers of neuronal survival; these are cited as research findings only.

Combinations examined in the research literature. Descriptive only — not a recommendation to combine compounds.

IGFBP familyNeutral
The N-terminal truncation specifically reduces IGFBP binding; a defining experimental variable rather than a synergy.
IGF-1 LR3Compatible
A parallel IGFBP-evading IGF-1 analog; the two are often compared side by side in receptor-potency studies.
Insulin receptorCaution
Partial cross-reactivity within the insulin/IGF receptor family is relevant to metabolic study design.
Growth hormoneSynergistic
IGF-1 is a downstream effector of GH in the endocrine axis; commonly studied jointly.

References are being compiled for this entry.

What is IGF-1 DES?
It is DES(1-3)IGF-1, a form of insulin-like growth factor 1 missing its first three N-terminal amino acids, which lowers IGF binding protein affinity in experimental systems.
Why is it described as more potent than IGF-1?
In cultures containing IGF binding proteins, the reduced IGFBP affinity leaves more of the molecule free to activate the IGF-1 receptor, so studies frequently report higher apparent potency than intact IGF-1.
Does it have a PubChem compound CID?
As a ~67-residue protein it is catalogued in protein databases rather than as a small-molecule PubChem compound, so no verified compound CID is provided.
What has research examined?
Published studies cover receptor-signaling potency, neuronal survival, muscle and epithelial cell proliferation, and structure-function analysis of the IGF-1 N-terminus.
Is IGF-1 DES for human or animal use?
No. It is supplied for laboratory research use only and is not intended to diagnose, treat, cure, or prevent any disease in humans or animals.
Disclaimer: This profile summarizes published preclinical and laboratory research for reference only. It is not medical advice and makes no claim of safety or efficacy in humans. Determining any research protocol is the sole responsibility of the qualified researcher. Products are sold strictly for in-vitro research and have not been evaluated by the FDA.