IGF-DES IGD
Truncated IGF-1
Truncated IGF-1 lacking three N-terminal amino acids, which does not bind IGF-binding proteins but retains IGF-1 receptor activity.
Evidence level. Evidence comes mainly from animal or other preclinical models. About the badges
- Class
- Truncated IGF-1
- Category
- Muscle & Growth Factors
- Type
- Single compound
- Abbreviation
- IGD
- Development and regulatory status
- Not approved for humans; research reagent; WADA-prohibited substance
What researchers study
Truncated IGF-1 lacking the first three N-terminal amino acids, so it does not bind IGF-binding proteins but retains IGF-1 receptor activity. It acts as a potent mitogen in cell assays.
Research areas
- IGF-1 receptor signalling and cell proliferation
- Tissue-growth models
- Prostate stromal cell growth studies
- Mammary gland transgenic mouse models
Reported findings
Summaries of published results. Each one is tagged with the type of study behind it. They describe research outcomes and are not claims about any product. Why study type matters.
- cell culture
Des(1-3)IGF-I, which does not bind IGF-binding proteins, was a potent mitogen for human benign prostatic hyperplasia stromal cells, stimulating growth and inhibiting apoptosis
- rodent
In transgenic mice overexpressing des(1-3)IGF-I in the mammary gland, 53% developed mammary adenocarcinomas by 23 months
- rodent
In rats, unchanged Des(1-3)-IGF-I was detectable for up to 24 h in an anti-doping assay
Studied alongside
Compounds that appear together in research because their mechanisms complement each other, or as comparators. The reasons given are research reasoning, not recommendations for use.
- IGF-1 LR3related IGF-1 analogue compared in receptor and growth assays
- MGFIGF-1 splice-variant peptide studied in muscle models
- Somatropin (rHGH)upstream hormone that stimulates IGF-1 production
