IGF-1 LR3 Dosage Calculator
A laboratory cell-culture reagent. No human trial has ever evaluated it for any endpoint, and its design makes hypoglycaemia the dose-limiting risk.
Written by Kashif Khan, who builds and maintains this site and is not a clinician. Every figure links to its primary source.
Not approved; never even nominated
IGF-1 LR3 is on no FDA compounding list — not Category 1, 2 or 3. It was never nominated, so the FDA has never evaluated it. It is sold as a research reagent and cell-culture supplement. The approved relative is mecasermin (Increlex), a different molecule, for severe primary IGF-1 deficiency. Any claim that IGF-1 LR3 is available through compounding is false.
No approved human dose exists for this compound in any country. The figures below are the doses used in named published studies, reproduced for reference only. Doses given to rats or mice do not convert to a human dose. The FDA has stated that labelling a product “research use only” or “not for human consumption” does not change its legal status when the seller's own marketing shows it is intended for people.
Anti-doping: Prohibited at all times. WADA class S2.2 — IGF-1 and its analogues are explicitly prohibited.
Key facts
- Molecular weight
- 9,111 DaNative human IGF-1 is 7649 Da. LR3 is a 70-amino-acid IGF-1 with a Glu3→Arg substitution plus a 13-amino-acid N-terminal extension.
- Half-life
- Not published. No accessible human pharmacokinetic study reports one, so any specific figure quoted elsewhere has no primary source behind it.
- Also sold as
- Long R3 IGF-1, LR3 IGF-I
Doses used in published studies
These are reproduced for reference. They are not recommendations, and an animal dose in mg/kg does not convert to a human dose.
How good is the evidence?
Zero human trials of any kind. What does exist is a small animal literature from the 1990s — rats, pigs and guinea pigs, almost all of it from one Adelaide group — in which LR3IGF-I was a research tool for probing IGF-binding protein biology, not a candidate drug. The only clinical read-across is the label of a different, weaker, buffered molecule. The substitution and N-terminal extension drop its affinity for IGF-binding proteins by orders of magnitude — normally about 99% of circulating IGF-1 is sequestered by those proteins, and LR3 largely escapes that buffer, so a given mass is far more bioavailable and longer-acting at both the IGF-1 and insulin receptors. That is not a theoretical point: in pigs the variants that bind IGFBPs poorly lowered blood glucose two to three times more potently than native IGF-I and kept it suppressed four to eight times longer. The Increlex label for the far weaker native molecule already requires a meal or snack within 20 minutes of every injection because of hypoglycaemia risk. LR3 has no label, no titration schedule and no monitoring protocol.
Common questions
Sources
Every number on this page comes from one of the documents below. Where no reliable source exists, the page says so instead of filling the gap.
- RegulatorFDA· 2026-05-14Bulk Drug Substances Nominated for Use in Compounding Under Section 503A
- ReferenceR&D SystemsRecombinant Human LR3 IGF-I — product datasheet (molecular weight, structure)
- FDA labelFDA / DailyMed· 2025-05INCRELEX (mecasermin) injection, solution — FDA prescribing information
- RegulatorWorld Anti-Doping Agency· 2026WADA 2026 Prohibited List
- RegulatorUSADAPeptides, Growth Hormones and Cosmetics
- Published studyJournal of Endocrinology 1993;137(3):413–21· 1993-06Tomas FM, Knowles SE, Chandler CS, Francis GL, Owens PC, Ballard FJ. Anabolic effects of insulin-like growth factor-I (IGF-I) and an IGF-I variant in normal female rats
- Published studyGrowth Hormone & IGF Research 2001;11(2):92–103· 2001-04Tomas FM. Insulin-like growth factor-I (IGF-I) analogue, LR(3)IGF-I, ameliorates the loss of body weight but not of skeletal muscle during food restriction
- Published studyJournal of Endocrinology 1997;155(2):377–86· 1997-11Tomas FM, Walton PE, Dunshea FR, Ballard FJ. IGF-I variants which bind poorly to IGF-binding proteins show more potent and prolonged hypoglycaemic action than native IGF-I in pigs and marmoset monkeys
- Published studyJournal of Endocrinology 1995;146(2):247–53· 1995-08Conlon MA, Tomas FM, Owens PC, Wallace JC, Howarth GS, Ballard FJ. Long R3 insulin-like growth factor-I infusion stimulates organ growth but reduces plasma IGF-I, IGF-II and IGF binding protein concentrations in the guinea pig
- Published studyGrowth Hormone & IGF Research 2010;20(5):386–90· 2010-10Kohler M, Thomas A, Walpurgis K, Terlouw K, Schänzer W, Thevis M. Detection of His-tagged Long-R³-IGF-I in a black market product