Peptide database / Growth factor

IGF-1 LR3

An engineered IGF-1 analog built for cell-culture labs that dodges IGF binding proteins. No published human studies of any kind.

Research chemical WADA prohibited D Evidence Animal or cell data only

Also called Long R3 IGF-1, LR3-IGF-I, Long Arg3 IGF-I, [Arg3]-IGF-I with N-terminal extension, LongR3-IGF-I

All peptides Last reviewed October 13, 2026
Legal status Research chemical Banned in sport (WADA)
Evidence grade D Animal or cell data only
Human studies 0 published, approximate count
Half-life Not established time for levels to halve
Route studied Subcutaneous injection (animal studies) plus intravenous or osmotic pump infusion (animal studies)
What it is

IGF-1 LR3 is a lab-made version of insulin-like growth factor 1, the hormone the liver releases in response to growth hormone. It has two changes: the glutamic acid at position 3 is swapped for arginine, and a 13-amino-acid tail is added to the front. Together these make it bind very weakly to the IGF binding proteins that normally hold IGF-1 in check in the blood, so more of it is free to hit the IGF-1 receptor. It was developed in Australia in the early 1990s and is sold mainly as a supplement for growing cells in bioreactors.

Every efficacy finding comes from rats and cell cultures. In rats it was 1.5 to 3 times more potent than native IGF-1 at driving weight gain, gut growth and protein synthesis, but in steroid-treated rats it was no better than IGF-1 at preventing muscle loss. No human trial, pharmacokinetic study or safety study of LR3 has been published.

Read the full overview 1 more

What is known about IGF-1 in humans comes from mecasermin (Increlex), recombinant native IGF-1 approved for children with severe IGF-1 deficiency. Its label warns about low blood sugar severe enough to cause seizures, swelling of the tonsils and adenoids, raised pressure in the skull, and cases of cancer in treated children. A one-year trial of IGF-1 injections in healthy older women found no change in muscle, fat, bone or strength. IGF-1 and its analogs are banned in sport at all times.

Structure 83 amino acids, full sequence not drawn
1. Residue 2. Residue 3. Residue 4. Residue 5. Residue 6. Residue 7. Residue 8. Residue 9. Residue 10. Residue 11. Residue 12. Residue 13. Residue 14. Residue 15. Residue 16. Residue 17. Residue 18. Residue 19. Residue 20. Residue 21. Residue 22. Residue 23. Residue 24. Residue N +59 more
Sequence
Human IGF-1 (70 aa) with Glu3 replaced by Arg, preceded by a 13-residue extension (the first 11 residues of methionyl porcine growth hormone plus Val-Asn)
Length
83 amino acids
Molecular weight
About 9.1 kDa
Origin
Recombinant protein produced in E. coli, designed by Australian researchers (Francis, King and colleagues, 1992) as a more potent IGF-1 for research and cell culture
Mechanism

How IGF-1 LR3 works

What it binds to, and what happens inside the body after that, step by step.

Outside the cell Inside the cell
Target Type 1 IGF receptor (IGF-1R) agonist, with some insulin receptor activity

LR3 activates the same receptor as native IGF-1, the type 1 IGF receptor, which switches on the PI3K-Akt and MAPK pathways that drive protein synthesis, cell division and cell survival. Its extra potency comes from barely binding IGF binding proteins, not from binding the receptor more tightly; its receptor affinity is slightly lower than IGF-1. Because it escapes binding proteins, it is also cleared from the blood faster than IGF-1 in rats.

  1. 1 Avoids binding proteins The Arg3 swap and N-terminal tail make LR3 bind poorly to IGFBP-2 and IGFBP-3, which normally hold most IGF-1 in an inactive reservoir.
  2. 2 Binds IGF-1 receptor Free LR3 attaches to IGF-1R on muscle, gut, liver and many other cell types.
  3. 3 Turns on PI3K-Akt and MAPK Receptor activation triggers the signaling pathways that raise protein synthesis and cell division and slow protein breakdown.
  4. 4 Tissue growth in animals In rats this shows up as faster weight gain, larger intestines and higher muscle protein synthesis than with native IGF-1.
  5. 5 Insulin-like effects IGF-1 signaling also pushes glucose into cells, which is why low blood sugar is the leading risk of the approved IGF-1 drug.
The research

What the studies show

Human results and animal results are kept apart below. A result in rats tells you a mechanism is plausible. It does not tell you what happens in a person.

D Evidence

There are no published human studies of IGF-1 LR3: no trials, no pharmacokinetics, no safety data. Rat studies show it is 1.5 to 3 times more potent than IGF-1 for weight gain and gut growth but not better at preventing muscle loss. Human data on native IGF-1 show a real risk of low blood sugar and, in healthy older adults, no gain in muscle or strength over a year.

How far the evidence reaches Highest rung: Randomized trials
  1. Cell studies In a dish 1 key study below
  2. Animal studies Rodents and other models 3 key studies below
  3. Small human studies Open-label, case series 1 key study below
  4. Randomized trials Placebo-controlled RCTs, meta-analyses 1 key study below
  5. Regulatory approval Not approved No
Preclinical: tells you a mechanism is plausible Human: tells you what happened in people (0 published studies, approx.)

In people 2

Randomized trial 2001

One year of IGF-I treatment does not affect bone density, body composition, or psychological measures in postmenopausal women

16 healthy women over 60 (native IGF-1, not LR3)

Blood IGF-1 rose about fivefold, yet lean mass, fat mass, bone density and strength did not change compared with placebo.

Read the study
Case series 2010

Detection of His-tagged Long-R3-IGF-I in a black market product

Seized injection vial analyzed by mass spectrometry

The vial contained a His-tagged lab reagent version of LR3, a form made for biochemistry work whose effects in humans are unknown.

Read the study

In animals and cells 4

Cell / lab 1992

Production and characterization of recombinant IGF-I and potent analogues of IGF-I, with Gly or Arg substituted for Glu3

Rat L6 myoblasts

Arg3 IGF-I bound very poorly to IGF binding protein-2 and was more potent than IGF-I at stimulating protein synthesis, showing the potency comes from escaping binding proteins.

Read the study
Animal 1993

Insulin-like growth factor-I and more potent variants restore growth of diabetic rats without inducing all characteristic insulin effects

Diabetic rats, 7-day infusion

LR3-IGF-I was 2.5 to 3 times more potent than IGF-I at restoring growth, and the IGF peptides raised muscle protein synthesis by up to 50%; unlike insulin, none reduced sugar loss in the urine.

Read the study
Animal 1996

Superior potency of infused IGF-I analogues which bind poorly to IGF-binding proteins is maintained when administered by injection

Normal and dexamethasone-treated rats, 7 days

When infused continuously, LR3 was 1.5 to 2 times more potent than IGF-I for weight gain and organ growth and kept some of that edge with daily injections, but it barely matched IGF-I at preventing muscle loss and cleared from blood faster.

Read the study
Show all 4 studies
Animal 1995

Administration of IGF-I peptides for three days stimulates proliferation of the small intestinal epithelium in rats

Female rats, 3-day infusion

LR3 increased small and large intestine weight by 20% and crypt length by up to 22%; native IGF-I did not.

Read the study
Gaps in the research

What nobody has measured yet

These are questions the published research has not answered.

  1. 01 Half-life, absorption and clearance in humans after subcutaneous or intramuscular injection.
  2. 02 Whether it builds muscle in humans at any dose; native IGF-1 did not in healthy older women.
  3. 03 Long-term cancer risk from a form of IGF-1 engineered to escape the body's binding proteins.
  4. 04 How often it causes hypoglycemia in humans and at what doses.
  5. 05 Immune reactions to the non-human porcine growth hormone tail.
  6. 06 Identity, purity and dose of products sold for injection, which are reagent-grade and unregulated.
History

IGF-1 LR3 from discovery to today

1992201725 years of research history
  1. 1992Australian researchers describe Long [Arg3] IGF-I and show its potency comes from poor binding to IGF binding proteins.
  2. 1993Rat studies show LR3 is 2.5 to 3 times more potent than IGF-I at restoring growth in diabetic rats.
  3. 1996Injected LR3 keeps its potency edge in rats but does no better than IGF-I against steroid-induced muscle loss.
  4. 2005FDA approves mecasermin (Increlex), native recombinant IGF-1, for children with severe IGF-1 deficiency. LR3 is never developed as a drug.
  5. 2010Anti-doping chemists identify a lab-grade His-tagged LR3 in a black market injection vial.
  6. 2017A plasma test for LongR3-IGF-I and its metabolites is published for doping control.
Approval or regulatory milestoneResearch milestone
Pharmacokinetics

How long it stays in the body

Half-life
Not established
Unknown in humans. In rats LR3 is cleared from the blood faster than native IGF-1. The 20 to 30 hour figure repeated online has no published human source.
Routes studied
Subcutaneous injection (animal studies), Intravenous or osmotic pump infusion (animal studies)
Bioavailability
Not measured in humans.
Notes
LR3 binds human plasma proteins more than rat plasma proteins, so rat clearance data may not predict human behavior. In rats a metabolite, (Des1-11)-LongR3-IGF-I, roughly doubled the window in which the drug could be detected. For comparison, the mecasermin label reports a half-life of about 5.8 hours for native IGF-1 in 12- to 22-year-olds.

No human half-life has been published for IGF-1 LR3, so we do not draw a clearance curve. Half-lives quoted online for it are usually estimates from animal data.

Dosing data

Doses used in published studies

No human study or approved label has published a dose for IGF-1 LR3, so there is no table to show.

Studied doses

No dose of IGF-1 LR3 has been tested in a published human study or approved on a label. Numbers that circulate online come from animal studies scaled up by guesswork or from sellers. We do not reproduce them.

Safety

Side effects, higher-risk groups and interactions

6Frequency unknownnot measured in trials
EffectCommonUncommonRareUnknown
Low blood sugar (hypoglycemia)Not measured for LR3 in humans. It is the leading risk of native IGF-1: the mecasermin label warns of hypoglycemic seizures.Frequency unknown
Headache, joint pain, swellingReported with high-dose native IGF-1 in older women over 4 weeks; not studied for LR3.Frequency unknown
Tonsil and adenoid enlargementLabel warning for native IGF-1 in children; not studied for LR3.Frequency unknown
Raised pressure in the skullLabel warning for native IGF-1, with papilledema and headache; not studied for LR3.Frequency unknown
Cancer growthIGF-1 drives cell division; cases of malignancy were reported in children on mecasermin. LR3 is designed to be more available to tissues, and its cancer risk has never been studied.Frequency unknown
Allergic reaction to contaminantsProducts are reagent-grade proteins; a seized vial contained a His-tagged lab form never meant for injection.Frequency unknown
Groups with specific risks
  • Active cancer or a history of cancer (contraindication for native IGF-1 in children)
  • Diabetes or use of insulin or sulfonylureas, because of additive low blood sugar
  • Pregnancy and breastfeeding: no data
  • Children and teens: LR3 has never been studied in them
  • Competitive athletes under WADA rules
Interactions
  • Insulin and other glucose-lowering drugs: additive risk of hypoglycemia expected from IGF-1 receptor and insulin receptor signaling.
  • Growth hormone or growth hormone secretagogues raise native IGF-1, so combining them adds to total IGF-1 receptor stimulation; no study has measured the combination with LR3.

Which symptoms are expected and which mean stop and get help: side effects and red flags.

Claims checked

What people say online, checked against the studies

Tap a claim to see what the studies found.

The claim"IGF-1 LR3 builds muscle by causing new muscle cells to form (hyperplasia)."UntestedNobody has measured this in people

No human study has looked. Cell and rat work shows more protein synthesis and myoblast division, but muscle fiber hyperplasia in adult humans has never been shown for any IGF-1 form.

The claim"LR3 lasts 20 to 30 hours in the body."Not supportedThe evidence does not back this

No human pharmacokinetic study exists. In rats LR3 actually cleared from the blood faster than native IGF-1, because it does not ride on binding proteins.

The claim"It is a safer alternative to growth hormone."Not supportedThe evidence does not back this

There is no human safety data at all. Native IGF-1 carries label warnings for hypoglycemic seizures, intracranial hypertension and malignancy.

The claim"IGF-1 injections reverse age-related muscle loss."Not supportedThe evidence does not back this

A placebo-controlled year of native IGF-1 in women over 60 raised blood IGF-1 about fivefold with no change in lean mass, strength or bone density.

The claim"LR3 targets only muscle."Not supportedThe evidence does not back this

IGF-1 receptors are on almost every tissue. In rats the most striking effect was growth of the intestine, along with other organs.

Untested pairings

Combinations people discuss

These pairings come up often. Almost none have been tested together in a trial, and the evidence note on each says so plainly.

IGF-1 LR3 with PEG-MGF

Bodybuilding forums pair a systemic IGF-1 analog with an IGF-1 splice-variant peptide, claiming one drives growth and the other repair.

EvidenceNeither has any human data, and no animal study has combined them.

Growth hormone secretagogue with IGF-1 LR3

Sold as raising the body's own GH and IGF-1 while adding an analog on top.

EvidenceNo study has tested this combination. It stacks IGF-1 receptor stimulation from two directions with no safety data.

Handling

Storage and stability

Dry powder (lyophilized)

Reagent suppliers ship LR3 freeze-dried for cell culture. There are no published stability data for injection use.

Mixed with water (reconstituted)

No published stability data for any solution intended for injection.

Guide Reconstitution and storage, explainedMembers Bacteriostatic water, fridge vs freezer, and how fast peptides break down.
Keep reading

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New IGF-1 LR3 research, explained when it is published

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Frequently asked questions
What is the difference between IGF-1 and IGF-1 LR3?
LR3 has arginine instead of glutamic acid at position 3 and a 13-amino-acid tail on the front. These changes stop it from being held by IGF binding proteins, so more of it reaches the receptor. Native IGF-1 is the hormone your liver makes and is available as the approved drug mecasermin; LR3 is a lab reagent.
Is IGF-1 LR3 FDA approved?
No. It has never been tested in a human trial and is sold as a cell-culture reagent. The only approved IGF-1 drug in the US is mecasermin (Increlex), for children with severe IGF-1 deficiency.
Does IGF-1 LR3 cause low blood sugar?
It has not been measured in humans, but IGF-1 acts partly like insulin and low blood sugar is the top warning on the approved IGF-1 drug. Rat data show LR3 does not lower glucose as strongly as insulin.
Is IGF-1 LR3 detectable in drug tests?
Yes. WADA bans IGF-1 and its analogues at all times, and anti-doping labs have published mass spectrometry methods that pick up LongR3-IGF-I and its breakdown products in plasma.
Can IGF-1 LR3 cause cancer?
No study has looked. IGF-1 drives cell division, higher IGF-1 levels are linked to some cancers in population studies, and the approved IGF-1 drug lists malignancy as a warning. That risk is unmeasured for LR3.