IGF-LR3
IGF-1 LR3 / Long R3 IGF-1
IGF-LR3 (IGF-1 LR3 / Long R3 IGF-1) is a gh & growth research compound. Modified IGF-1 that resists binding proteins, so it stays active far longer than native IGF-1 — drives anabolism and hyperplasia.
IGF-LR3 quick facts
| Reported research dosing | 25mcg-100mcg |
| Route | Either |
| Cycle length | 4-8 Week |
| Frequency | 1x Daily Post Workout · 5 On 2 Off or Daily |
| Half-life | ~20–30 hrs |
| Forms | Injectable |
| Evidence level | Animal + anecdotal |
Potent and unforgiving — this is deep-end stuff. Blood sugar awareness matters.
How IGF-LR3 works
Modified IGF-1 that resists binding proteins, so it stays active far longer than native IGF-1 — drives anabolism and hyperplasia.
Proposed benefits
Anabolism, muscle hyperplasia and recovery (advanced tool).
Where to get IGF-LR3
Buy IGF-LR3 at AminoWell USA →IGF-LR3 reconstitution calculator
Research reconstitution calculator
The evidence for IGF-LR3
Graded by what exists behind each claim.
Human clinical evidence
- No randomized human trials — a research compound with no commercial route to funding one, so the correlative and theoretical tiers are the evidence base rather than a consolation prize.
📊 Correlative data
- Recombinant IGF-1 itself (mecasermin) IS an approved human drug for severe primary IGF-1 deficiency, and its label is the most useful document here — hypoglycemia is the dose-limiting effect in humans, serious enough to require dosing with food.
- LR3 is a modified analog with far lower binding-protein affinity, so it circulates active for far longer. Nothing about the human data on mecasermin transfers cleanly to it except the direction of the risk.
🧪 How the mechanism reads
- The Long-Arg3 modification prevents IGF-binding-protein capture, extending the active half-life from minutes to hours. That is the whole design and it predicts both effects: much greater anabolic signaling per unit, and much greater hypoglycemia risk than native IGF-1.
- Sustained IGF-1 receptor activation is also the mechanism behind the long-term concern nobody can resolve — IGF-1 signaling promotes proliferation indiscriminately, which is useful in muscle and unwelcome anywhere with an undiagnosed problem.
Why an empty tier is not a verdict →
How to read these tiers: they say how much human evidence exists, not how well something works — and ✗ flags harm, never a disappointing trial. How the evidence tiers work →
What IGF-LR3 actually does
The name says what was done to the molecule, and the market has read it as something else. Long R3 IGF-I is human IGF-I with two changes: arginine substituted at residue 3 in place of the native glutamate, and a 13-residue extension added to the N-terminus. Tomas 1992 describes it in exactly those terms — “a variant with an N-terminal extension as well as arginine at residue 3”. ‘Long’ refers to the peptide extension, not to a long half-life. That single misreading is responsible for most of what is said about this compound, and the published pharmacokinetics run the other way.
What the Arg3 substitution actually does. The N-terminal region of IGF-I contains the contact residues for the IGF-binding proteins, and Glu3 is one of them. Replace it with arginine — swapping a negative side chain for a positive one at a contact point — and the binding-protein interaction is destroyed while the receptor-binding face, which is elsewhere on the molecule, is left intact. The whole design is a targeted disruption of one protein-protein interface. Tomas 1992 calls the resulting peptides “IGF-I analogs that bind poorly to IGF-binding proteins”, alongside the truncated des(1-3)IGF-I which achieves the same thing by deleting the first three residues outright.
Why that matters: in blood, almost no IGF-I is free. Circulating IGF-I is carried in a 150 kDa ternary complex with IGFBP-3 and the acid-labile subunit. That complex is too large to leave the capillary, so it is a reservoir rather than a delivery vehicle, and it is why endogenous IGF-I has a plasma half-life measured in hours rather than minutes. Bastian 1993 shows the contrast directly: in rat plasma, labeled IGF-I was mainly associated with the 150 kDa complex, whereas the majority of LR3IGF-I was detected as free peptide.
Now the fact that almost nobody states, and it is in the first paper. Tomas 1992 reports that the response to LR3IGF-I was “particularly striking because this peptide binds 3-fold less well than IGF-I to the type 1 IGF receptor”. Read that carefully. The analog is a weaker agonist at the receptor it is supposed to activate. Its entire potency advantage comes from escaping the binding proteins, not from engaging the receptor better. Take away the binding-protein problem — as happens in a healthy person who is not catabolic and not on dexamethasone — and what is left is a molecule with a third of native IGF-I's receptor affinity.
And the potency advantage was measured in a specific, artificial situation. In Tomas 1992 the rats were made catabolic with dexamethasone, and the authors attribute the analogs' advantage to the substantially increased plasma IGF-binding protein levels, particularly IGFBP-3, produced by the combined treatment — binding proteins that would sequester IGF-I but not the variants. The advantage is a property of the model, not of the molecule. That is a considerable difference from the way it is sold.
Cell, rodent, human — and where it stops
Step one, catabolic rats, and the numbers are worth quoting. Tomas 1992 gave 150 g male rats 20 µg/day of dexamethasone to produce a catabolic state, with IGF peptides delivered by subcutaneously implanted osmotic pumps. The highest IGF-I dose, 695 µg/day, produced a 6 g gain in body weight over 7 days against a 19 g loss in the dexamethasone-only group and an 18 g gain in pair-fed controls. LR3IGF-I and des(1-3)IGF-I were about 2.5-fold more potent than IGF-I. Muscle protein breakdown fell — 3-methylhistidine excretion from 83.5 ± 4.2 down to 65.1 ± 2.2 µmol/kg per 7 days. And here is the sentence that should be on every vendor page: the IGF analogs increased gut weight by up to 45%, and the authors note part of the 3-methylhistidine response may reflect reduced gut protein breakdown rather than muscle. Fractional carcass weights remained low.
Step two, guinea pigs, and the title is the finding. Conlon 1995: female guinea pigs of 350 g continuously infused for 7 days with 120 µg/day of LR3IGF-I. The fractional weights of adrenals, gut, kidneys and spleen were significantly increased — and overall growth was not stimulated. Body weight gain, feed intake, feed conversion efficiency and carcass composition were unaffected by any treatment. The paper's title states the other half: LR3IGF-I infusion “stimulates organ growth but reduces plasma IGF-I, IGF-II and IGF binding protein concentrations”. So the analog grew the viscera, left the carcass alone, and suppressed the animal's own IGF axis while doing it.
Step three, injection rather than infusion — which is the route people actually use. Tomas 1996 compared osmotic-pump infusion with once- or twice-daily subcutaneous injection at 320 µg/day in normal rats and 400 µg/day in catabolic rats over 7 days. “As expected, continuous infusion of IGFs showed greater efficacy than either of the injection modes”, especially for anti-catabolic effects. Infused, LR3IGF-I was 1.5- to 2-fold more potent than IGF-I; injected, it retained superiority for several endpoints but with “potency much reduced compared with continuous infusion”. And then the sentence that matters most for the use this compound is bought for: “LR3IGF-I was barely equipotent with IGF-I for reversal of carcass muscle loss in dexamethasone-treated rats”. On the muscle endpoint specifically, the expensive analog was level with the ordinary peptide.
Step four, where the drug goes. Bastian 1993 measured tissue distribution of both tracers and found more LR3IGF-I in kidneys, ovaries and adrenals, and more IGF-I than LR3IGF-I in caecum, brain, liver and heart. Bastian 2000 went further and studied transport of circulating IGF-I and LR3IGF-I from blood to extracellular wound fluid sites in rats — the question of whether escaping the binding proteins actually improves delivery to a tissue compartment.
Step five, humans: there is none. No human pharmacokinetic study. No human trial of any kind. No case series. The entire published record for this molecule is rats and guinea pigs from 1992 to 2000. Every number on this page has a species attached to it and none of them is ours.
The obstacles, named. (1) The potency advantage was measured in animals whose binding proteins had been driven up by dexamethasone Tomas 1992; a healthy trained adult is not that model. (2) The endpoints that responded most were visceral organ weights Conlon 1995 Tomas 1992, not carcass muscle. (3) The route that works is continuous infusion, and injection loses most of the advantage Tomas 1996. (4) The analog has threefold lower affinity for the type 1 IGF receptor than the peptide it replaces Tomas 1992, so where binding proteins are not limiting it should be worse. (5) There is no human data at all.
IGF-LR3 pharmacokinetics — how much of it actually gets in
This site's card says about 20–30 hours. The published measurement says the opposite, and by a factor of eleven. Bastian 1993 gave intravenous boluses of radiolabelled peptide to catheterized rats and measured metabolic clearance rate directly. In virgin rats: IGF-I, MCR = 0.90 ± 0.05 mL/min per kg. LR3IGF-I, MCR = 9.84 ± 0.28 mL/min per kg. The analog is cleared from plasma roughly eleven times faster than native IGF-I. The paper states it plainly — “LR3IGF-I was cleared more rapidly than IGF-I from plasma” — and Tomas 1996 repeats it: LR3IGF-I “has very low affinity for the IGF-binding proteins in the rat and hence is cleared from the circulation more quickly than is IGF-I”.
The mechanism of that is the same mechanism as the drug's selling point, which is why it cannot be engineered away. IGF-I lasts in plasma because IGFBP-3 and the acid-labile subunit hold it in a 150 kDa complex that the kidney cannot filter and the capillary cannot leak. Free IGF-I has no such protection. LR3 was designed to not be bound — and an unbound 9 kDa peptide is filtered at the glomerulus and taken up by tissue. Bastian 1993 confirms both ends of that: the majority of LR3IGF-I was detected as free peptide, and more LR3IGF-I tracer was found in the kidneys than IGF-I tracer. You cannot have the escape from binding proteins and the long half-life at the same time. They are the same interaction.
The pregnancy arm of that study is an elegant confirmation. In pregnant rats, whose IGFBP-3 falls dramatically, IGF-I clearance rose from 0.90 to 2.88 ± 0.12 mL/min per kg — moving toward the analog's rate — while LR3IGF-I clearance was unchanged at 9.19 versus 9.84 Bastian 1993. Reduce the binding proteins and native IGF-I starts behaving like LR3. That is as clean a demonstration as this field offers that binding-protein association is the half-life.
What degrades it, and where. Bastian 1993 also reports that a larger proportion of tracer appeared as small molecular-weight breakdown products in plasma under conditions of reduced binding-protein association — in pregnancy, and when LR3IGF-I was the tracer — suggesting greater rates of IGF degradation. Unbound peptide is proteolysed; bound peptide is protected. So the analog is not only cleared faster, it is destroyed faster.
What that means for a once-daily injection. Tomas 1996 measured exactly this and found continuous infusion clearly superior to once- or twice-daily injection for the same total dose, with the gap largest for anti-catabolic actions. A molecule with an elevenfold clearance rate given once a day produces a brief spike and a long trough — and the animal data says the trough is where the effect is lost. Anyone injecting this once daily is using the schedule the published work identified as the weaker one.
What would have to be true, and how you would know it was not
Four predictions with a marker, a direction and a window. The first runs opposite to what almost everyone expects, and it is measured rather than reasoned.
1. Your IGF-1 result should FALL, not rise. Two independent reasons, and they compound. First, Conlon 1995's own title: LR3IGF-I infusion “reduces plasma IGF-I, IGF-II and IGF binding protein concentrations” — exogenous IGF signaling suppresses pituitary growth hormone, and hepatic IGF-I production follows it down. Second, a standard clinical IGF-1 immunoassay is raised against native human IGF-I; LR3 carries a 13-residue N-terminal extension and a substitution at residue 3 Tomas 1992, and whether any given assay recognizes it is unknown. Draw IGF-1 at baseline and at 4 weeks. A falling IGF-1 on this compound is the expected result and is not evidence that it is not working. A large rise would be more surprising and would point at the vial containing something else — growth hormone or a secretagogue, both of which raise native IGF-1 reliably.
2. Fasting glucose should fall and hypoglycemia is the acute risk. IGF-I at high concentrations activates the insulin receptor as well as its own, and the free, unbuffered peptide is precisely the form that reaches those receptors Bastian 1993. Draw Fasting Glucose and Fasting Insulin at baseline and 4 weeks, and — far more usefully — measure capillary glucose symptomatically in the two hours after a dose. This is the one prediction on the page with a same-day read-out.
3. The prediction that cuts against it: lean body mass should not move much. The endpoints that responded in animals were gut, kidney, spleen and adrenal weights; carcass fractional weight stayed low in Tomas 1992, overall growth was not stimulated in Conlon 1995, and on the specific endpoint of carcass muscle reversal, LR3IGF-I was “barely equipotent with IGF-I” Tomas 1996. Measure lean mass by DEXA at baseline and 12 weeks, with training and protein intake held constant. If lean mass rises substantially, that contradicts three separate rodent studies and is worth documenting carefully.
4. Watch for the visceral endpoint, because it is the one the animals actually showed. Tomas 1992 reported gut weight up by as much as 45%. There is no blood marker for intestinal mass. The observable is waist circumference measured at the navel, fasted, first thing, weekly, held against DEXA lean mass. A rising waist with unchanged lean mass and unchanged body fat is the human shadow of the rodent finding, and nobody has looked for it.
What nobody has tested yet
Nobody knows whether a clinical IGF-1 assay detects this molecule. This is the most answerable question on the page and the most consequential: spike LR3IGF-I into serum at known concentrations and run it on the common commercial IGF-1 platforms. One afternoon in any clinical chemistry laboratory. Until somebody does it, every IGF-1 result taken by a person using this compound is uninterpretable — a low number could mean suppression of endogenous IGF-I, or simply an assay that cannot see the analog, and those have opposite implications.
Nobody has measured the pharmacokinetics in a human. The elevenfold clearance figure is a rat number from 1993 Bastian 1993. Humans have a different IGFBP-3 and acid-labile subunit system and a different renal clearance. A single-dose study in eight volunteers with serial sampling would produce the half-life that this site's card currently reports without a source.
Nobody has tested continuous delivery against injection in a human. Tomas 1996 found the route mattered more than the molecule in rats. A subcutaneous pump versus once-daily injection, same total dose, with DEXA and nitrogen balance, would answer whether the anabolic claim survives the schedule everybody actually uses. It has never been attempted.
Nobody has looked for the gut effect in a person. A 45% increase in gut weight Tomas 1992 is an enormous, reproducible animal finding for a peptide taken by people for aesthetic reasons. Abdominal imaging — ultrasound bowel wall thickness, or MRI visceral organ volumes — before and after a cycle would be straightforward and has never been published.
IGF-LR3 — its own safety story, not its class's
There is no human safety data for this compound. None. No trial, no case series, no pharmacovigilance. Everything below is either a rodent observation or a mechanism-level inference, and it is labeled as such, because inventing a human risk profile for a molecule that has never been given to a person in a study would be worse than saying this plainly.
Hypoglycemia is the acute hazard and it is mechanistic rather than speculative. IGF-I and insulin receptors are close relatives and IGF-I activates the insulin receptor at high concentrations. LR3 circulates as free peptide Bastian 1993 rather than in the 150 kDa reservoir, which means the concentration available to any receptor is higher for the same dose than it would be for native IGF-I. Anyone using this fasted, before training, or alongside insulin or a GLP-1 agonist is combining that with the other things that lower glucose.
The organ-growth pattern is the risk nobody discusses. Across two species and three studies, what grew was gut, kidneys, spleen and adrenals — gut by up to 45% Tomas 1992, and adrenals, gut, kidneys and spleen with no increase in overall growth in guinea pigs Conlon 1995. The tissue distribution data points the same way: more LR3IGF-I tracer in kidneys, ovaries and adrenals than IGF-I tracer Bastian 1993. A growth factor concentrating in the kidney and driving visceral organ mass is not a reassuring profile, and no one has measured renal function on it in any species over any duration.
The proliferation question, stated as the open question it is. IGF-1 receptor signaling is mitogenic and anti-apoptotic; that is what a growth factor does. A molecule engineered specifically to escape the binding proteins that normally restrain how much free IGF activity reaches tissue is, by design, delivering more unbuffered mitogenic signal than the physiological system permits. Nobody has run a carcinogenicity study on LR3IGF-I. The direction of the concern is not controversial; its magnitude in a person is entirely unmeasured.
And the suppression of your own axis, which is the one thing here with a published measurement. Conlon 1995 reports LR3IGF-I infusion reducing plasma IGF-I, IGF-II and IGF binding protein concentrations. That is negative feedback working as designed, and it means the compound is not additive to your endogenous production — it partly replaces it. What happens to that axis after a cycle stops has not been measured in any species, which makes the recovery period the single largest blank on this page.
Sources read for this page
- Tomas FM, Knowles SE, Owens PC, Chandler CS, Francis GL, Read LC, Ballard FJ. Insulin-like growth factor-I (IGF-I) and especially IGF-I variants are anabolic in dexamethasone-treated rats.. Biochem J 1992 · PMID 1371669
- Bastian SE, Walton PE, Wallace JC, Ballard FJ. Plasma clearance and tissue distribution of labelled insulin-like growth factor-I (IGF-I) and an analogue LR3IGF-I in pregnant rats.. J Endocrinol 1993 · PMID 7693845
- Conlon MA, Tomas FM, Owens PC, Wallace JC, Howarth GS, Ballard FJ. Long R3 insulin-like growth factor-I (IGF-I) infusion stimulates organ growth but reduces plasma IGF-I, IGF-II and IGF binding protein concentrations in the guinea pig.. J Endocrinol 1995 · PMID 7561636
- Tomas FM, Lemmey AB, Read LC, Ballard FJ. Superior potency of infused IGF-I analogues which bind poorly to IGF-binding proteins is maintained when administered by injection.. J Endocrinol 1996 · PMID 8708565
- Bastian SE, Walton PE, Belford DA. Transport of circulating IGF-I and LR3IGF-I from blood to extracellular wound fluid sites in rats.. J Endocrinol 2000 · PMID 10607940
IGF-LR3 — safety, predicted from mechanism
Predicted from mechanism, not from a human safety trial. How that reasoning works →
What the mechanism predicts
Derived from the molecule, not a trial.
- Everything here follows from one fact: these raise GH and therefore IGF-1. The predicted problems are the known consequences of elevated GH/IGF-1, drawn from acromegaly and clinical GH therapy where it HAS been studied — insulin resistance and rising fasting glucose, fluid retention (puffy hands and face, and the ring that stops fitting), carpal tunnel symptoms from that same fluid pressing on the median nerve, and joint aches.
- The proliferation question is the serious one. IGF-1 is a growth signal, and growth signals do not distinguish between tissue you want to grow and tissue you do not. There is no evidence these compounds cause cancer. There is also a clear mechanistic reason not to run them with an active or recent malignancy, and that reasoning does not require a trial to be sound.
What has actually been reported
- Injection-site reactions, transient flushing, tingling and head-rush on dosing — most commonly with the GHRPs, which also release cortisol and prolactin at higher doses.
- Increased hunger is near-universal with the ghrelin-mimetic ones (GHRP-6, MK-677, Hexarelin). That is the mechanism working, not a side effect — the same receptor drives GH release and appetite.
How to reduce the risk
Same mechanism as the prediction.
- Draw an IGF-1 baseline BEFORE you start. Once you are on, that number is the drug and you have permanently lost the comparison. This is the single highest-value thing on this list and it costs one blood draw.
- Watch fasting glucose and HbA1c, not the scale. Insulin resistance is the most likely thing to move and the one you cannot feel. Re-test at 8–12 weeks. If fasting glucose is climbing, that is your signal to cut the dose or come off — long before anything shows up symptomatically.
- Dose at night, on an empty stomach. GH release is pulsatile and largest during early sleep; food, and carbohydrate in particular, blunts the pulse through insulin. This is not a ritual — it is the same mechanism working with you rather than against you.
- Don't run a secretagogue through a high-carbohydrate surplus. The predicted problem is insulin resistance; adding a large carb load is pushing the same lever from the other end.
- Cycle rather than run continuously. Most of the predicted problems — fluid retention, carpal tunnel, glucose drift — are dose-and-duration dependent and reverse on cessation. Time off is the cheapest safety intervention available.
- If fluid retention is the issue, it usually resolves on a dose reduction long before it needs anything else. Reach for the dose before you reach for a diuretic.
What it does to your bloodwork
A fact about the assay.
- IGF-1 drawn on-cycle is not your baseline — it is the drug working, and it will read high. If you want a real baseline, draw before starting or after a proper washout.
- Watch fasting glucose and HbA1c, because insulin resistance is the most likely thing to move and the one you will not feel.
- GHRP-6 and Hexarelin can raise prolactin and cortisol; if you are chasing an unexplained prolactin result, this is a candidate.
What it overlaps with
- Stacking two secretagogues that work by the same route is redundancy, not synergy. A GHRH analog (CJC-1295, Sermorelin, Tesamorelin) plus a ghrelin mimetic (Ipamorelin, GHRP-2, GHRP-6) is the deliberate pairing — two different levers on the same axis. Two GHRH analogs together is paying twice for one lever.
Don't run this if
- Active or recent malignancy — the IGF-1 reasoning above.
- Diabetes or poor glycemic control, unless you are monitoring fasting glucose and HbA1c and know what you are looking at.
- Untreated diabetic retinopathy.
The honest unknown
- Nobody has run long-term studies of intermittent secretagogue use in healthy adults. The specific unmeasured thing is what years of repeatedly pushing IGF-1 above your natural set point does — not whether a single cycle is tolerable, which it evidently is.
Not medical advice. If you take prescription medication or have a diagnosed condition, check this with a pharmacist or doctor.
Fasted, and away from food either side
The fasted flag is on this one for a reason — food measurably reduces how much reaches circulation. An hour before eating, or two hours after, is the practical version.
From half-life and route, not a dosing trial.
IGF-LR3 — interference & stacking
Predicted from mechanism, not from an interaction study. How mechanism-predicted claims are made →
What IGF-LR3 moves on your bloodwork
Expected direction, not a measured one.
- IGF-1 (Insulin-like Growth Factor 1) — ↑ expected to rise
This is the point. IGF-1 rising is the compound doing its job — it is the stable downstream readout of a GH pulse.
What to do: Test it before you start and again at 6–8 weeks. It is the only number that tells you whether the product was real and the dose was enough. - Growth Hormone, Serum — ✕ unreliable here
A random GH level is close to meaningless here. GH is secreted in pulses during deep sleep and sits undetectable between them, so a daytime draw catches a trough almost every time — including when the compound is working perfectly.
What to do: Do not use GH to judge a secretagogue. Read IGF-1 instead. - Fasting Insulin — ↑ expected to rise
GH is a counter-regulatory hormone: it opposes insulin. Fasting insulin and glucose drifting up is the predicted trade-off, not a surprise.
What to do: Check fasting insulin and HbA1c at baseline and again at 8–12 weeks. This is the marker that decides whether you keep running it. - HbA1c (Hemoglobin A1c) — ↑ expected to rise
Same mechanism, longer window — a slow drift rather than a jump.
What to do: Pair it with fasting insulin; either alone can mislead. - Free T4 (Thyroxine) — ↓ expected to fall
GH accelerates the peripheral conversion of T4 to T3, so free T4 can fall while free T3 holds or rises. Read alone it looks like new hypothyroidism, and it usually isn't.
What to do: Run a full thyroid panel rather than TSH alone before concluding anything.
Everything above follows from one fact: these raise GH and therefore IGF-1. Nothing here needs a trial of the specific molecule.
Everything on this page, in an order
This one is free and stays free. What Skool adds is the rest of the shelf — 278 compounds and 371 supplements with the protocol, the stack order and the bloodwork to run beside it.
Join Skool — $10/mo →Bloodwork to run alongside IGF-LR3
Baseline first, then again at 8–12 weeks.
| Marker | What it’s watching for |
|---|---|
| Comprehensive Metabolic Panel (CMP) | Fasting glucose. IGF-1 analogs cause genuine hypoglycemia, not theoretical |
| IGF-1 (Insulin-like Growth Factor 1) | Baseline before adding exogenous IGF on top |
| Fasting Insulin | The whole axis you're manipulating |
| HbA1c (Hemoglobin A1c) | Longer-term glycemic picture |
The “Running GH Peptides or MK-677” panel covers these in one order — 9 markers, $132.30 with the discount applied.
Check results you already have → · All 103 markers A–Z
IGF-LR3 — frequently asked questions
What is IGF-LR3?
IGF-LR3 (IGF-1 LR3 / Long R3 IGF-1) is a gh & growth research compound. Modified IGF-1 that resists binding proteins, so it stays active far longer than native IGF-1 — drives anabolism and hyperplasia.
What dosing does the research reference for IGF-LR3?
In the research literature, IGF-LR3 is referenced in the 25mcg-100mcg range, 1x Daily Post Workout · 5 On 2 Off or Daily. It is supplied as a lyophilized powder and reconstituted with acetic acid; the calculator above converts a research amount into syringe units. For research use only — not a recommendation for human use.
What is the half-life of IGF-LR3?
IGF-LR3 has an approximate half-life of ~20–30 hrs, which is part of what determines how often it's dosed.
What's the evidence behind IGF-LR3?
Current evidence level: Animal + anecdotal. IGF-LR3 is offered for research purposes only and is not an approved medicine.
IGF-LR3 inside a finished plan
One arm of 1 Protocol Blueprint, free to read in full.
What IGF-LR3 is used for
IGF-LR3 appears under 1 goal in the goal router.
Related GH & Growth compounds
Where this goes next
IGF-LR3 is the gh / igf-1 arm of this plan. The page above is the free breakdown of one compound; the plan it belongs to — the dosing, the order to correct things in, the week-by-week schedule and what to retest — is a lesson inside Skool.