GHRH Analog / SubQ / 200-500mcg daily, before bed
Sermorelin
Growth hormone-releasing hormone was characterized in 1982, not from the hypothalamus that makes it but from pancreatic tumors that had poured it into two patients and given them acromegaly. Sermorelin is a shortened copy of that sequence, synthesized and bioassayed in the same year by the group that sequenced it.
In plain words
Sermorelin is a shortened lab-made copy of growth hormone-releasing hormone, the natural signal that tells the pituitary gland to release growth hormone; it keeps the first 29 of that hormone's 44 building blocks. Rather than supplying growth hormone itself, it prompts the body to release its own. It was once an approved medicine in the United States, first as a test of whether the pituitary can still secrete growth hormone and later for growth failure in children, but the maker discontinued it and the approvals were withdrawn in 2009; regulators later determined that this was not for reasons of safety or effectiveness, the market had simply gone to lab-made growth hormone. The human evidence is thin and mixed: the children's study had no placebo group, and in the one small placebo-controlled trial in older adults the IGF-1 rise drifted back toward the starting point while treatment continued, lean mass rose in the men and not the women, and fat mass and bone density changed in neither. It is broken down in the blood within minutes, and with no approved product it now reaches people through compounding pharmacies, hormone clinics and research-chemical sellers, where community reports cluster on sleep and recovery rather than any visible change in body composition.
At a glance
| Half-life | 0.007 days |
|---|---|
| Tmax | 0.003 days |
| Route(s) | SubQ |
| Published dosing range | 200-500mcg daily, before bed |
| Vial strengths | 2, 5, 9, 15 mg |
Reference data from the DosePlot canon -- not a protocol recommendation.
Serum curve
Single 350 mcg dose by SubQ, rendered from the same engine that powers the interactive chart. Relative levels, not lab values.
What does the evidence show?
Two things are labeled separately here because they answer different questions. The tier is how a study was built. The distance chips are whether that study touched this molecule, by this route, in a population resembling the reader. A randomized trial of a different molecule keeps its tier and still says nothing about this compound.
| Finding | Tier | Distance from use | Study |
|---|---|---|---|
| One year of once-daily sermorelin at 30 mcg/kg, injected under the skin at bedtime, raised height velocity in growth-hormone-deficient children from 4.1 cm/yr at baseline to 8.0 cm/yr at six months and 7.2 cm/yr at twelve months. The trial was multicenter but open-label, with no placebo or comparator arm. | clinical | not recorded | Thorner M, Rochiccioli P, Colle M, et al. Once daily subcutaneous growth hormone-releasing hormone therapy accelerates growth in growth hormone-deficient children during the first year of therapy.Journal of Clinical Endocrinology and Metabolism 81(3):1189-1196, 1996 |
| In short prepubertal children who were not growth hormone deficient, twice-daily GHRH(1-29) amide at 20 mcg/kg raised height velocity from 4.8 to 7.2 cm/yr over twelve months. Growth slowed to 3.9 cm/yr during the three months after treatment stopped and returned to the pretreatment rate thereafter. | clinical | not recorded | Kirk JM, Trainer PJ, Majrowski WH, et al. Treatment with GHRH(1-29)NH2 in children with idiopathic short stature induces a sustained increase in growth velocity.Clinical Endocrinology 41(4):487-493, 1994 |
| In a single-blind, randomized, placebo-controlled trial, 19 adults aged 55 to 71 self-injected nightly saline for four weeks and then a GHRH(1-29) analog nightly at 10 mcg/kg for sixteen weeks. IGF-1 rose within two weeks and then drifted back toward baseline by week 16 while dosing continued. Lean body mass rose in the men and not in the women; fat mass and bone mineral density changed in neither. | rct | not recorded | Khorram O, Laughlin GA, Yen SS. Endocrine and metabolic effects of long-term administration of [Nle27]growth hormone-releasing hormone-(1-29)-NH2 in age-advanced men and women.Journal of Clinical Endocrinology and Metabolism 82(5):1472-1479, 1997 |
| Six weeks of a single 2 mg nightly injection in healthy men aged 64 to 76 increased nocturnal growth hormone release and pulse amplitude, and improved two of six strength measures, but left IGF-1, IGF-binding protein 3, weight, body composition by DEXA, muscle histology, and lipids unchanged. The authors concluded that one nightly dose is less effective than multiple daily doses. | clinical | not recorded | Vittone J, Blackman MR, Busby-Whitehead J, et al. Effects of single nightly injections of growth hormone-releasing hormone (GHRH 1-29) in healthy elderly men.Metabolism 46(1):89-96, 1997 |
| On cultured rat pituitary cells, GHRH(1-29) amide releases growth hormone with full intrinsic activity at roughly half the potency of the full-length hormone. Further shortening keeps costing potency without abolishing activity until residue 19, where activity disappears; the minimal active core is residues 3 to 21. | preclinical | not recorded | Ling N, Baird A, Wehrenberg WB, et al. Synthesis and in vitro bioactivity of C-terminal deleted analogs of human growth hormone-releasing factor.Biochemical and Biophysical Research Communications 123(2):854-861, 1984 |
| Plasma dipeptidyl peptidase IV cleaves GHRH(1-29) amide at the 2-3 bond exactly as it cleaves the native hormone, and a D-amino acid at position 1 or 2 blocks the cut. The shortened peptide also acquires a trypsin-like cleavage after residue 12 that the native hormone does not show. | preclinical | not recorded | Frohman LA, Downs TR, Heimer EP, Felix AM. Dipeptidylpeptidase IV and trypsin-like enzymatic degradation of human growth hormone-releasing hormone in plasma.Journal of Clinical Investigation 83(5):1533-1540, 1989 |
| At the 200 to 500 mcg nightly range typical of unregulated use, community reports cluster on sleep depth and recovery rather than visible change in body composition, and generally treat sermorelin as the weakest and shortest-acting member of the GHRH family, displaced in practice by longer-acting analogs. | anecdotal | not recorded | community reports aggregated from reddit, MESO-Rx, and similar forumsno study |
How did it get here?
- preclinical1982
- Two groups purify growth hormone-releasing factor from human pancreatic tumors that had caused acromegaly. Guillemin and colleagues, in Science, report the full 44-residue structure ending in an amide. Spiess, Rivier, Thorner and Vale, in Biochemistry, establish 39 residues by sequencing and propose a 40-residue free acid; the same paper reports that synthetic hpGRF(1-29) amide is already as active in vitro as the full-length material. A hypothalamic hormone is solved from a tumor because the human hypothalamus yields far too little of it.
- preclinical1984
- Ling and colleagues delete the C-terminus one residue at a time and find that potency stops falling around position 31 and holds through GHRH(1-29) amide. Twenty-nine residues becomes the working scaffold for sermorelin and for the short GHRH analogs built on it. It does not become the only one: tesamorelin, approved in the United States in 2010 and marketed as EGRIFTA SV, carries the full 44-residue sequence with a hexenoyl group attached at the N-terminal tyrosine.
- first-human1985
- Thorner and colleagues give pulsed growth hormone-releasing factor by subcutaneous pump to two growth-hormone-deficient children for six months. One child's growth rate goes from 4.6 to 7.1 cm/yr, the other from 2.1 to 13.7 cm/yr. The report closes by calling it premature to say how useful the approach will prove.
- clinical-adoption1990
- FDA approves Geref, 0.05 mg base per ampoule, on December 28 under NDA 19-863 as a pituitary function test: a single intravenous dose to see whether the somatotrophs can still secrete growth hormone at all.
- clinical-adoption1997
- FDA approves the 0.5 mg and 1 mg treatment vials on September 26 under NDA 20-443, for idiopathic growth hormone deficiency in children with growth failure. Recombinant growth hormone is already the standard of care, and sermorelin never displaces it.
- grey-market2008-present
- EMD Serono tells FDA both products are discontinued (letters dated July 11 and December 2, 2008) and FDA withdraws the approvals in 2009. FDA determined in 2013 that neither was pulled for reasons of safety or effectiveness; the market had simply gone to recombinant growth hormone. With no approved product, sermorelin reaches users through compounding pharmacies, hormone clinics, and research-chemical vendors, sold as a lyophilized powder the buyer reconstitutes.
How is it made?
Sermorelin is built by solid-phase peptide synthesis, in four stages.
1. Building the chain. The peptide is assembled on a resin bead one residue at a time, from the C-terminal arginine back to the N-terminal tyrosine. Each cycle couples one amino acid whose side groups are masked, then removes the mask so the next can attach. Twenty-nine cycles. The resin chosen at the outset fixes the C-terminal amide, matching the natural hormone's amidated end.
2. Cleaving and purifying. Strong acid frees the chain from the resin and strips the side-chain protection in one step. What comes off is not pure sermorelin. Any cycle running at 99 percent instead of 100 leaves chains short a residue, and twenty-nine cycles accumulate a family of near-identical shortfalls. Reversed-phase chromatography separates them. Purity is won or lost here, not in the synthesis.
3. Salt and drying. The purified peptide is isolated as an acetate salt and freeze-dried with a bulking agent. The dry form is not packaging convenience: in neutral solution at body temperature the asparagine at position 8 rearranges into a far weaker peptide.
4. Filling. Sterile filtration, aseptic fill, then batch testing for identity, peptide content, water, sterility, and endotoxin. The chemistry is textbook and the sequence is public. What varies outside regulated manufacturing is how much of a labeled milligram is peptide rather than acetate and water, how many deletion sequences ride along, and whether the fill was sterile.
Worth knowing
Sermorelin carries a slow chemical self-destruct in its own sequence. In neutral solution at body temperature the asparagine at position 8 rearranges, and the rearranged peptide is 400 to 500 times weaker at releasing growth hormone. Swapping that asparagine for serine stretched a related analog's solution half-life from 202 hours to 1550 hours. It is a large part of why the peptide ships freeze-dried rather than premixed.
Friedman AR, Ichhpurani AK, Brown DM, et al. Degradation of growth hormone releasing factor analogs in neutral aqueous solution is related to deamidation of asparagine residues. Replacement of asparagine residues by serine stabilizes.International Journal of Peptide and Protein Research 37(1):14-20, 1991
Long-acting GHRH analogs patch the same four known weak spots. Campbell and colleagues, working on hGRF(1-32) free-acid analogs rather than the 29-residue chain, swapped the human Tyr1-Ala2 pair for the mouse His1-Val2 pair, which shut down dipeptidyl peptidase IV cleavage completely over a 24-hour incubation; substituted residue 8 to slow the asparagine rearrangement; used Ala15, already known to raise receptor binding affinity; and used Leu27 in place of the oxidizable methionine. Sermorelin has the native residue at all four positions, which is much of why it is also the shortest-acting.
Campbell RM, Stricker P, Miller R, et al. Enhanced stability and potency of novel growth hormone-releasing factor (GRF) analogues derived from rodent and human GRF sequences.Peptides 15(3):489-495, 1994
Anti-doping laboratories test for the peptide's leftovers as much as the peptide itself. Working across four GHRH analogs including sermorelin, one group identified nineteen major in vitro metabolites, synthesized and characterized them in house, and spiked them into urine as reference materials alongside the parent peptides and a separately sourced sermorelin metabolite, sermorelin(3-29) amide, which is what remains after dipeptidyl peptidase IV takes the first two residues off.
Memdouh S, Gavrilovic I, Ng K, Cowan D, Abbate V. Advances in the detection of growth hormone releasing hormone synthetic analogs.Drug Testing and Analysis 13(11-12):1871-1887, 2021
Reconstitution
Sermorelin ships lyophilized and is mixed before use; the published vial strengths are 2, 5, 9, 15 mg. The water volume you add sets the concentration, not the dose -- the calculator turns a vial size and a water volume into mg/mL, draw volume, and units on an insulin syringe.
Open in the reconstitution calculatorWritten and reviewed by Evan Marlow, developer of DosePlot · Updated 2026-08-27
Not medical advice. DosePlot is an informational tool, not a healthcare provider, and using it creates no provider-patient relationship. Do not start, stop, or change any protocol without the approval of a licensed healthcare professional.
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