Sermorelin — identity, handling and published literature

Sermorelin is a synthetic 29-residue peptide, the C-terminally amidated 1–29 fragment of human growth hormone-releasing hormone, supplied as a sterile lyophilised powder for laboratory reconstitution.

Presentation and physical properties

Sermorelin is the shortest fragment of human GHRH that retains full activity at the GHRH receptor in the published pharmacology, which is why the 1–29 sequence became the reference structure for the whole GHRH-analogue series. It is normally handled as the acetate salt. The free base has a molecular formula of C₁₄₉H₂₄₆N₄₄O₄₂S and an average molecular mass of approximately 3358 g/mol; an acetate-salt preparation will weigh more than the free-base figure for the same peptide content, and the certificate of analysis for a given lot states the peptide content separately from the gross weight. Where a nominal vial content is quoted without qualification it should be read as free-base peptide unless the supplier’s documentation says otherwise, because the difference propagates directly into every concentration calculated from it.

The lyophilisate is a white to off-white amorphous cake or powder. It is hygroscopic and carries a strong static charge when dry, so material is readily lost to the walls of a vial or a weighing boat. Solubility in water and in aqueous buffers is good at the concentrations used for laboratory work; the sequence carries three arginine and two lysine residues against two aspartate residues, giving a basic net charge at neutral pH, and dilute acetic acid is the conventional first choice where a lot dissolves slowly in water alone.

Two residues govern the chemical behaviour of the molecule more than any others. The first is the N-terminal tyrosine–alanine pair, which is the recognised substrate motif for dipeptidyl peptidase-4 and is the principal route by which GHRH-family peptides are degraded in biological matrices. The second is the methionine at position 27, a thioether that oxidises to the sulfoxide on exposure to air, peroxide traces or light. That oxidation liability is the explicit reason a norleucine-substituted variant, [Nle²⁷]GHRH(1-29)NH₂, was synthesised and used in some of the human literature [14]: norleucine is isosteric with methionine but has no sulfur to oxidise. A laboratory working with sermorelin should treat any assay of the peptide as an assay in which methionine sulfoxide is a plausible, and separately detectable, impurity.

Reconstitution arithmetic

Reconstitution is a single division. The concentration of the resulting solution is the mass of peptide in the vial divided by the volume of diluent added:

concentration (mg/mL) = vial content (mg) ÷ diluent volume (mL)

Multiplying the result by 1000 converts it to micrograms per millilitre. The arithmetic below is worked for four nominal vial contents at three common diluent volumes. It is arithmetic only; it states no target amount of any kind, and nothing in this table should be read as one.

Three arithmetical points are worth stating because each is a common source of error in laboratory records. First, the peptide itself contributes negligible volume at these masses, so the final volume can be taken as the diluent volume; the error introduced is far smaller than the tolerance on the diluent measurement. Second, graduated syringes marked in units are marked in volume, not in mass: on a U-100 syringe, 100 unit marks correspond to 1 mL, so one unit mark is 0.01 mL and ten unit marks are 0.1 mL. Converting a mark to a mass therefore requires the concentration from the table above and nothing else. Third, the relationship is linear in both directions, so halving the diluent volume doubles the concentration exactly — there is no correction term.

What the arithmetic cannot supply is any figure for how much peptide an experiment should use. That is a matter for the protocol, the ethics or institutional approval covering the work, and the investigator; it is not a property of the compound and it is not published here.

Storage and stability

The lyophilised powder is the stable form and should be kept as a lyophilisate for as long as possible. Conventional laboratory practice for peptides of this class is storage at −20 °C or below, sealed, desiccated and protected from light, with long-term stores at −80 °C. Because the material is hygroscopic, a vial taken from a freezer should be allowed to reach room temperature fully before the seal is broken; opening a cold vial draws in moist air that condenses onto the cake and starts hydrolysis in what is nominally a dry store.

Once in solution the peptide is markedly less robust. Reconstituted material is normally held at 2–8 °C, protected from light, and repeated freeze–thaw cycling is avoided by aliquoting at the point of reconstitution rather than by returning a single working vial to the freezer. Where a solution will be entered more than once, a bacteriostatic diluent is the usual choice; where a single-use sterile solution is wanted, water for injection or a defined buffer is used instead. Neither choice changes the arithmetic above.

The oxidation liability at methionine 27 makes headspace air, light and any peroxide-bearing container or stopper material a real stability variable rather than a theoretical one, and it is the reason a solution stored for an extended period should be re-assayed rather than assumed intact. Susceptibility to enzymatic cleavage is a separate matter and applies specifically to biological matrices: González-López and colleagues characterised the enzymatic and serum stability and the degradation profile of GHRP- and GHRH-related peptides, sermorelin among them [20]. Memdouh and colleagues studied the in vitro metabolism of four of the larger GHRH synthetic analogues, sermorelin included, and identified nineteen metabolites across the set [5]. Both findings bear on how a sample containing the peptide must be collected, stored and analysed, not on how a dry vial is kept on a shelf.

Analytical identity

Identity and purity for a peptide of this size are established by orthogonal methods, and no single result is sufficient on its own.

Reversed-phase HPLC with ultraviolet detection at 214 nm gives the purity figure quoted on a certificate of analysis and resolves the principal process-related impurities: deletion sequences, truncated chains and, for this molecule in particular, the methionine sulfoxide form, which typically elutes earlier than the parent under standard water/acetonitrile gradients because it is more polar.

Electrospray ionisation mass spectrometry confirms the mass. At an average mass near 3358 Da the peptide ionises into a multiply charged envelope; calculated from the average mass, the triply protonated species falls near m/z 1120 and the quadruply protonated species near m/z 840. These are approximations from the average mass, and a high-resolution instrument should be worked against the monoisotopic value. One specific check matters for this compound: the C-terminal amide differs from the corresponding free acid by only about 0.98 Da, so a method must have sufficient resolution and mass accuracy to distinguish sermorelin from its free-acid analogue. A synthesis that has failed at the amidation step will otherwise pass a low-resolution mass check.

Sequence confirmation is by tandem mass spectrometry of the b- and y-ion series, or by Edman degradation where a laboratory has the capability. Amino acid analysis after hydrolysis gives the residue ratios and, crucially, the peptide content of the salt — the figure that governs whether a nominal vial content means what the label says.

A substantial anti-doping literature has developed methods for detecting sermorelin and related GHRH analogues in human matrices, and it is the most methodologically detailed body of analytical work on the compound. Knoop and colleagues reported qualitative identification of growth hormone-releasing hormones in human plasma by immunoaffinity purification with LC-HRMS/MS [17]; Coppieters and colleagues described an antibody-free, ultrafiltration-based assay for the same class [18]; Uçaktürk and Nemutlu reported analysis of GHRH and its analogues in urine by nano liquid chromatography [19]; and Memdouh and colleagues developed an LC-MS/MS method reaching detection limits at or below 1 ng/mL, meeting the performance level required by WADA [5].

What the published literature investigated

In vitro and in silico

Chang and colleagues screened 4865 drugs against transcriptomic data from 1018 glioma cases and reported that recurrent glioma samples scored as most sensitive to sermorelin in their computational model; they followed the screen with cell viability assays in the U87 and LN229 glioma cell lines and reported dose- and time-dependent inhibition [4]. The work is a drug-repositioning screen with in vitro follow-up. No clinical study of sermorelin in glioma has followed it.

Memdouh and colleagues characterised the in vitro metabolism of sermorelin alongside tesamorelin, CJC-1295 and CJC-1295 with drug affinity complex, identifying nineteen metabolites across the four analogues as the basis for an anti-doping detection method [5].

Rodent

Lance and colleagues used GRF(1-29)-amide as the parent molecule against which a series of substituted analogues was compared for growth hormone release in rats, reporting that [D-Ala²]-hpGRF(1-29)-NH₂ was approximately fifty times more potent than the parent in that model [2]. The paper is one of the earliest structure–activity studies on the 1–29 fragment and is the origin of the substitution strategy that later analogues in this class use.

Girard and colleagues administered human GHRH(1-29)NH₂ to young and aged rats over fourteen days and examined regulation of the pituitary GHRH receptor, reporting that the higher of two exposures restored age-related declines in receptor binding parameters and normalised transcript levels in the aged animals, without change in body weight or hypothalamic hormone content [3].

Human studies

Sermorelin has a genuine human trial base in its own right, which distinguishes it from most peptides in this category. It was developed as a pharmaceutical product, carried an approved indication, and the trials that supported it are indexed and readable. The clinical literature is nonetheless concentrated in one population — children investigated or treated for growth hormone deficiency — and is now, in the main, thirty years old.

The largest study is the Geref International Study Group trial reported by Thorner and colleagues: a multicentre, open-label study in which 110 previously untreated prepubertal growth-hormone-deficient children received GHRH(1-29) for twelve months, with 86 evaluable for efficacy. Mean height velocity rose from 4.1 ± 0.9 cm/year at baseline to 8.0 ± 1.5 cm/year at six months and 7.2 ± 1.3 cm/year at twelve months; 74% were classed as good responders at six months; bone age progression tracked growth; and the authors reported no adverse biochemical or hormonal changes, no alteration in fasting glucose and no excessive IGF-I generation [6]. Lanes and Carrillo, with the Venezuelan Collaborative Study Group, reported long-term therapy with a single daily dose in prepubertal growth-hormone-deficient children [7]. Grunt and colleagues reported effects of long-term GHRH(1-29) in significantly short children [9], and Schwartz and colleagues reported growth during and after a trial of GHRH(1-29) in children with idiopathic short stature or growth hormone neurosecretory dysfunction [10]. Saenger, Pescovitz and Bercu reported the outcome of subsequent growth hormone therapy in children who had responded inadequately to GHRH [11].

A diagnostic literature runs alongside the therapeutic one. Bueno and colleagues studied priming with GHRH(1-29)NH₂ over six consecutive days in sixteen short-statured children who had not responded to a single GHRH challenge, and reported that the procedure separated the group into eight who responded to priming, with a rise in plasma growth hormone from 6.0 ± 2.1 to 18.0 ± 5.4 ng/mL, and eight who did not, in whom the change was not significant; they interpreted this as distinguishing hypothalamic from primary pituitary deficiency [8]. Prakash and Goa reviewed the compound’s use in both the diagnosis and the treatment of children with idiopathic growth hormone deficiency [1].

The adult literature is much thinner and consists of small, short physiological studies in older men. Corpas and colleagues conducted a randomised trial in which ten healthy non-obese older men (mean age 68.0 years) received GHRH(1-29) twice daily at each of two exposure levels for fourteen-day periods separated by a fourteen-day washout, with nine young men (mean age 26.2 years) as comparators; the authors reported dose-related increases in mean 24-hour growth hormone, pulse amplitude and IGF-I, no significant difference between age groups after the higher exposure, and no adverse effect on glucose metabolism or blood pressure over the study period [12]. Vittone and colleagues studied single nightly injections of GHRH(1-29) over six weeks in eleven healthy ambulatory non-obese men aged 64 to 76 with low baseline IGF-I, measuring growth hormone secretion, muscle strength, muscle histology, body composition and metabolic variables, and concluded that single nightly doses were less effective than multiple daily doses [13].

Two further human studies are frequently cited in connection with sermorelin and should be read with their limits stated. Khorram, Laughlin and Yen conducted a randomised controlled trial of long-term administration in age-advanced men and women — but the peptide studied was [Nle²⁷]GHRH(1-29)NH₂, a norleucine-substituted analogue, not sermorelin [14]. That single substitution at position 27 is precisely the modification made to remove the oxidation-labile methionine, so the two molecules are not interchangeable for the purpose of citing evidence. Sigalos and colleagues reported a retrospective record review in hypogonadal men on testosterone therapy in which fourteen compliant patients received a combination of GHRP-6, GHRP-2 and sermorelin, with mean IGF-1 rising from 159.5 to 239.0 ng/mL over approximately 134 days [15]; because three secretagogues were given together, no part of that result can be attributed to sermorelin alone.

Analytical, forensic and regulatory literature

Yuen, Biller, Molitch and Cook published a clinical review examining the consequences for growth hormone deficiency testing of recombinant GHRH no longer being available in the United States, and what alternatives that absence forced [16].

Venhuis and colleagues reported laboratory analysis of biopharmaceutical injectables seized during Operation Pangea 7 in 2014 across several European countries. Human growth hormone, sermorelin and melanotan II were among the substances identified, alongside products containing no active ingredient at all; the authors noted that shipment sizes indicated onward distribution rather than personal supply [21]. It is the clearest published evidence that material sold as sermorelin in unregulated European channels has, on analysis, sometimes not been sermorelin.

Evidence gaps and limitations

Human trials of sermorelin itself exist and are not in doubt. What is thin is almost everything beyond the indication the product was developed for.

The trial base is old and narrow. The pivotal work dates from the early to mid 1990s, was conducted in prepubertal children being investigated or treated for growth hormone deficiency, and used endpoints — height velocity, provoked growth hormone response, IGF-I — appropriate to that question and to no other. There is no modern trial conducted to current standards, and no trial in healthy adults of any size. The adult literature is three small studies: two physiological studies in older men lasting fourteen days and six weeks respectively [12][13], and one retrospective review of fourteen patients on a three-drug combination [15]. None of those establishes anything about sustained administration, and the combination study cannot be attributed to sermorelin at all.

There is no long-term safety dataset in adults. The safety observations in the paediatric trials cover twelve months of a supervised, licensed pharmaceutical product in a defined patient group under endocrinological monitoring, and they do not transfer to any other context.

The literature on the compound is literature on a pharmaceutical-grade product. Every clinical study cited here used material made to a marketing authorisation specification, with a known identity, a known purity, a known content and a known impurity profile. Research-grade powder does not inherit any of that by sharing a name, and Venhuis and colleagues found sermorelin among seized injectables in Europe in a study whose other finding was that some seized products contained no active ingredient [21]. Any inference from the published trials to a particular vial of research material rests entirely on that vial’s own analysis.

The glioma finding [4] is in silico with in vitro follow-up. It has generated no clinical study in the five years since publication, and a computational sensitivity score is not a clinical result.

Finally, the substitution point is worth stating twice because it is routinely elided in secondary sources: trials of [Nle²⁷]GHRH(1-29)NH₂ [14] are trials of a different molecule. They belong in a reading list on this compound; they are not evidence about it.

Regulatory and standards position

United Kingdom. No sermorelin product currently holds a UK marketing authorisation, and none is marketed. Sermorelin is not a controlled drug: the Class C entries at Schedule 4 Part II of the Misuse of Drugs Regulations 2001 cover somatotropin, somatrem and somatropin — growth hormone itself — and do not extend to GHRH or its analogues. That is a narrow point and it does not make the compound unregulated. Sermorelin holds an International Nonproprietary Name and was an authorised medicinal product; any presentation of it for human use would fall within the Human Medicines Regulations 2012, and no such product is authorised here. Material supplied as a laboratory chemical is supplied for research use only, and it is the presentation and the claim, not the molecule, that determine whether something is a medicinal product in UK law.

European Union. There is no centrally authorised sermorelin product. The substance carries ATC classifications H01AC04 (pituitary and hypothalamic hormones and analogues) and V04CD03 (tests for pituitary function), which record what it was authorised for historically rather than any current authorisation.

United States. Sermorelin acetate was approved and marketed as Geref. FDA records two new drug application approvals, dated 28 December 1990 and 26 September 1997, held latterly by EMD Serono, covering injection presentations at 0.05 mg base per ampoule and at 0.5 mg and 1.0 mg base per vial — the lower-strength presentation used diagnostically, the higher-strength presentations for treatment of growth hormone deficiency in children. During 2008 the manufacturer notified FDA that the products were being discontinued and requested withdrawal of the applications. A determination published in the Federal Register on 4 March 2013 recorded that Geref was not withdrawn from sale for reasons of safety or effectiveness; the discontinuation was a commercial decision by the manufacturer. That distinction matters and is frequently reported wrongly in both directions — the product was withdrawn from the market, and it was not withdrawn because it had been found unsafe or ineffective. No sermorelin product has been approved in the United States since. Yuen and colleagues examined the practical consequence of that absence for the diagnosis of adult growth hormone deficiency [16]. Sermorelin now reaches the US market principally through pharmacy compounding; compounded preparations are not FDA-approved products and are not reviewed for safety, effectiveness or manufacturing quality before they are dispensed.

Anti-doping. Sermorelin is prohibited in sport at all times, in and out of competition. It appears in Section S2 of the WADA Prohibited List (Peptide Hormones, Growth Factors, Related Substances and Mimetics), at S2.2.4, growth hormone releasing factors, where it is named explicitly among GHRH analogues alongside CJC-1293, CJC-1295 and tesamorelin. Being named rather than caught by a general clause removes any argument about scope. Validated detection methods for the compound in plasma and urine are published and in routine use in accredited laboratories [5][17][18][19].

Documented enforcement. Sermorelin was among the biopharmaceutical injectables identified in seizures made under Operation Pangea 7 in 2014 and analysed by Venhuis and colleagues, in a sample set that also included products containing no active ingredient [21].

Laboratory handling and safety

Sermorelin is supplied for laboratory research use only. It is not for human or veterinary use, not for use as a food or cosmetic ingredient, and not for administration to any person.

There is no comprehensive toxicological dataset for the research-grade substance, and the safety observations recorded in the clinical literature relate to a supervised pharmaceutical product under medical monitoring. Handle the material as a substance of unknown hazard: a COSHH assessment before first use, nitrile gloves, safety spectacles and a laboratory coat as the minimum, and no eating, drinking or storing of food in the work area.

The lyophilisate is fine, light and strongly static-prone, so weighing and transfer generate airborne particulate readily. Weigh and open vials in a fume cupboard or a suitable containment enclosure, avoid inhalation of the powder, and wipe down surfaces afterwards — static-dispersed peptide travels further than it appears to. Reconstitute using aseptic technique with an appropriate sterile diluent, label every aliquot with the compound, the lot, the concentration and the reconstitution date, and record the diluent used, because the concentration cannot be reconstructed later without it.

Dispose of surplus material, contaminated consumables and sharps through the appropriate laboratory waste stream in accordance with local rules and the institution’s waste policy. Consult the supplier’s safety data sheet for the specific lot before first handling.

References

1. Prakash A, Goa KL. Sermorelin: a review of its use in the diagnosis and treatment of children with idiopathic growth hormone deficiency. BioDrugs. 1999;12(2):139–57. Review. PMID 18031173
2. Lance VA, Murphy WA, Sueiras-Diaz J, Coy DH. Super-active analogs of growth hormone-releasing factor (1-29)-amide. Biochemical and Biophysical Research Communications. 1984;119(1):265–72. Rodent (rat) in vivo. PMID 6231028
3. Girard N, Boulanger L, Denis S, Gaudreau P. Differential in vivo regulation of the pituitary growth hormone-releasing hormone (GHRH) receptor by GHRH in young and aged rats. Endocrinology. 1999;140(6):2836–42. Rodent. PMID 10342875
4. Chang Y, Huang R, Zhai Y, Huang L, Feng Y, Wang D, Chai R, Zhang W, Hu H. A potentially effective drug for patients with recurrent glioma: sermorelin. Annals of Translational Medicine. 2021;9(5):406. In silico screen with in vitro glioma cell line assays. PMID 33842627
5. Memdouh S, Gavrilović I, Ng K, Cowan D, Abbate V. Advances in the detection of growth hormone releasing hormone synthetic analogs. Drug Testing and Analysis. 2021;13(11-12):1871–87. In vitro metabolism and LC-MS/MS method validation. PMID 34665524
6. Thorner M, Rochiccioli P, Colle M, Lanes R, Grunt J, Galazka A, Landy H, Eengrand P, Shah S. Once daily subcutaneous growth hormone-releasing hormone therapy accelerates growth in growth hormone-deficient children during the first year of therapy. Geref International Study Group. The Journal of Clinical Endocrinology and Metabolism. 1996;81(3):1189–96. Human trial, multicentre, 110 enrolled. PMID 8772599
7. Lanes R, Carrillo E; Venezuelan Collaborative Study Group. Long-term therapy with a single daily subcutaneous dose of growth hormone releasing hormone (1-29) in prepubertal growth hormone deficient children. The Journal of Pediatric Endocrinology. 1994;7(4):303–8. Human trial, multicentre. PMID 7735367
8. Bueno G, Bueno M, Garagorri JM, Juste G, Rejas J, Alvarez I. Priming with GHRH (1-29) NH2: an aid in differential diagnosis between hypothalamic and pituitary deficiencies. The Journal of Pediatric Endocrinology. 1994;7(4):309–16. Human trial, n=16. PMID 7735368
9. Grunt JA, Schwartz ID, Buchanan C, Howard CP. Effects of long-term growth hormone releasing hormone 1-29 in significantly short children. Acta Paediatrica. 1995;84(6):631–3. Human study. PMID 7670244
10. Schwartz ID, Grunt JA, Berg S, et al. Growth during and after a trial of growth hormone releasing hormone 1-29 in children with idiopathic short stature or growth hormone neurosecretory dysfunction. Journal of Pediatric Endocrinology & Metabolism. 2000;13(6):645–50. Human study. PMID 10905389
11. Saenger P, Pescovitz OH, Bercu BB. Outcome of growth hormone therapy in children with growth hormone deficiency showing an inadequate response to growth hormone-releasing hormone. Endocrine. 2001;15(1):51–6. Human trial, multicentre. PMID 11572326
12. Corpas E, Harman SM, Piñeyro MA, Roberson R, Blackman MR. Growth hormone (GH)-releasing hormone-(1-29) twice daily reverses the decreased GH and insulin-like growth factor-I levels in old men. The Journal of Clinical Endocrinology and Metabolism. 1992;75(2):530–5. Human randomised trial, n=19. PMID 1379256
13. Vittone J, Blackman MR, Busby-Whitehead J, Tsiao C, Stewart KJ, Tobin J, Stevens T, Bellantoni MF, Rogers MA, Baumann G, Roth J, Harman SM, Spencer RG. Effects of single nightly injections of growth hormone-releasing hormone (GHRH 1-29) in healthy elderly men. Metabolism: Clinical and Experimental. 1997;46(1):89–96. Human trial, n=11. PMID 9005976
14. 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. The Journal of Clinical Endocrinology and Metabolism. 1997;82(5):1472–9. Human randomised controlled trial — of the norleucine-27 analogue, not sermorelin. PMID 9141536
15. Sigalos JT, Pastuszak AW, Allison A, Ohlander SJ, Herati A, Lindgren MC, Lipshultz LI. Growth Hormone Secretagogue Treatment in Hypogonadal Men Raises Serum Insulin-Like Growth Factor-1 Levels. American Journal of Men’s Health. 2017;11(6):1752–7. Human retrospective review, n=14, three-secretagogue combination. PMID 28830317
16. Yuen KC, Biller BM, Molitch ME, Cook DM. Clinical review: Is lack of recombinant growth hormone (GH)-releasing hormone in the United States a setback or time to consider glucagon testing for adult GH deficiency? The Journal of Clinical Endocrinology and Metabolism. 2009;94(8):2702–7. Review. PMID 19509104
17. Knoop A, Thomas A, Fichant E, et al. Qualitative identification of growth hormone-releasing hormones in human plasma by means of immunoaffinity purification and LC-HRMS/MS. Analytical and Bioanalytical Chemistry. 2016;408(12):3145–53. Analytical method, human plasma. PMID 26879649
18. Coppieters G, Deventer K, Polet M, et al. An antibody-free, ultrafiltration-based assay for the detection of growth hormone-releasing hormones. Journal of Pharmaceutical and Biomedical Analysis. 2022;214:114726. Analytical method. PMID 35298973
19. Uçaktürk E, Nemutlu E. Analysis of growth hormone releasing hormone and its analogs in urine using nano liquid chromatography. Journal of Pharmaceutical and Biomedical Analysis. 2026;268:117207. Analytical method, human urine. PMID 41138283
20. González-López NM, Guerra-Acero-Turizo LM, Blanco-Medina I, et al. In-house standards derived from doping peptides: Enzymatic and serum stability and degradation profile of GHRP and GHRH-related peptides. Biomedical Chromatography. 2023;37(12):e5741. In vitro stability and degradation. PMID 37688464
21. Venhuis BJ, Keizers PHJ, Klausmann R, Hegger I. Operation resistance: A snapshot of falsified antibiotics and biopharmaceutical injectables in Europe. Drug Testing and Analysis. 2016;8(3-4):398–401. Laboratory analysis of seized products. PMID 26456392

Research use only

NovoVita does not supply sermorelin. This entry exists because the library documents the field rather than the catalogue, and a reference work that covered only what is on the shelf would be a price list.

Sermorelin is described here as a laboratory chemical and as a record of published literature. Nothing on this page is a statement that the compound does anything, nothing on this page is a recommendation to use it, and no amount, schedule or route of administration is given or implied. Reporting that a study observed a result is a statement about that study and about nothing else.

Sermorelin is not authorised as a medicine in the United Kingdom, and no product supplied for research use is authorised for human or veterinary use, for administration to any person or animal, for use in food, or for any household purpose. Anyone conducting work with it is responsible for holding the appropriate institutional and ethical approvals and for complying with the Human Medicines Regulations 2012 and all other applicable law.