For laboratory research use only. This page summarises the published scientific literature on sermorelin in plain English. It does not give medical advice, and it contains no guidance on doses or administration.
What is sermorelin?
Sermorelin is a synthetic peptide made of the first 29 amino acids of human growth hormone-releasing hormone (GHRH), with an amidated C-terminus. It is often written as GHRH(1-29)-NH2. Early work in the 1980s showed that this shortened fragment keeps the receptor activity of the full 44-amino-acid hormone, which made it a convenient tool for studying how the hypothalamus controls growth hormone (GH) release from the pituitary gland [1, 3].
Key molecular facts
| Property | Value |
|---|---|
| Sequence | Tyr-Ala-Asp-Ala-Ile-Phe-Thr-Asn-Ser-Tyr-Arg-Lys-Val-Leu-Gly-Gln-Leu-Ser-Ala-Arg-Lys-Leu-Leu-Gln-Asp-Ile-Met-Ser-Arg-NH2 |
| Length | 29 amino acids |
| Molecular formula | C149H246N44O42S |
| Average molecular weight | approx. 3,358 Da |
| CAS number | 86168-78-7 |
| Usual supplied form | Lyophilised (freeze-dried) acetate salt |
How it works: the GHRH receptor
In the body, GHRH is released by the hypothalamus and binds to the GHRH receptor on somatotroph cells in the anterior pituitary. This receptor is a G-protein-coupled receptor. Binding raises intracellular cyclic AMP, activates protein kinase A and leads to GH synthesis and release. Somatostatin acts as the opposing brake. Because sermorelin acts on the same receptor, researchers use it to study this signalling pathway and its feedback controls, including the role of IGF-1 and somatostatin [1, 4].
Stability and breakdown
Sermorelin breaks down quickly in plasma. The main reason is the enzyme dipeptidyl peptidase-4 (DPP-4), which cuts the peptide between alanine at position 2 and aspartic acid at position 3, producing an inactive GHRH(3-29) fragment. Trypsin-like enzymes also cleave it at basic residues [2]. Later GHRH analogues were designed with changes at position 2 or a blocked N-terminus to resist this enzyme.
For laboratory handling, the methionine at position 27 is the other weak point: it can oxidise to methionine sulfoxide. Good practice is to store the lyophilised powder cold, dry and protected from light, and to check oxidation products in analytical results.
Main areas of published research
- Neuroendocrine physiology: how GHRH, somatostatin and ghrelin pathways interact to shape GH pulses [1, 4].
- Receptor pharmacology: sermorelin is used as a reference GHRH agonist when comparing newer, longer-lasting analogues.
- Ageing biology: reviews describe the gradual decline of GH secretion with age (sometimes called the somatopause) and discuss GHRH-based tools for studying it [4, 5]. These are review discussions, not evidence about any supplied product.
- Peptide chemistry: enzymatic degradation, oxidation and formulation stability of GHRH fragments [2].
Limits of the evidence
Much of the literature is decades old, many studies are small, and results from one study design do not transfer automatically to another. A published paper about the sermorelin molecule is not proof that any particular batch has a given biological effect. Purity data show what is in a vial; they do not show sterility, safety or suitability for any use outside the laboratory.
Regulatory status in the UK
Sermorelin is not licensed as a medicine in the UK. A sermorelin product was previously marketed as a prescription medicine in some countries and was withdrawn from the US market by its manufacturer in 2008 [3]. Research-use labelling does not settle how a product is classified, so laboratories should check their own regulatory obligations.
Quality checks for research material
- Batch-specific certificate of analysis (COA)
- HPLC purity, with the chromatogram available
- Mass spectrometry confirming identity (expected mass about 3,358 Da)
- Evidence of low oxidised (Met27 sulfoxide) and truncated (3-29) species
- Peptide content and counter-ion information, so concentrations can be calculated accurately
Researchers can find sermorelin acetate with batch documentation on our sermorelin product page.
Related research pages
- Growth-hormone peptides research hub
- Sermorelin vs tesamorelin: a structural comparison
- Research-grade peptides guide
- How to read a peptide certificate of analysis
References
- Thorner MO, et al. Human pancreatic growth-hormone-releasing factor selectively stimulates growth-hormone secretion in man. Lancet 1983;1(8314-5):24–28. PubMed 6129370
- Frohman LA, et al. Dipeptidylpeptidase IV and trypsin-like enzymatic degradation of human growth hormone-releasing hormone in plasma. J Clin Invest 1989;83:1533–1540. PubMed 2565342
- Prakash A, Goa KL. Sermorelin: a review of its use in the diagnosis and treatment of children with idiopathic growth hormone deficiency. BioDrugs 1999;12:139–157. PubMed 18031173
- Corpas E, Harman SM, Blackman MR. Human growth hormone and human aging. Endocr Rev 1993;14:20–39. PubMed 8491152
- Walker RF. Sermorelin: a better approach to management of adult-onset growth hormone insufficiency? Clin Interv Aging 2006;1:307–308. PubMed 18046908
Reference titles are reproduced as published. Their inclusion documents the literature and does not imply that any product is suitable for, or approved for, use in people.
For laboratory research use only. Sermorelin sold by Peptides Lab UK is supplied strictly for in vitro laboratory research. It is not for human or veterinary use, and nothing on this page is medical advice or guidance on administration. UK purchasers are responsible for complying with all applicable legislation.
