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Research library, GHRH(1-29) fragment, amidated

Sermorelin: chemistry, literature and regulatory status

Written by the Peptency editorial teamLast reviewed 5 studies checked in PubMed on 5 October 2026

Research-use information. This page summarises published literature and regulator records. It is not guidance for use, not medical advice, and not a statement that any material is suitable for use in people or animals.

What is Sermorelin?

Sermorelin is GRF(1-29)-NH2, the first 29 residues of human growth hormone-releasing hormone, which was isolated as a 44-residue peptide from a human pancreatic tumour in 1982. Published work covers the isolation and sequence, receptor cloning and reviews. It is supplied here as a research material for laboratory use only.

What are the chemical facts for Sermorelin?

Name
Sermorelin
Also written
GRF 1-29
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 (source: PMID 6812220 (residues 1 to 29))
Length
29 residues
Molecular formula
C149H246N44O42S (matches the formula computed from the sequence)
Average molecular weight
3357.9 g/mol
CAS number
86168-78-7 (confirmed in PubChem)
PubChem
CID 16132413

Chemistry checked against PubChem on 2026-10-05. Where the formula can be computed from the listed sequence, it was, and the two routes agree.

How does the literature describe the mechanism of Sermorelin?

  • A 44-residue growth hormone-releasing peptide was isolated from a human pancreatic tumour and its amino acid sequence determined, with full activity of the synthetic replicate.[4],[5]
  • The pituitary receptor for growth hormone-releasing hormone was cloned and expressed, with ligand binding and cyclic AMP production measured in transfected cells.[3]
  • Reviews cover the receptor's signal transduction and synthetic growth hormone-releasing peptides.[1],[2]

Receptor and pathway background: Growth hormone-releasing hormone receptor.

What has published research on Sermorelin looked at?

5 studies are cited for Sermorelin. Each is labelled by design below, and each entry says what the paper measured.

  • 2 review
  • 2 chemistry
  • 1 receptor biology

PubMed returns 365 records for the search terms published on the method page (9 of them with a review publication type, 63 with a clinical-trial publication type), checked 5 October 2026. ClinicalTrials.gov lists 27 registered studies whose intervention matches the name (25 interventional), checked 5 October 2026.

Studies are listed by what they measured. Papers whose titles state an amount or schedule, or describe a clinical outcome of an approved medicine, are not listed. This is a wording rule, not a quality filter; see the method page.

What is the regulatory status of Sermorelin?

FDA

2 applications listed (Discontinued)

Drugs@FDA lists 2 applications naming this active ingredient: NDA019863, NDA020443. Marketing status as listed: Discontinued. Checked 2026-10-05.

Drugs@FDA via openFDA

EMA

No centrally authorised medicine listed

No centrally authorised procedure in the EMA medicines database (checked 5 October 2026) names sermorelin as an active substance. National authorisations are not in this dataset.

EMA medicines data

MHRA

No product document found

No SmPC, PIL or PAR document in MHRA Products matches the exact name "sermorelin". Checked 2026-10-05; the control lookup (semaglutide) returned 271 documents.

MHRA Products

WADA

Named, S2.2.4

The WADA 2026 Prohibited List, in force 1 January 2026 names sermorelin under S2.2.4 (growth hormone releasing factors,). A WADA entry is a sporting rule, not a statement about legality outside sport.

WADA Prohibited List 2026

A regulator record is information about a database entry. It is not advice and not a statement that any use is lawful or unlawful in any country. How regulators approach research peptides.

Data dates: regulatory records 2026-10-05; WADA list 2026-10-05.

Which studies are cited for Sermorelin?

  1. [1] Mayo KE, Miller TL, DeAlmeida V, Zheng J, Godfrey PA. The growth-hormone-releasing hormone receptor: signal transduction, gene expression, and physiological function in growth regulation. Ann N Y Acad Sci. 1996;805:184-203.

    Review of GHRH receptor signal transduction, gene expression and physiological function.

  2. [2] Argente J, García-Segura LM, Pozo J, Chowen JA. Growth hormone-releasing peptides: clinical and basic aspects. Horm Res. 1996;46:155-9.

    Review of synthetic growth hormone-releasing peptides: clinical and basic aspects in animals and humans.

  3. [3] Mayo KE. Molecular cloning and expression of a pituitary-specific receptor for growth hormone-releasing hormone. Mol Endocrinol. 1992;6:1734-44.

    Cloning and expression of the pituitary GHRH receptor, with ligand binding and cAMP production in transfected cells.

  4. [4] Guillemin R, Brazeau P, Böhlen P, Esch F, Ling N, Wehrenberg WB. Growth hormone-releasing factor from a human pancreatic tumor that caused acromegaly. Science. 1982;218:585-7.

    Isolation and amino-acid sequence of a 44-residue growth hormone-releasing peptide from a human pancreatic tumour, with a synthetic replicate.

  5. [5] Rivier J, Spiess J, Thorner M, Vale W. Characterization of a growth hormone-releasing factor from a human pancreatic islet tumour. Nature. 1982;300:276-8.

    Isolation and characterisation of growth hormone-releasing factor from a human pancreatic islet tumour.

Data dates: citations read from PubMed 2026-10-05.

Where else in the research library is Sermorelin covered?

Who wrote this page and how is it checked?

Peptency editorial team, last reviewed 5 October 2026. Citations are read back from PubMed, chemistry is checked against PubChem, and regulator records are read from each regulator's own database on the dates shown. The method page lists every source, search term and rule. Corrections are welcome through the contact details on the About page.