Also known as GRF 1-29 · Geref
Truncated GHRH(1-29) — historically the first GHRH analog approved by the FDA.
Sermorelin is the first 29 amino acids of endogenous GHRH and was approved by the FDA in 1990 (subsequently discontinued commercially) for diagnostic and pediatric GH deficiency use.
Sermorelin is the first 29 amino acids of endogenous GHRH — the shortest fragment that retains full GH-releasing activity. As a GHRH-receptor agonist it prompts the pituitary to release the body’s own growth hormone.
It was FDA-approved in 1990 (Geref) for diagnostic evaluation of pituitary GH reserve and for pediatric GH deficiency, but was later discontinued commercially. It remains a widely referenced GHRH analog in research.
GHRH receptor agonism.
Behind every vial of Sermorelin is the same exacting pipeline every research peptide runs — but the chemistry plays out differently for this molecule. Here is how Sermorelin, specifically, is brought into being.
On paper, Sermorelin is C149H246N44O42S — about 3,358 daltons of precisely arranged atoms. Before a single bond is made, the target sequence, salt form, and purity threshold are written down as the contract the finished material must meet.
Assembling Sermorelin means roughly 29 coupling cycles on the synthesizer — one protected residue added at a time, which is also 29 chances for an incomplete coupling to seed a deletion impurity.
The crude mixture — Sermorelin plus its deletions and side products — is then separated on preparative HPLC, and where the cut is taken decides the difference between a genuinely pure peptide and a barely-passable one. It also contains oxidation-prone methionine or tryptophan residues, another family of impurities the chromatography has to resolve away.
A real batch of Sermorelin proves itself: identity confirmed by mass spectrometry against its ~3,358 Da, purity read directly off an analytical HPLC trace, water and counterion content measured. That batch-specific certificate of analysis is the only honest way to know what is actually in a vial of Sermorelin — and a short, cold, accountable chain of custody is how that purity survives the trip to your bench.
Producing Sermorelin to a genuine purity spec means solid-phase synthesis, preparative HPLC purification, and batch quality control — none of it cheap, and none of it something you can verify by eye.
Don't judge a vial by its cake. A fluffy, good-looking lyophilized powder reflects bulking agents and freeze-drying parameters — not purity. Insist on a batch-specific certificate of analysis.
Recent clinical trials and publications mentioning Sermorelin, pulled automatically from ClinicalTrials.gov and PubMed and refreshed daily. Listings are unfiltered search results, not curated endorsements.
Sermorelin is GHRH(1-29), the shortest active fragment of growth-hormone-releasing hormone, historically approved to assess and treat GH deficiency.
It was approved in 1990 (Geref) but later discontinued commercially. It is referenced today largely as a research compound.
CJC-1295 is a stabilized, longer-acting modification of the same GHRH(1-29) backbone; sermorelin is the unmodified fragment with a short half-life.
No — this page is a research and educational reference.
Recombinant 191-amino-acid human growth hormone — a folded protein biologic identical in sequence to pituitary GH, not a synthetic research peptide.
ViewThe downstream effector of growth hormone — a 70-amino-acid recombinant protein, structurally a cousin of proinsulin, that carries out most of GH’s growth signal.
ViewA long-acting modified IGF-1 analog with reduced IGFBP binding and prolonged systemic activity.
ViewDosing protocols, mechanism, comparisons, and the latest trials — citation-backed answers grounded in PubMed, PubChem, and ClinicalTrials.gov.