Sermorelin
Also known as GRF(1-29), GHRH(1-29), Sermorelin acetate
Sermorelin is GRF(1-29), the native active fragment of human GHRH and the parent sequence behind the modified analogs. A research profile with the full 29-residue sequence.
If the CJC-1295 analogs are the engineered members of the GHRH family, sermorelin is the original. It is simply GRF(1-29) — the first 29 amino acids of human growth-hormone-releasing hormone, the stretch that carries the hormone's activity — with no stabilizing substitutions and no albumin-binding complex.
That makes it the natural anchor for this whole cluster: the reference sequence the modified analogs are measured against. This page keeps to the verifiable — its identity, its structure, and its research contexts — and stays clear of outcomes and dosing.
Sermorelin is GRF(1-29): the first 29 amino acids of human growth-hormone-releasing hormone, with an amidated C-terminus. Unlike the CJC-1295 analogs, it is the unsubstituted native fragment — the reference sequence the modified analogs are built from.
The native fragment, not an analog
Full-length human GHRH is 44 amino acids, but its receptor-activating core lives in the first 29. Sermorelin is exactly that fragment, produced synthetically. Where CJC-1295 (no DAC) introduces four substitutions into this same GRF(1-29) backbone to slow its breakdown, sermorelin leaves it unmodified — which is why it is often used as the baseline reference when the analogs are discussed.
Because it is the native sequence with standard amino acids, sermorelin is one of the few peptides in this group whose full residue list can be written plainly, as shown above. That readability is part of why it is a useful teaching molecule for the class.
A GHRH-receptor molecule
Sermorelin acts at the GHRH receptor on the pituitary — the same target as tesamorelin and the CJC-1295 analogs, and distinct from the ghrelin (GHS) receptor engaged by ipamorelin and the GHRPs. Historically it has appeared in the research literature as a probe of pituitary growth-hormone reserve, precisely because it stimulates the releasing-hormone side of the axis directly.
As with the other GHRH analogs, it is frequently studied alongside a ghrelin-receptor secretagogue, since the two receptor systems represent complementary inputs.
Reading a sermorelin certificate
The well-defined 29-residue sequence means a certificate of analysis should show a clean single HPLC peak and a mass matching GRF(1-29) with an amidated terminus. Because sermorelin is unmodified, its mass will be lower than the substituted CJC-1295 forms and much lower than the DAC conjugate — a quick way to keep the family members straight. Verify each lot by its batch number.
These are research areas the compound is associated with in the literature — not medical claims or intended uses.
Handling & storage
Supplied lyophilized. Stored sealed and cold; reconstituted with bacteriostatic water only as a protocol requires, then refrigerated. Handle per accepted laboratory practice.
Verify a certificate by lot →Common questions
It is GRF(1-29): the first 29 amino acids of human growth-hormone-releasing hormone, with an amidated C-terminus. It is the native active fragment, not a substituted analog.
CJC-1295 is built on the same GRF(1-29) backbone but adds four substitutions (and, in the DAC form, an albumin-binding linker). Sermorelin is the unmodified reference sequence.
A GHRH analog — in fact the native GHRH fragment. It acts on the GHRH receptor, unlike ghrelin mimetics such as ipamorelin and the GHRPs.
This monograph is a research-use reference. It describes composition and the contexts in which the compound has been studied — it is not medical advice, a description of effects, or a recommendation for use. Sold strictly for laboratory and research use; not for human or animal consumption.