All information below describes the compound's chemical identity, laboratory handling, and the published research literature. It describes molecular targets and results in laboratory and animal models only — not effects in humans — and is not evidence of any human benefit.
What Is Sermorelin?
Sermorelin is a synthetic 29-amino-acid peptide corresponding to the N-terminal 1–29 fragment of human growth hormone-releasing hormone (GHRH), carrying a C-terminal amide (sequence YADAIFTNSYRKVLGQLSARKLLQDIMSR-NH2). It is the shortest fragment of the 44-residue native GHRH that retains full receptor-binding activity in the literature and is classified as a GHRH analogue and growth-hormone secretagogue. It does not occur freely in nature as an isolated fragment; it is a synthetic peptide developed after the isolation and sequencing of GHRH from pancreatic tumor tissue by Guillemin, Rivier and colleagues in the early 1980s.
It is supplied as a reference compound for in vitro and animal research use only. The sections below summarize its chemical identity, laboratory handling, the molecular targets and model systems examined in the published literature, and the primary references — without describing outcomes, efficacy, or effects in humans.
Research Targets & Pathways
Published literature has examined sermorelin, and the parent GHRH(1–29) sequence, in relation to several molecular systems. These are pathway associations reported in laboratory, animal, and pharmacology models; refer to the cited studies for methods and findings.
- GHRH receptor (GHRHR) — a class B G-protein-coupled receptor expressed on anterior-pituitary somatotrophs; the primary binding target characterized in the literature.
- Gsα / adenylate cyclase / cAMP — the canonical second-messenger cascade examined downstream of GHRHR in receptor-signaling assays.
- Protein kinase A (PKA) axis — studied as a downstream node of cAMP accumulation in pituitary cell models.
- Somatotroph GH1 transcription — examined in anterior-pituitary cell systems in relation to growth-hormone gene expression.
- Hypothalamic–pituitary–somatotropic axis — the neuroendocrine feedback system within which GHRH(1–29) pharmacology has been characterized.
Model Systems Studied
Sermorelin and the GHRH(1–29) sequence have been used as test compounds across a range of published model systems, spanning in vitro assays, rodent studies, and early-phase human pharmacology. Refer to the cited literature for study designs, endpoints, and findings.
- Receptor & second-messenger assays — GHRHR radioligand-binding and cAMP-accumulation assays in vitro.
- Pituitary cell models — cultured rat anterior-pituitary somatotroph systems.
- Rodent models — including aged-rodent neuroendocrine model systems.
- Human pharmacology — early-phase and diagnostic pharmacology literature characterizing GHRH(1–29)NH2 administration.
- Structural / analytical — HPLC, mass-spectrometric, and structure–activity characterization of the GHRH fragment series.
Note: the GHRH(1–29) pharmacology literature includes both preclinical and clinical work from multiple independent groups; study designs and populations vary, and findings in one model system do not transfer to others.
Stability & Handling
Sermorelin is supplied as a lyophilized powder. As a peptide containing a methionine residue, it is subject to oxidation, and its solutions are sensitive to elevated temperature and to repeated freeze–thaw; the literature and standard peptide-handling practice therefore call for cold, desiccated, light-protected storage. The N-terminal residues are important to receptor recognition, and enzymatic clearance of GHRH(1–29) at physiological pH is described in the pharmacology literature — a property relevant to formulation and handling in research settings.
Molecular & Technical Profile
C149H246N44O42S | MW ~3357.9 g/mol | CAS 86168-78-7 | Sequence: YADAIFTNSYRKVLGQLSARKLLQDIMSR-NH2
Storage, Reconstitution & Working Concentrations
Storage, reconstitution, and working-concentration values are general laboratory guidance for in vitro and animal research; always confirm against the lot-specific Certificate of Analysis. The precise molecular weight is reported as approximately 3357.9 g/mol for the free-base peptide; supplied material is commonly the acetate salt.
Current Research Status
Sermorelin has an extensive pharmacology literature spanning in vitro, rodent, and early-phase human studies characterizing the GHRH(1–29) sequence. A sermorelin acetate prescription product (formerly marketed in the United States as Geref) has held approval from the U.S. Food and Drug Administration (FDA), historically in a diagnostic and pediatric growth-hormone-deficiency context; that product was later discontinued from the U.S. market. The material supplied by Explicit Research is research-grade sermorelin for laboratory use only — it is not the approved drug product and is not intended for human or animal use. Ongoing research continues to characterize the compound's mechanistic profile and analytical properties.
Research FAQ
Is sermorelin approved for human use?
A sermorelin acetate prescription product (formerly marketed as Geref) has held FDA approval in a diagnostic and pediatric growth-hormone-deficiency context, and was later discontinued from the U.S. market. The material supplied here is research-grade sermorelin for laboratory research use only — it is not the approved drug product and is not for human consumption.
What is sermorelin's molecular formula and sequence?
A synthetic 29-amino-acid GHRH analogue, sequence YADAIFTNSYRKVLGQLSARKLLQDIMSR-NH2 — molecular formula C149H246N44O42S, MW approximately 3357.9 g/mol, CAS 86168-78-7.
How is sermorelin stored and reconstituted?
Store lyophilized at −20°C, desiccated and protected from light. Reconstitute in sterile or bacteriostatic water; store the reconstituted solution at 2–8°C for up to ~28 days and avoid repeated freeze–thaw. Contains a methionine residue, so minimize air exposure to limit oxidation.
What molecular targets has sermorelin been studied for?
As a GHRH(1–29) analogue, sermorelin has been characterized in relation to the GHRH receptor (GHRHR) on anterior-pituitary somatotrophs and the downstream Gs / adenylate cyclase / cAMP–PKA cascade, examined in receptor-binding, cAMP, pituitary-cell, rodent, and early-phase human pharmacology model systems.
Selected References
- Guillemin R, et al. (1982). Growth hormone-releasing factor from a human pancreatic tumor that caused acromegaly. Science / Proc Natl Acad Sci USA — isolation and characterization of the hypothalamic GHRH peptide.
- Rivier J, Spiess J, Thorner M, Vale W (1982). Characterization of a growth hormone-releasing factor from a human pancreatic islet tumour. Nature, 300:276–278.
- Vance ML, et al. (1985). Growth hormone-releasing hormone (1–29)NH2 and pulsatile growth hormone secretion in normal adults. Journal of Clinical Endocrinology & Metabolism.
- Cella SG, et al. (1986). Dose-response characterization of GHRH(1–29)NH2 in healthy volunteers. Journal of Clinical Endocrinology & Metabolism.
- Kerkhofs M, et al. (1993). Growth hormone-releasing hormone and sleep EEG, measured by polysomnography in normal men. Sleep, 16(4):357–364.
- Corpas E, Harman SM, Blackman MR (1993). Human growth hormone and human aging. Endocrine Reviews, 14(1):20–39.