Endocrine

Sermorelin

Sermorelin is a synthetic peptide made of the first 29 amino acids of human growth hormone-releasing hormone (GHRH), with a C-terminal amide: GHRH(1-29)NH2.[2][8] Native human GHRH has 44 residues.[1]...

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Certificate of Analysis

Certificate of Analysis included with every order.

Technical Specifications

Purity≥98%
FormLyophilized Powder
Storage-20°C
Molecular Weight3357.89 Da (C149H246N44O42S)
SequenceYADAIFTNSYRKVLGQLSARKLLQDIMSR-NH₂ (human GHRH 1-29)
CAS Number86168-78-7

About Sermorelin

Sermorelin is a synthetic peptide made of the first 29 amino acids of human growth hormone-releasing hormone (GHRH), with a C-terminal amide: GHRH(1-29)NH2.[2][8] Native human GHRH has 44 residues.[1][10] Sermorelin stimulates growth hormone secretion from the anterior pituitary.[3] Pepitiva supplies sermorelin as a lyophilized powder (5 mg vials, ≥98% purity, CAS 86168-78-7) for in vitro and preclinical research.[9]

Regulatory status

Sermorelin acetate was approved by the FDA under two applications, in 1990 and in 1997; both are now listed as discontinued, with an FDA determination that the product was not withdrawn for safety or effectiveness reasons.[6][7] It was used as a diagnostic test for growth hormone deficiency and to treat some children with idiopathic growth hormone deficiency.[3] The product sold here is a research-grade peptide, not a pharmaceutical product, and is intended only for laboratory use.

Why researchers study sermorelin

The 1-29 fragment is the shortest form of GHRH that keeps substantial activity, which makes sermorelin the reference compound for GHRH-receptor studies and the parent of later analogues.[2]

For research use only. Not for human consumption.

Quality & Storage

≥98% purity. Lyophilized Powder. Storage: -20°C. For research purposes only.

Mechanism of Action

GHRH receptor agonism

Sermorelin acts on the GHRH receptor of the anterior pituitary and specifically stimulates growth hormone secretion.[3][8] Because it acts upstream of the pituitary, the GH it releases is the animal's own, subject to normal feedback.

Structure-activity: why 29 residues

In rat anterior pituitary cells, deleting C-terminal residues of human GRF gradually lowered activity down to GRF(1-34); the GRF(1-31)NH2, (1-30)NH2 and (1-29)NH2 fragments then held steady at about 50% of the potency of the full peptide, and activity disappeared completely only at GRF(1-19)NH2.[2]

Sequence and properties

YADAIFTNSYRKVLGQLSARKLLQDIMSR-NH2, the first 29 residues of human GHRH (full sequence YADAIFTNSYRKVLGQLSARKLLQDIMSRQQGESNQERGARARL-NH2). Formula C149H246N44O42S, molecular weight 3357.89 Da.[1][8][10] A longer GHRH analogue is tesamorelin (all 44 residues plus an N-terminal hexenoyl group).

Research Applications

Clinical research highlights

  • Diagnosis and treatment of GH deficiency (review, 1999): intravenous sermorelin was described as a rapid and relatively specific test for GH deficiency, and once-daily subcutaneous treatment increased height velocity in some prepubertal children with idiopathic GH deficiency; increases were smaller than with somatropin, and transient facial flushing and injection-site pain were the most common adverse events.[3]
  • Older men (1992): 14 days of twice-daily GHRH(1-29) at the higher of two doses raised 24-hour GH and IGF-I in healthy older men to levels that no longer differed from those of young men, without changing fasting glucose or blood pressure.[4]
  • Single nightly injections in older men (1997): 6 weeks increased nocturnal GH release but not IGF-I; two of six strength measures improved, with no change in body composition, and the authors concluded that single nightly doses were less effective than multiple daily doses.[5]

Laboratory research applications

  • GHRH receptor pharmacology: structure-activity work on truncated and substituted GHRH analogues.[2]
  • Pituitary function models: GH release from somatotroph cultures and provocative testing in animal models.[3]
  • Comparing secretagogue classes: GHRH-receptor agonism versus ghrelin-receptor agonism with ipamorelin, or both pathways together in CJC-1295 + Ipamorelin. For a full-length GHRH analogue, see tesamorelin.

Sermorelin is among the GH-axis peptides now sold outside regulated supply chains, where product composition and dosing are uncertain.[11] The findings above are scientific background only; this product is sold for laboratory research and is not intended for human or veterinary use.

Storage & Handling Guidelines

Proper storage and handling are essential to maintain peptide integrity and ensure reliable research results. All Pepitiva Biolabs peptides are supplied as lyophilized (freeze-dried) powder, which provides excellent long-term stability when stored correctly. Store lyophilized peptides at -20°C for long-term storage or 2-8°C for short-term use. Once reconstituted, peptide solutions should be stored at 2-8°C and used within the timeframe specified in the product documentation. Always use sterile bacteriostatic water for reconstitution and handle peptides in a clean laboratory environment to prevent contamination. Avoid repeated freeze-thaw cycles, as thermal stress can cause peptide degradation and loss of biological activity.

Quality Control & Certification

This product is manufactured under strict quality control protocols and has been verified through comprehensive analytical testing. Each batch undergoes reverse-phase HPLC analysis for purity determination and electrospray ionization mass spectrometry (ESI-MS) for molecular identity confirmation. A detailed Certificate of Analysis (COA) is available for download, documenting purity percentage, molecular weight verification, appearance, and recommended storage conditions. Pepitiva Biolabs maintains batch-level traceability from synthesis through delivery, ensuring complete transparency and quality assurance for your research.

Frequently Asked Questions

What is sermorelin?

A synthetic peptide made of the first 29 amino acids of human growth hormone-releasing hormone, with a C-terminal amide (GHRH 1-29 NH2). It stimulates growth hormone release from the pituitary.

Is sermorelin FDA approved?

Sermorelin acetate was FDA-approved in 1990 and 1997, but both applications are now discontinued; the FDA determined the product was not withdrawn for safety or effectiveness reasons. The research-grade peptide sold here is not a pharmaceutical product.

What is the molecular weight and CAS number of sermorelin?

Molecular weight 3357.89 Da, formula C149H246N44O42S (KEGG DRUG D08509); CAS 86168-78-7.

Is GHRH(1-29) as active as full-length GHRH?

Not quite. In rat pituitary cells GRF(1-29)NH2 had about 50% of the potency of the full 44-residue peptide, and it is the shortest fragment that keeps that level of activity.

How is sermorelin different from tesamorelin?

Both act on the GHRH receptor. Sermorelin is the 29-residue fragment; tesamorelin contains all 44 residues of GHRH plus an N-terminal hexenoyl group.

How is sermorelin different from ipamorelin?

Sermorelin acts on the GHRH receptor, while ipamorelin acts on the ghrelin (growth hormone secretagogue) receptor. Both lead to release of the pituitary's own growth hormone.

How should sermorelin be stored?

Keep the lyophilized powder at −20 °C, protected from light and moisture.

Is this product approved for human use?

No. This product is intended exclusively for in vitro scientific research and laboratory use. It is not approved for human or veterinary use, not intended for diagnostic or therapeutic purposes, and should not be administered to humans or animals under any circumstances.

How do I reconstitute this peptide?

Add sterile bacteriostatic water slowly to the vial, directing the stream against the glass wall rather than directly onto the lyophilized powder. Gently swirl the vial until the powder is fully dissolved — do not shake vigorously. The recommended reconstitution volume depends on your desired concentration. Refer to the product documentation for specific guidance.

Can I get a Certificate of Analysis (COA)?

Yes. A Certificate of Analysis is included with every order and is also available for download from the product page. The COA documents HPLC purity, mass spectrometry identity confirmation, batch number, production date, and storage recommendations.

Scientific References

  1. Ling N, Esch F, Böhlen P, et al. Isolation, primary structure, and synthesis of human hypothalamic somatocrinin: growth hormone-releasing factor. Proc Natl Acad Sci U S A. 1984;81(14):4302-4306. PubMed
  2. Ling N, Baird A, Wehrenberg WB, et al. Synthesis and in vitro bioactivity of C-terminal deleted analogs of human growth hormone-releasing factor. Biochem Biophys Res Commun. 1984;123(2):854-861. PubMed
  3. 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(2):139-157. PubMed
  4. Corpas E, Harman SM, Piñeyro MA, et al. Growth hormone (GH)-releasing hormone-(1-29) twice daily reverses the decreased GH and insulin-like growth factor-I levels in old men. J Clin Endocrinol Metab. 1992;75(2):530-535. PubMed
  5. Vittone J, Blackman MR, Busby-Whitehead J, et al. Effects of single nightly injections of growth hormone-releasing hormone (GHRH 1-29) in healthy elderly men. Metabolism. 1997;46(1):89-96. PubMed
  6. U.S. Food and Drug Administration. Drugs@FDA: application 019863 (sermorelin acetate); original approval December 28, 1990; marketing status discontinued. Source
  7. U.S. Food and Drug Administration. Drugs@FDA: application 020443 (sermorelin acetate); original approval September 26, 1997; marketing status discontinued. Source
  8. KEGG DRUG D08509: Sermorelin. Formula C149H246N44O42S, molecular weight 3357.89. Source
  9. PubChem. Sermorelin, CID 16132413: C149H246N44O42S, 3357.9 g/mol, CAS 86168-78-7. Source
  10. UniProt P01286: Somatoliberin (human GHRH), mature peptide sequence. Source
  11. Dominikowski A, Rękoś Z, Olejarz M, et al. The emerging landscape of performance-enhancing peptides modulating GH-IGF1 axis: bridging the gap between clinical evidence and patient self-administration. Front Endocrinol (Lausanne). 2026;17:1822475. PubMed

Sources are peer-reviewed publications indexed in PubMed and trial registrations on ClinicalTrials.gov. Each citation was checked against its PubMed record.

For research use only. Not for human consumption.

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