Peptide Registry

Hexarelin Acetate

$75.00

  • Contents: Hexarelin Acetate (Examorelin acetate; His-(D-2-Me-Trp)-Ala-Trp-(D-Phe)-Lys-NH2 acetate salt)
  • Form: Lyophilized powder
  • Purity: >99%
Quantity Discount Price
1 - 3 - $75.00
4 - 7 10% $67.50
8 + 18% $61.50
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Description

Hexarelin Acetate is the acetate salt form of Hexarelin (Examorelin), the synthetic hexapeptide GHSR-1a agonist. The peptide sequence is identical to Hexarelin, with acetate as the counterion rather than the trifluoroacetate or free base forms sometimes encountered in research-grade peptide preparations. The acetate salt form improves aqueous solubility relative to the free base, which is relevant for research protocols requiring precise peptide concentration in aqueous buffer systems. Beyond GHSR-1a, Hexarelin engages CD36 scavenger receptor activity in cardiac tissue models; a secondary receptor interaction that connects it to cardioprotective signaling research independently of its GH secretagogue properties, and that is shared with GHRP-6 but absent from more selective GHSR-1a agonists such as Ipamorelin.

Chemical Information

  • Chemical Name: Hexarelin Acetate (Examorelin acetate)
  • Also Known As: Examorelin; HEX; His-D-2-Methyl-Trp-Ala-Trp-D-Phe-Lys-NH2 acetate salt
  • Sequence: His-(D-2-Me-Trp)-Ala-Trp-(D-Phe)-Lys-NH2
  • Molecular Formula: C47H58N12O6 (free base peptide); C47H58N12O6 x CH3COOH (acetate salt)
  • Molecular Weight: 887.0 Da (free base peptide portion)
  • CAS Number: 208251-52-9 (acetate salt); 140703-51-1 (free base)
  • Salt Form: Acetate (counterion; improves aqueous solubility over free base)
  • Non-standard residues: D-2-methyltryptophan (position 2); D-phenylalanine (position 5)
  • Production: Solid-phase peptide synthesis (SPPS)

Applications

  • GHSR-1a receptor activation studies. Hexarelin Acetate binds GHSR-1a with higher affinity than endogenous ghrelin and activates Gq/11-coupled calcium mobilization signaling; the acetate salt form provides improved solubility for aqueous assay systems compared to free base preparations
  • CD36 scavenger receptor signaling research. Hexarelin engages CD36 in cardiac tissue models independently of GHSR-1a; researchers studying how GH secretagogues interact with peripheral scavenger receptor biology use Hexarelin specifically because this dual receptor profile is absent from more selective GHSR-1a agonists
  • GHRP selectivity spectrum research. Hexarelin sits at the broader end of the GHRP selectivity spectrum alongside GHRP-6 and in contrast to Ipamorelin; comparative designs examining how receptor selectivity differences affect GH pulse amplitude, ACTH co-stimulation, and CD36-mediated signaling use Hexarelin as the broad-spectrum reference compound
  • Salt form comparative studies. The acetate salt and free base forms of Hexarelin carry the same peptide sequence but differ in counterion, which affects aqueous solubility, HPLC retention behavior, and mass spectrometry ionization profiles; researchers designing analytical characterization protocols use both forms to understand how salt form affects compound behavior in their specific assay systems
  • Cardiac biology research. CD36 expression in cardiomyocytes and the Hexarelin-CD36 interaction are studied in ischemia and cardioprotective signaling models; this research angle is specific to Hexarelin among the GHRP class and does not require the GH secretagogue mechanism

Storage and Handling

Store lyophilized powder at -20C for long-term stability, or at 2-8C for short-term use. Protect from heat, moisture, and direct light. The acetate salt form offers improved aqueous solubility; reconstitute in sterile water or bacteriostatic water. Avoid repeated freeze-thaw cycles to maintain compound integrity and GHSR-1a binding activity across experimental batches.

Compliance Notice

Hexarelin Acetate is for laboratory research use only. It is not for human or veterinary use and carries no therapeutic, diagnostic, or clinical indication. This product has not been evaluated by the FDA. By purchasing this product, the buyer confirms that they will follow appropriate institutional safety procedures and use it exclusively for controlled research.

Frequently Asked Questions

What is Hexarelin Acetate and how does it differ from Hexarelin?

Hexarelin Acetate is the acetate salt form of Hexarelin -- the same synthetic hexapeptide sequence (His-(D-2-Me-Trp)-Ala-Trp-(D-Phe)-Lys-NH2) with acetate as the counterion. The peptide itself is chemically identical; the salt form designation refers to the counterion present in the lyophilized preparation. The acetate salt improves aqueous solubility relative to free base preparations, which is relevant for research protocols requiring peptide dissolution in aqueous buffer systems at precise concentrations. CAS 208251-52-9 specifically identifies the acetate salt; CAS 140703-51-1 identifies the free base form.

Why does Hexarelin engage both GHSR-1a and CD36 when more selective GHRPs do not?

GHSR-1a selectivity in the GHRP class correlates with structural modifications introduced in later-generation compounds. Ipamorelin achieves high GHSR-1a selectivity through specific structural features that restrict its pharmacological footprint. Hexarelin's broader receptor engagement, including CD36 in cardiac tissue, reflects its position as an earlier-generation GHRP with a wider pharmacological profile. CD36 is a scavenger receptor expressed in cardiomyocytes, adipose tissue, and immune cells; its engagement by Hexarelin is mechanistically independent of GHSR-1a and operates through separate signaling cascades. Researchers select Hexarelin specifically when this dual receptor profile is the experimental variable.

How does the acetate counterion affect Hexarelin's analytical characterization?

The acetate counterion affects several analytical properties of the lyophilized preparation. In mass spectrometry, the acetate salt produces different ionization behavior than the free base, and the acetate adduct may appear in certain MS acquisition modes. In reversed-phase HPLC, the counterion influences retention time and peak shape under some mobile phase conditions. Researchers switching between acetate salt and free base preparations of the same peptide sequence should account for these differences when comparing analytical data across preparations or when validating bioanalytical methods.