Blend: Ipamorelin CJC-1295 (No DAC) 20MG

GH release from the pituitary is stimulated through two separate receptor systems:

• The GHRH receptor, activated by growth hormone-releasing hormone and its analogs
• The GHRP (ghrelin) receptor, activated by ghrelin and synthetic GH secretagogues such as ipamorelin

This page summarizes one paper related to each system:

• Coy et al. (1991), European Journal of Pharmacology: GHRH (1-29) analogs with alanine substitutions, tested in rat pituitary cells
• Raun et al. (1998), European Journal of Endocrinology: Ipamorelin, tested in rat pituitary cells, anesthetized rats and conscious swine

Neither paper studied the two compounds together.

What it tested: GHRH (1-29) analogs with alanine substitutions at positions 8, 9 and/or 15, some with D-Ala² at position 2. The substitutions were designed to strengthen the peptide's α-helix. Researchers measured GH release from cultured rat pituitary cells.

Findings: The substitutions increased GH-releasing potency in an additive way. The most potent analog, [D-Ala², Ala⁸,⁹,¹⁵]GRH (1-29)NH₂, was about 49 times more potent than the GRH (1-29)NH₂ standard.

Relationship to CJC-1295 No DAC: "CJC-1295 No DAC" usually refers to Modified GRF (1-29), which has D-Ala², Gln⁸, Ala¹⁵ and Leu²⁷. It shares the D-Ala² and Ala¹⁵ substitutions with analogs in this study but is a different peptide, and the 49-fold figure applies only to the analog tested in the paper. The assembled tetrasubstituted sequence appears instead in Jetté et al. (2005), as the peptide core of CJC-1295, which that study tested in its albumin-conjugated form in rats. No published study characterizes the unconjugated peptide on its own.

What it tested: Ipamorelin, a pentapeptide GHRP-receptor agonist, compared with GHRP-6, GHRP-2 and GHRH.

Findings:

• Ipamorelin released GH with potency and efficacy similar to GHRP-6 in rat pituitary cells, anesthetized rats and conscious swine.
• In swine, GHRP-6 and GHRP-2 increased ACTH and cortisol. Ipamorelin did not raise them beyond GHRH-like levels, even at more than 200 times its GH ED₅₀.
• None of the secretagogues changed FSH, LH, prolactin or TSH.

Limitations: Single intravenous doses, anesthetized rats, and 6 swine per compound. The study was conducted by the developing company.

• Receptor: GHRH analogs act on the GHRH receptor. Ipamorelin acts on the GHRP (ghrelin) receptor. In the 1998 study, a GHRH receptor antagonist did not block ipamorelin's effect.
• Structure: Modified GRF (1-29) is a 29-amino-acid GHRH analog. Ipamorelin is a 5-amino-acid peptide (Aib-His-D-2-Nal-D-Phe-Lys-NH₂).
• Evidence type: The Coy paper is an in vitro structure–activity study of related analogs. The Raun paper is a pharmacology study of ipamorelin itself in cells and two animal species.

• Neither paper tested CJC-1295 No DAC and ipamorelin together. Claims of combined or "synergistic" GH release would not be supported by these papers.
• The Coy study did not test Modified GRF (1-29). That sequence appears in Jetté et al. (2005) only as the peptide core of the albumin-conjugated CJC-1295.
• Neither paper establishes effects, safety or dosing for either compound in people.

The Coy et al. (1991) and Raun et al. (1998) papers describe separate lines of GH-secretagogue research. The first covers alanine-substituted GHRH (1-29) analogs in rat pituitary cells, and the second covers ipamorelin's GH release and hormonal selectivity in cells, rats and swine. They do not address the two compounds in combination. Researchers should evaluate each source on its own.

This summary is provided for research and educational purposes. Statements on this page have not been evaluated by the FDA. Research compounds offered on this site are for laboratory research use only. They are not intended for human or veterinary use, or to diagnose, treat, cure, mitigate or prevent any disease.