CJC-1295 (No DAC)
CJC-1295 (No DAC) is a 29-residue C-terminally amidated analogue of the biologically active 1-29 fragment of human growth hormone-releasing hormone, carrying four substitutions relative to the native sequence: D-alanine at position 2, glutamine at position 8, alanine at position 15 and leucine at position 27. Its name is a persistent misnomer. The molecule identified as CJC-1295 in the peer-reviewed literature is a tetrasubstituted hGRF(1-29) bearing an additional N-epsilon-3-maleimidopropionamide derivative of lysine at the C terminus, a drug affinity complex (DAC) that bioconjugates the peptide to the free thiol on Cys34 of serum albumin and extends plasma exposure to the order of a week; the compound sold as 'No DAC' is that peptide's tetrasubstituted core with the maleimide linker removed, so it lacks the very feature that defines CJC-1295 in the published record. It has no marketing authorisation in any jurisdiction for any indication, and growth hormone-releasing hormone and its synthetic analogues are prohibited under Section S2 of the World Anti-Doping Agency Prohibited List. Material of this structure, a 29-amino-acid peptide with a C-terminal amide, was recovered by mass spectrometry from a seized preparation sold under the CJC-1295 name.
Information on this page is provided for laboratory research reference. The compound is not a drug, supplement, or medical product, and is not for human or veterinary use, ingestion, or consumption.
No reviewed report has been published for this product family yet. The molecular values opposite are public reference data, not results measured on a CRX sample.
Browse published reports →- Ala
- D-Alanine
The peptide is an agonist at the growth hormone-releasing hormone receptor (GHRHR), a class B G protein-coupled receptor on anterior pituitary somatotrophs, where receptor occupancy couples through the stimulatory G protein to adenylyl cyclase, raising cyclic AMP and driving both synthesis and release of growth hormone; released growth hormone in turn stimulates hepatic IGF-1 production. Because the signal enters the axis upstream of the pituitary rather than replacing growth hormone itself, secretion remains subject to somatostatin opposition and to negative feedback from growth hormone and IGF-1, and the endogenous pulse generator continues to operate — pulse frequency and amplitude were unaltered in men given the DAC-conjugated analogue. The four substitutions are stability engineering rather than novel pharmacology: D-alanine at position 2 removes the dipeptidyl peptidase IV cleavage site that otherwise inactivates GHRH within minutes in plasma, glutamine at position 8 removes the asparagine that deamidates to alpha- and beta-aspartyl forms of much reduced potency in aqueous solution, leucine at position 27 removes the oxidation-prone methionine, and alanine at position 15 was introduced because it had previously been shown to enhance receptor binding affinity. What is established is the receptor target, the signalling route and the chemical rationale for each substitution. What is not established is this molecule's pharmacokinetic and pharmacodynamic behaviour in humans: without the albumin-binding DAC linker, the sustained exposure demonstrated for CJC-1295 does not apply, and no peer-reviewed human study has reported the no-DAC peptide's half-life or growth hormone response.5,6,7,8,9,10,11
Primary target. Class B GPCR on pituitary somatotrophs; agonist binding activates Gs-adenylyl cyclase-cAMP signalling to promote growth hormone synthesis and secretion.1,6
Not a signalling target but the principal inactivating enzyme the molecule is designed to evade; DPP-4 cleaves the Ala2-Asp3 bond of native GHRH, and a D-configuration residue at position 2 abolishes that cleavage.8,9
Growth hormone axis
A 2026 narrative review of GH-IGF-1 axis peptides assigned CJC-1295 without DAC to its lowest evidence tier, D: no peer-reviewed human studies, only preclinical extrapolation and grey-literature user reports. No controlled clinical study has evaluated it in humans and none reports its half-life. It places the DAC-conjugated form in tier B on phase I pharmacokinetic and pharmacodynamic data in healthy adults, tabulating a half-life of roughly 5.8 to 8 days, still with no controlled efficacy data.5
In two randomised, double-blind, placebo-controlled ascending-dose trials in healthy adults aged 21 to 61, single subcutaneous doses of the DAC-conjugated CJC-1295 raised mean growth hormone 2- to 10-fold for 6 days or more and mean IGF-1 1.5- to 3-fold for 9 to 11 days, half-life 5.8 to 8.1 days; after multiple doses IGF-1 stayed above baseline for up to 28 days. These results describe the conjugate, not the no-DAC peptide.13
In an uncontrolled before-and-after study in healthy men aged 20 to 40, each serving as his own control with no placebo group, a single injection of the DAC-conjugated CJC-1295 raised basal growth hormone 7.5-fold (P < 0.0001), mean growth hormone by 46% (P < 0.01) and IGF-1 by 45% (P < 0.001) one week later, while the frequency and magnitude of secretory pulses were unaltered.11
In normal male Sprague-Dawley rats given a single subcutaneous injection, the albumin-binding conjugate CJC-1295 produced a 4-fold greater growth hormone area under the curve over 2 hours than unmodified hGRF(1-29) and remained in plasma beyond 72 hours, with immunoreactivity on the serum albumin band by Western blot from 15 minutes. The authors attributed the advantage to the C-terminal maleimide that bioconjugates the peptide to albumin, which the no-DAC peptide lacks.1
In GHRH-knockout mice treated from one week of age for five weeks, the DAC-conjugated CJC-1295 given at 24-hour intervals produced normal body weight and length, while the same dose at 48- or 72-hour intervals reached higher body weight and length than placebo-treated knockouts without fully normalising growth. Treatment raised total pituitary RNA and growth hormone mRNA, suggesting somatotroph proliferation, which immunohistochemistry supported. Placebo-treated knockouts and heterozygous littermates served as controls.12
In assays with purified human placental dipeptidyl peptidase IV, native GRF(1-44)-NH2 and the GRF(1-29)-NH2 and GRF(1-20)-NH2 fragments were all cleaved at the Ala2-Asp3 bond at initial rates of approximately 5 micromol per minute per milligram, while analogues carrying a D-configuration residue at the subsites flanking that bond were not cleaved at all. Position 2, which this peptide fills with D-alanine, is one of those subsites.8
In cultured bovine anterior pituitary cells, the asparagine-8 deamidation product [beta-Asp8, Leu27]hGRF(1-32)NH2 was a 400- to 500-fold weaker growth hormone secretagogue than its Asn8 parent, and the alpha-Asp8 form 25-fold weaker. In neutral aqueous buffer the Asn8 parent disappeared with a half-life of 202 hours, extended to 1,550 hours when Asn8 was replaced by serine. This peptide instead carries glutamine at residue 8, removing the same deamidation route.10
Liquid chromatography-high resolution tandem mass spectrometry of an unknown pharmaceutical preparation submitted by Norwegian police and customs authorities in 2009 resolved a 29-amino-acid peptide with a C-terminal amide, consistent with material then sold as CJC-1295. The paper did not distinguish the DAC and no-DAC forms; a 29-residue C-terminally amidated peptide corresponds to the no-DAC structure, not to the maleimidopropionamide-lysine-extended conjugate characterised in the pharmacological literature.2
In fortified human urine, an assay treating sermorelin, tesamorelin, CJC-1295 and CJC-1295 with drug affinity complex as four separate analytes identified 19 in vitro metabolites, characterised in house as reference materials, reaching limits of detection generally at or below the WADA required performance limit of 1 ng/mL. Despite admissions and intelligence indicating use, the authors noted GHRH analogues appeared not to have been found in anti-doping samples.4
What investigators recorded alongside the results above, at the rates their papers state.
No human safety data exist for this compound. A 2026 narrative review of GH-IGF-1 axis peptides classified CJC-1295 without DAC as tier D, no peer-reviewed human studies, reported that no controlled clinical study has directly evaluated it in humans, and recorded that its half-life has not been reported in human studies. Safety inferences are therefore drawn entirely from the DAC-conjugated analogue and from the GHRH class, not from this molecule.5
Not established; no peer-reviewed human studies exist
Adverse effects reported across the GH-IGF-1 axis peptide class in clinical practice and self-administration: endocrine and metabolic disturbance including prolactin and cortisol elevation, appetite change and dysglycaemia; fluid retention syndromes; myalgia and arthralgia; and injection-site reactions. The same review flags a biologically plausible but unproven mitogenic concern from GH/IGF-1 signalling, with no established clinical carcinogenic signal, and notes that no long-term safety data are available for any of these compounds.5
Not quantified; reported as class effects spanning the compounds reviewed
No serious adverse reactions were reported in the two randomised, double-blind, placebo-controlled ascending-dose trials of the DAC-conjugated analogue in healthy adults. The investigators concluded the compound was safe and relatively well tolerated, particularly in the 30 and 60 microgram/kg study arms. The published abstract does not report tolerability findings for the other arms.13
No serious adverse reactions reported
Mild facial flushing lasting 1 to 3 minutes after intravenous GHRH-(1-44)-NH2, the native hormone acting at the same receptor, in normal men. This is the characteristic acute effect of GHRH receptor agonism; no adverse clinical effects or laboratory abnormalities followed the comparator GH-releasing hexapeptide in the same subjects.14
16 of 18 subjects who received GHRH-(1-44)-NH2
Product-quality risk distinct from pharmacological risk. Narrative reviews of the peptide gray market note that unapproved compounds are supplied largely outside regulatory oversight, that many show favourable outcomes in animal models while rigorous human safety data are scarce, and that GH-axis secretagogues including CJC-1295 remain investigational with uncertain safety profiles, product quality concerns and antidoping restrictions. Identity confusion between the DAC and no-DAC forms sold under one name compounds this, since seized material carrying the CJC-1295 label was shown by mass spectrometry to be a 29-residue amide rather than the conjugate.2,15,16
Not quantified
- 1.Human growth hormone-releasing factor (hGRF)1-29-albumin bioconjugates activate the GRF receptor on the anterior pituitary in rats: identification of CJC-1295 as a long-lasting GRF analog. · Endocrinology · 2005 · PMID 15817669
- 2.Identification of CJC-1295, a growth-hormone-releasing peptide, in an unknown pharmaceutical preparation. · Drug Test Anal · 2010 · PMID 21204297
- 3.A method for confirming CJC-1295 abuse in equine plasma samples by LC-MS/MS. · Drug Test Anal · 2019 · PMID 30938069
- 4.Advances in the detection of growth hormone releasing hormone synthetic analogs. · Drug Test Anal · 2021 · PMID 34665524
- 5.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 · PMID 42395176
- 6.Structural basis for activation of the growth hormone-releasing hormone receptor. · Nat Commun · 2020 · PMID 33060564
- 7.Enhanced stability and potency of novel growth hormone-releasing factor (GRF) analogues derived from rodent and human GRF sequences. · Peptides · 1994 · PMID 7937325
- 8.Kinetics of dipeptidyl peptidase IV proteolysis of growth hormone-releasing factor and analogs. · Biochim Biophys Acta · 1992 · PMID 1353684
- 9.Dipeptidylpeptidase IV and trypsin-like enzymatic degradation of human growth hormone-releasing hormone in plasma. · J Clin Invest · 1989 · PMID 2565342
- 10.Degradation of growth hormone releasing factor analogs in neutral aqueous solution is related to deamidation of asparagine residues. Replacement of asparagine residues by serine stabilizes. · Int J Pept Protein Res · 1991 · PMID 1904406
- 11.Pulsatile secretion of growth hormone (GH) persists during continuous stimulation by CJC-1295, a long-acting GH-releasing hormone analog. · J Clin Endocrinol Metab · 2006 · PMID 17018654
- 12.Once-daily administration of CJC-1295, a long-acting growth hormone-releasing hormone (GHRH) analog, normalizes growth in the GHRH knockout mouse. · Am J Physiol Endocrinol Metab · 2006 · PMID 16822960
- 13.Prolonged stimulation of growth hormone (GH) and insulin-like growth factor I secretion by CJC-1295, a long-acting analog of GH-releasing hormone, in healthy adults. · J Clin Endocrinol Metab · 2006 · PMID 16352683
- 14.Growth hormone (GH)-releasing peptide stimulates GH release in normal men and acts synergistically with GH-releasing hormone. · J Clin Endocrinol Metab · 1990 · PMID 2108187
- 15.Safety and Efficacy of Approved and Unapproved Peptide Therapies for Musculoskeletal Injuries and Athletic Performance. · Sports Med · 2026 · PMID 41966639
- 16.Injectable Peptides in Sports Medicine: A Structured Narrative Review of Evidence, Safety, and Antidoping Implications. · JBJS Rev · 2026 · PMID 42160466
- 17.Determinants of GH-releasing hormone and GH-releasing peptide synergy in men. · Am J Physiol Endocrinol Metab · 2009 · PMID 19240251