Peptides & growth hormone

CJC-1295 (No DAC)

Updated · 21 sources · Editorial policy

“CJC-1295 no DAC” is a market name for a synthetic peptide built from the active 29-amino-acid fragment of growth hormone-releasing hormone (GHRH), the hypothalamic hormone that tells the pituitary gland to release growth hormone (GH). Four amino acids in that fragment are substituted, which makes the peptide more resistant to the blood enzymes that destroy natural GHRH (Dominikowski et al., Front Endocrinol 2026). Doping-control laboratories and sellers also call the same molecule “modified GRF (1-29)” or “Mod GRF 1-29,” covered separately in this library at MOD-GRF (1-29).

The naming is genuinely confusing. In the paper that introduced it, “CJC-1295” was the version carrying a drug affinity complex (DAC), a chemical group that bonds the peptide to albumin in the blood (Jetté et al., Endocrinology 2005) and stretches its half-life in healthy adults to an estimated 5.8–8.1 days (Teichman et al., JCEM 2006). What is sold as “no DAC” is the same peptide backbone without that albumin-binding group, so it behaves like a short-acting GHRH analog instead.

The single most important fact: no controlled human study of the no-DAC peptide has been published, and it has never been approved as a medicine. A 2026 review of GH-axis peptides concluded that this compound “remains essentially uncharacterised in the peer-reviewed human literature,” with its reported effects extrapolated from related molecules (Dominikowski et al., 2026).

This page summarizes what the published chemistry, doping-control and regulatory literature reports. It is for education only and is not medical advice.

Property Detail
Class Synthetic GHRH analog (growth hormone-releasing factor)
Other names Modified GRF (1-29), Mod GRF 1-29; also labeled simply “CJC-1295” in several doping-control papers
Mechanism Binds the GHRH receptor on pituitary somatotroph cells, which then release GH
Route Not established; no published human study of this peptide reports a route of administration
Human trials None published for this peptide; published trials cover only the DAC version and the related approved drugs
Half-life Not measured in humans; the unmodified parent fragment clears from plasma within minutes
Approval status Never approved by FDA or EMA; no prescribing information exists
FDA compounding Named by FDA among bulk substances that may present significant safety risks (nomination later withdrawn)
WADA status Prohibited at all times under S2.2.4, GHRH and its analogues

What it is

Natural human GHRH is 44 amino acids long, but its first 29 residues carry essentially all of the hormone’s activity. That amidated 29-residue fragment is itself a drug: sermorelin, once sold as Geref (Knoop et al., Anal Bioanal Chem 2016; Esposito et al., Adv Drug Deliv Rev 2003). CJC-1295 no DAC is that same fragment with four of its amino acids exchanged for others.

Two problems limit natural GHRH as a drug, and the substitutions address the first:

  • Enzymatic cleavage. The plasma enzyme dipeptidyl peptidase IV (DPP-IV) clips the first two amino acids off GHRH, and the resulting fragment has less than a thousandth of the parent’s biological activity. After intravenous GHRH in healthy volunteers, the cleaved product appeared in plasma within one minute and the intact hormone had a half-life of 6.8 minutes (Frohman et al., J Clin Invest 1986). Replacing the second amino acid with its mirror-image (D) form blocks this cut. In 10 healthy men given constant infusions, that single change cut metabolic clearance roughly in half, from 39.7 to 21 mL/kg/min, and lengthened the disappearance half-time from 4.3 to 6.7 minutes (Soule et al., JCEM 1994).
  • Rapid clearance by the kidney. Even protected from DPP-IV, a peptide this small is filtered out quickly; the unmodified fragment’s plasma half-life in humans is about 10–20 minutes (Esposito et al., 2003). Substitutions do not fix this, which is why longer-acting versions attach the peptide to albumin (the DAC approach) or to polyethylene glycol.

So the four substitutions buy resistance to one enzyme, not long duration. Nothing published measures how long the no-DAC peptide actually lasts in people.

ConjuChem, the Montreal company behind the molecule, took the four-substitution GRF(1-29) peptide and added a group that bonds covalently to albumin after injection. That albumin-binding conjugate is what the developer called CJC-1295, and what later papers call “CJC-1295 with DAC” (Jetté et al., 2005).

Usage since then has drifted:

  • A preparation seized in Norway in 2009 and sold as “CJC-1295” turned out on mass spectrometry to contain a 29-amino-acid amidated peptide, not the albumin-binding conjugate (Henninge et al., Drug Test Anal 2010).
  • Anti-doping method papers routinely use “CJC-1295” for the non-conjugated peptide and spell out “CJC-1295 with drug affinity complex” for the conjugate (Knoop et al., 2016; Memdouh et al., Drug Test Anal 2021).
  • Danish forensic chemists analyzing seized powders called the same peptide “modified growth hormone releasing factor (modified GRF 1-29)” (Gajda et al., Drug Test Anal 2019).
  • A 2026 clinical review lists the compound as “CJC-1295 (without DAC) (Mod GRF 1-29/Mod GHRH 1-29),” treating all three as one entry (Dominikowski et al., 2026).
Name Relationship to this page Status
MOD-GRF (1-29) Usually the same molecule under a different market name Never approved
CJC-1295 w/ DAC Same peptide backbone plus an albumin-binding group; half-life estimated at 5.8–8.1 days in healthy adults Never approved; development discontinued
Sermorelin The unmodified GHRH(1-29) fragment, no substitutions FDA-approved as Geref (NDA 020443, 1997); discontinued
Tesamorelin GHRH(1-44) with a fatty-acid group added at one end FDA-approved as Egrifta, 2010
Ipamorelin, GHRP-2, GHRP-6 Not GHRH analogs; these act on the ghrelin receptor instead Never approved

Because sermorelin and tesamorelin were approved drugs, they have labels, trial data and known safety profiles. The no-DAC peptide has none of those, and findings from the approved analogs cannot be assumed to carry over to it.

What the research shows

On this peptide

Nothing in humans. The 2026 review that systematically catalogued GH-axis peptides found no peer-reviewed human studies of CJC-1295 without DAC: no published route of administration, no human half-life, no efficacy data, and no safety data (Dominikowski et al., 2026). Claims that it produces more “physiologic” GH pulses, or that it changes body composition, trace to extrapolation from GHRH(1-29) and to non-academic sources rather than to trials of the peptide itself.

The non-conjugated peptide has been given to animals in analytical work. When 0.1 mg was injected intravenously into Wistar rats, the intact peptide was still detectable in plasma 8 hours later, the last sampling point; sermorelin, by contrast, was detectable only at 2 hours. The authors noted that these were qualitative detection results only, with no pharmacokinetic interpretation, and the work was in rats, not people (Knoop et al., 2016).

On the DAC version, for contrast

The albumin-binding conjugate was taken into clinical trials. In two randomized, placebo-controlled, double-blind ascending-dose studies in healthy adults aged 21–61, a single subcutaneous injection raised mean plasma GH 2- to 10-fold for 6 days or more and IGF-I 1.5- to 3-fold for 9–11 days, with an estimated half-life of 5.8–8.1 days and no serious adverse reactions reported (Teichman et al., JCEM 2006). A separate study in healthy men aged 20–40 sampled GH every 20 minutes overnight one week after a single injection and found trough GH raised about 7.5-fold (p under 0.0001), mean GH up 46% (p under 0.01) and IGF-I up 45% (p under 0.001), with pulse frequency and amplitude unchanged (Ionescu and Frohman, JCEM 2006).

Those results describe the conjugate at the doses tested, not the no-DAC peptide. The conjugate was never approved and its development did not continue.

On the “more natural pulses” claim. The argument usually made for the no-DAC version is that a short-acting GHRH analog preserves natural GH pulsing better than a long-acting one. The one human study that measured GH pulsatility directly tested the long-acting DAC conjugate and found pulse frequency and amplitude preserved. No published human study has compared pulsatility between the two versions.

Side effects and risks

No human safety data exist for this specific peptide, so the risks below come from regulators, from the related approved GHRH drugs and from the class generally.

What FDA has said

FDA placed CJC-1295 in category 2 of its bulk drug substances review, the list of substances that “may present significant safety risks” when used in compounded drugs. FDA’s stated concerns were risk of immunogenicity by certain routes, complexity around peptide-related impurities and characterization of the active ingredient, limited clinical data, and serious adverse events it identified with CJC-1295 including increased heart rate and a systemic vasodilatory reaction (FDA bulk drug substances, category 2). The nomination for CJC-1295 was subsequently withdrawn by the nominator, so it sits in FDA’s table of withdrawn nominations; either way, no FDA-approved or FDA-sanctioned compounded product containing it exists.

Class-level concerns

  • GH and IGF-I elevation. Anything that raises GH raises IGF-I downstream. The 2026 review flags mitogenic GH/IGF-I signaling as a theoretical oncologic concern across this class, while noting there is no established clinical carcinogenic signal (Dominikowski et al., 2026).
  • Glucose tolerance. GH opposes insulin. In a trial of a long-acting PEGylated GHRH in healthy elderly subjects, repeated dosing produced some impairment of glucose tolerance, and injection-site reactions were more frequent than with placebo (Munafo et al., Eur J Endocrinol 2005).
  • Immunogenicity. Antibody formation is a standard concern for injected peptide analogs and is one of the risks FDA named for compounded CJC-1295. The PEG-GHRH trial above did not detect anti-GHRH antibodies, but that was a different molecule.
  • Unknown unknowns. With no published human trial, there is no systematic record of adverse events, no dose at which safety has been demonstrated, and no information on long-term use.

Product quality

Peptides sold under these names are not made to pharmaceutical standards, and analyses of seized material repeatedly find the labeled identity wrong or the chemistry imperfect:

  • Danish customs seizures of GH-secretagogue powders, including material identified as modified GRF 1-29, all carried an extra glycine added at one end of the peptide compared with reference standards (Gajda et al., 2019).
  • A confiscated product sold as a GHRH analog was found to contain a modified 44-amino-acid GHRH variant with incomplete amidation at one end, which the authors described as revealing the poor pharmaceutical quality of the preparation and a public-health concern (Esposito et al., Drug Test Anal 2014).
  • The 2009 Norwegian case showed that a vial labeled “CJC-1295” need not contain the molecule that name originally described (Henninge et al., 2010).

In the US, this peptide is not a controlled substance; the anabolic steroid schedule in 21 CFR 1308.13 does not name GHRH analogs. It is instead an unapproved new drug: there is no FDA-approved product containing it, and FDA has flagged it as a compounding safety risk.

In sport it is banned. The WADA 2026 Prohibited List prohibits growth hormone releasing factors at all times, in and out of competition, under section S2.2.4, and names GHRH and its analogues with CJC-1295 given as an example alongside CJC-1293, sermorelin and tesamorelin. The “including, but not limited to” wording means alternative market names do not place a molecule outside the ban.

Detection has improved. WADA-accredited laboratories have published validated methods that identify the intact peptide in plasma at under 50 pg/mL (Knoop et al., 2016) and in urine at or below WADA’s 1 ng/mL required performance limit (Memdouh et al., 2021; Uçaktürk and Nemutlu, J Pharm Biomed Anal 2026). Because the substitution at position 2 blocks the cleavage that destroys sermorelin, the intact peptide persists longer in samples than sermorelin does, which makes it the easier of the two to detect (Knoop et al., 2016).

Key takeaways

  • One molecule, several names. “CJC-1295 no DAC,” “modified GRF (1-29)” and “Mod GRF 1-29” generally refer to the same four-substitution GHRH(1-29) peptide. The original CJC-1295 of the 2005 literature was the albumin-binding version.
  • No human evidence. A 2026 review found no peer-reviewed human studies of this peptide: no established route, no measured half-life, no efficacy data, no safety data.
  • The trial data belong to its siblings. Published human results come from the DAC conjugate and from the approved drugs sermorelin and tesamorelin, and cannot be assumed to transfer.
  • The substitutions buy enzyme resistance, not duration. Blocking DPP-IV cleavage roughly halved clearance of the parent peptide in healthy men, but small peptides are still cleared by the kidney within minutes.
  • FDA has flagged it. FDA listed CJC-1295 among bulk substances that may present significant safety risks, citing limited clinical data and serious adverse events including increased heart rate and a systemic vasodilatory reaction.
  • Banned in sport and detectable. Prohibited at all times under WADA S2.2.4, with validated laboratory methods now reaching sub-nanogram-per-milliliter limits.

Sources

  1. Jetté L, Léger R, Thibaudeau K, et al. 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;146(7):3052–3058. PubMed.
  2. Teichman SL, Neale A, Lawrence B, Gagnon C, Castaigne JP, Frohman LA. 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;91(3):799–805. PubMed.
  3. Ionescu M, Frohman LA. 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;91(12):4792–4797. PubMed.
  4. Dominikowski A, Rękoś Z, Olejarz M, Szczepanek-Parulska E, 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.
  5. Knoop A, Thomas A, Fichant E, Delahaut P, et al. Qualitative identification of growth hormone-releasing hormones in human plasma by means of immunoaffinity purification and LC-HRMS/MS. Anal Bioanal Chem. 2016;408(12):3145–3153. PubMed; PMC.
  6. Memdouh S, Gavrilović I, Ng K, Cowan D, Abbate V. Advances in the detection of growth hormone releasing hormone synthetic analogs. Drug Test Anal. 2021;13(11–12):1871–1887. PubMed.
  7. Henninge J, Pepaj M, Hullstein I, Hemmersbach P. Identification of CJC-1295, a growth-hormone-releasing peptide, in an unknown pharmaceutical preparation. Drug Test Anal. 2010;2(11–12):647–650. PubMed.
  8. Gajda PM, Holm NB, Hoej LJ, Rasmussen BS, et al. Glycine-modified growth hormone secretagogues identified in seized doping material. Drug Test Anal. 2019;11(2):350–354. PubMed.
  9. Esposito S, Deventer K, Van Eenoo P. Identification of the growth hormone-releasing hormone analogue [Pro1, Val14]-hGHRH with an incomplete C-term amidation in a confiscated product. Drug Test Anal. 2014;6(11–12):1155–1159. PubMed.
  10. Frohman LA, Downs TR, Williams TC, Heimer EP, et al. Rapid enzymatic degradation of growth hormone-releasing hormone by plasma in vitro and in vivo to a biologically inactive product cleaved at the NH2 terminus. J Clin Invest. 1986;78(4):906–913. PubMed.
  11. Soule S, King JA, Millar RP. Incorporation of D-Ala2 in growth hormone-releasing hormone-(1-29)-NH2 increases the half-life and decreases metabolic clearance in normal men. J Clin Endocrinol Metab. 1994;79(4):1208–1211. PubMed.
  12. Bai JP, Chang LL. The involvement of dipeptidyl peptidase IV in brush-border degradation of GRF(1-29)NH2 by intestinal mucosal cells. J Pharm Pharmacol. 1995;47(8):698–701. PubMed.
  13. Bongers J, Felix AM, Campbell RM, Lee Y, Merkler DJ, Heimer EP. Semisynthesis of human growth hormone-releasing factors by alpha-amidating enzyme catalyzed oxidation of glycine-extended precursors. Pept Res. 1992;5(4):183–189. PubMed.
  14. Esposito P, Barbero L, Caccia P, et al. PEGylation of growth hormone-releasing hormone (GRF) analogues. Adv Drug Deliv Rev. 2003;55(10):1279–1291. PubMed.
  15. Munafo A, Nguyen TX, Papasouliotis O, Lécuelle H, Priestley A, Thorner MO. Polyethylene glycol-conjugated growth hormone-releasing hormone is long acting and stimulates GH in healthy young and elderly subjects. Eur J Endocrinol. 2005;153(2):249–256. PubMed.
  16. Uçaktürk E, Nemutlu E. Analysis of growth hormone releasing hormone and its analogs in urine using nano liquid chromatography coupled with quadrupole/orbitrap mass spectrometry. J Pharm Biomed Anal. 2026;268:117207. PubMed.
  17. Food and Drug Administration. Certain bulk drug substances for use in compounding may present significant safety risks (category 2 under the interim policies). FDA.
  18. Food and Drug Administration. Drugs@FDA: Geref (sermorelin acetate), NDA 020443, approved September 26, 1997, now discontinued. Drugs@FDA.
  19. Food and Drug Administration. Drugs@FDA: Egrifta (tesamorelin), BLA 022505, approved November 10, 2010. Drugs@FDA.
  20. World Anti-Doping Agency. 2026 Prohibited List, section S2.2.4 (growth hormone releasing factors), in effect 1 January 2026. WADA 2026 Prohibited List.
  21. Drug Enforcement Administration. Schedule III controlled substances, 21 CFR 1308.13. 21 CFR 1308.13.