CJC-1295 No DAC

What CJC-1295 No DAC is

CJC-1295 No DAC is a lab-made peptide that prompts the body to release growth hormone (GH). What is known about it comes mostly from rats, from cell tests and from drug-testing labs. As of April 2026, there is little direct human research on this form. The lab that created it ran most of its human blood-level studies on a sister compound, CJC-1295 with DAC. Later outside work on the No DAC form has centered on anti-doping tests in human and horse samples [10], [12], [14]. The FDA, the EMA and the MHRA have not approved it as a treatment.

A peptide is a short chain of amino acids, the building blocks of protein. This one has 29. It is an analog, meaning a changed copy, of human GHRH (growth hormone-releasing hormone). GHRH is the body’s own signal that tells the pituitary gland, a gland at the base of the brain, to let out GH.

The copy covers the first 29 amino acids of natural GHRH, which is the stretch that does the work. Four of them have been swapped: numbers 2, 8, 15 and 27 in the chain. The swaps shield the peptide from enzymes that would break it down. It still holds on to the GHRH receptor, the spot on a cell where GHRH attaches [1].

Science papers mostly use other names for it. The three most common are MOD-GRF 1-29, modified GRF(1-29) and tetrasubstituted GRF(1-29)NH2.

Why “No DAC” matters

Two different compounds share the name CJC-1295, and “No DAC” tells them apart.

• With DAC. Jetté and colleagues described the first CJC-1295 in 2005. It had an extra piece on its tail end, the C-terminus. The piece is a maleimidopropionic acid linker, known as a Drug Affinity Complex (DAC). It lets the peptide form a fixed chemical bond, called a covalent bond, with albumin, a protein that travels in blood serum [1]. Riding on albumin makes the peptide last far longer. Published human data show that one injection of CJC-1295 with DAC raises GH for 6 days or more and IGF-1 for 9 to 11 days [2].
• No DAC. Take the linker away and the peptide is free again and short-acting. Its half-life is often given as about 30 minutes, and its GH effects are expected to fade within hours. No paper in this guide’s reference list measured that figure in people. Half-life is the time it takes for half of a compound to leave the blood.

A lot of online and sales material lumps both under the one label “CJC-1295”. On this page, the No DAC name means only the free analog, tetrasubstituted GRF(1-29)NH2. The DAC-bound form has its own guide. It moves through the body differently, and its published evidence is not the same.

How much research there is

The basic drug science is well mapped. The human papers are mostly about the DAC form.

Question	Answer
Published studies on CJC-1295, either form	28 listed in PubMed under the search term “CJC-1295” (April 2026). The “25+” at the top of this page counts something else: the papers in this guide’s reference list, which also covers background work on GHRH and on drug testing
Studies that used MOD-GRF 1-29 (No DAC) itself	Few. Mainly animal and lab work, and detection methods
Phase I data in people	In print for the DAC form [2], [4], [3]. None found for No DAC
Checked by other labs	Detection methods: widely, by many labs. Effects on GH: little outside the group that created it
Randomized controlled trials	None found for this form on any treatment outcome
Evidence grade	Preclinical. What human data exist are limited and mostly about the DAC form
Approval	None (FDA, EMA, MHRA)

How it might work

CJC-1295 No DAC works at the pituitary gland. It is a GHRH receptor agonist, meaning a compound that switches that receptor on. Four things shape what it does: how it attaches, what the four swaps change, what the missing DAC linker means for timing, and the IGF-1 system that follows.

Attaching to the GHRH receptor

The GHRH receptor is shortened to GHRHR. It belongs to class B of the G-protein-coupled receptors, a common family of cell switches. It is found almost only on somatotrophs, the cells in the front part of the pituitary that make GH [16], [17].

When GHRH or an analog attaches, a chain of steps follows [17]:

1. The receptor turns on an enzyme, adenylate cyclase, through a link called Gαs.
2. Levels of cyclic AMP (cAMP), a messenger inside the cell, go up.
3. The cell makes more GH and sends it into the small blood vessels that drain the pituitary, the hypophyseal portal circulation.

Natural GHRH is 44 amino acids long. Residues 1 to 29, at the N-terminal or front end, hold everything needed to bind and switch on the receptor. The back end is not needed for action at the pituitary [1].

CJC-1295 No DAC keeps that working front end. In pituitary cells studied on their own, it bound GHRHR about as tightly as natural GHRH did. The cAMP signal and the GH release were equal too [1].

Tang and colleagues reported a separate class of GHRH analogs, each with four swaps. In rodent pituitary tests, their work confirmed that swaps at several sites along the 1 to 29 chain can keep or raise GH release through the receptor [18], [19].

The four swaps, and the DAC linker

Natural GHRH(1-29) does not last in the blood. In humans its half-life is around 7 minutes. It gets cut fast in two places [1]:

• An enzyme called dipeptidyl peptidase-IV (DPP-IV) cuts the bond between Ala2 and Asp3.
• Trypsin-like activity in plasma cuts at an Asn site inside the chain.

Both forms of CJC-1295 carry the same four swaps, meant to block both of these routes.

Swap	What it does
D-Ala2	Stands up to cutting by DPP-IV
Gln8	Takes the place of an Asn that trypsin-like enzymes attack
Ala15	Adds stability to the middle of the chain
Leu27	Takes the place of a Met that oxidizes easily

With all four, the half-life is often given as about 30 minutes. That would be long enough for a strong GH release. It would also be brief enough that the effect comes as a pulse and does not linger.

The DAC form has one more part. A maleimidopropionic acid linker is fixed at Lys30. Inside the body it forms a thioether bond with a free Cys34 on human serum albumin in the blood [1]. The binding is described as permanent [4]. Albumin has a half-life of about 19 days. The bound peptide takes on much of that long stay. In people its half-life was 5.8 to 8.1 days. One dose raised GH for 6 days or more and IGF-1 for 9 to 11 days [2].

The short-acting form has no maleimide linker. It does not join to albumin, so it does not pick up the longer half-life.

Some sales and online material says the No DAC peptide has a “hexenoyl trans-3 modification”. That wording goes back to early technical write-ups of how the DAC linker is built. It is wrong for this molecule, which has no lipid or hexenoyl group on it. The right description is GRF(1-29)NH2 with four swaps and nothing added at the C-terminus to bind albumin.

One pulse at a time

The body lets out GH in separate bursts every 3 to 5 hours. Two signals from the hypothalamus, a part of the brain, mainly set the rhythm. GHRH pushes release and somatostatin holds it back [16], [20]. The size and timing of the bursts change with age, sex and the state of the metabolism. Delivery in pulses is thought to matter for how well tissues respond to GH [20].

CJC-1295 No DAC clears within hours. So one dose gives one GH pulse. That pulse sits on top of the body’s own rhythm and does not flatten it. The DAC form is different. It gives nonstop GHRH-like stimulation, above normal body levels, for days at a stretch.

Ionescu and Frohman ran a key human study on this. Even under constant GHRH stimulation, the somatotrophs kept pulsing. GH peaks could still be picked out above the raised baseline. This points to somatostatin still gating release, whatever the GHRH exposure [4].

For scientists working with the No DAC form, this makes the timing of blood samples critical. After a dose of a short-acting GHRH analog, GH is expected to peak within 30 to 60 minutes and be back near baseline by about 3 hours. No published human study has measured this timing for the No DAC form.

IGF-1 further down the chain

Released GH travels to the liver and to outlying tissues. There it attaches to the GH receptor and turns on a signal route called JAK2/STAT5. The cell then starts making IGF-1, or insulin-like growth factor 1 [16]. IGF-1 carries out most of the effects of GH on bone, muscle, cartilage and other connective tissue. These include tissue building, cell division and metabolism.

• DAC form. A single dose in healthy adults raised IGF-1 to 1.5 to 3 times baseline for 9 to 11 days [2].
• No DAC form. Published human IGF-1 data are sparse. The GH pulse is brief, so the IGF-1 response is expected to be much smaller and shorter than with DAC. No published peer-reviewed human study has formally measured it.
• Blood proteins. Sackmann-Sala and colleagues used the DAC form in a proteomic study, a survey of many proteins at once. They found shifts in several blood proteins one week after a dose and proposed them as possible markers of GH and IGF-1 action. Nobody can assume the same changes apply to No DAC [3].

What the studies found

One problem keeps coming up in reading this research. Several well-known papers with “CJC-1295” in the title really used the DAC-bound molecule. Their results are marked below so the two forms do not get mixed up.

Blood-level studies in people

The main human papers with “CJC-1295” as their label were done with the DAC form.

• Teichman and colleagues, 2006. This phase I work enrolled healthy adults aged 21 to 61. In the first trial, each got one dose of CJC-1295 (with DAC) under the skin. Mean GH went up 2- to 10-fold for 6 days or more. Mean IGF-1 went up 1.5- to 3-fold for 9 to 11 days. The rises grew with dose. The half-life ran from 5.8 to 8.1 days. In a second trial, people got two or three doses, and mean IGF-1 stayed above baseline for up to 28 days [2].
• Ionescu and Frohman. Also with the DAC form, they recorded that GH still came out in pulses for the whole period that baseline release was raised [4].

For the short-acting form, peer-reviewed human data of this kind are limited. The first animal paper, by Jetté and colleagues, found that the free tetrasubstituted GRF(1-29)NH2 released GH in rats for a few hours. That fits a short plasma half-life. The paper did not produce human blood-level curves for that molecule [1].

Later data that bear on humans come mainly from studies of detection methods in urine and blood. These show that the compound is present and how it clears. They do not give a full set of pharmacokinetic measures, the numbers that describe how the body handles a drug [10], [14].

The shape of the GH response

Many things shape how much GH a GHRH analog releases. They include dose, route, the level of somatostatin at the time, sex, age and how sound the person’s GH system is to begin with [20].

For short-acting GHRH analogs like this one, published data and models of body function point to a typical pattern:

• GH climbs steeply within 15 to 30 minutes of a dose under the skin.
• It usually peaks 30 to 60 minutes after the dose.
• It is back near baseline within about 3 hours.
• GH rises less when the dose lands at a time of high natural somatostatin, for example after a meal.
• Giving it together with a ghrelin mimic, also called a GH secretagogue (ipamorelin is one), yields a synergistic response. That means more GH than either compound gives alone. Much of the research on combinations rests on this finding [20].

The GH system also differs by sex. In women the pulses are bigger and more irregular than in men. This probably affects the size of the response to any GHRH analog [20].

No DAC and DAC side by side

This table lists the main published differences. Each study belongs to one form or the other.

Feature	No DAC	With DAC
Structure	GRF(1-29)NH2 with four swaps (tetrasubstituted)	The same four-swap GRF(1-29) plus an MPA-DAC linker at the C-terminus
Binds albumin	No	Yes, by covalent bond to Cys34 on the albumin in serum
Apparent half-life	Often given as about 30 minutes. Not measured in a published human study	5.8 to 8.1 days in humans [2]
Pattern of GH release	One pulse lasting 1 to 3 hours	Raised baseline with pulses on top, for 6 days or more
Direct human trials	Limited. Mostly rodent work or detection tests	Phase I in healthy adults [2], [4], [3]
Usual name in papers	“MOD-GRF 1-29”, “Modified GRF 1-29” or “tetrasubstituted GRF(1-29)NH2”	“CJC-1295-DAC” or plain “CJC-1295”

Drug testing in sport

A large part of the peer-reviewed work on this peptide is lab chemistry and doping-control methods. The reason is that both forms are banned by WADA, the World Anti-Doping Agency. They fall under section S2 of its Prohibited List, the section for peptide hormones, growth factors, related substances and mimetics. Within S2 they sit in the subclass for GHRH and its analogs [25].

Examples of the methods work:

• Henninge and colleagues identified CJC-1295 in seized drug products. That confirmed the molecule is in the illegal supply chain [10].
• Labs pulled GHRH analogs, CJC-1295 No DAC among them, out of human plasma and urine with antibodies (immunoaffinity purification), then detected them by LC-HRMS/MS [11], [14], [13], [27].
• Timms and colleagues built horse tests to confirm that racehorses had been given CJC-1295 [22], [23].
• A nanoLC-HRMS/MS method that uses ultrafiltration and no antibodies picks it up in urine at pg/mL levels [24].
• Reviews trace how the plan for detecting GHRH analogs has changed over time [12], [28].

Peer-reviewed studies of online groups and internet forums, called netnographic studies, have recorded patterns of use without medical oversight in bodybuilding circles. They show the public health setting these tests work in [8], [9].

Animal studies

There are fairly few animal studies of the No DAC form. Closely related work helps fill in the picture.

• Rats, both forms. Jetté and colleagues gave single doses under the skin. The free tetrasubstituted GRF(1-29)NH2 caused a strong but brief GH release. The DAC-bound form kept plasma GH and IGF-1 raised for several days [1].
• Mice missing GHRH. Alba and colleagues gave CJC-1295 (with DAC) once a day to GHRH knockout mice. Growth returned to normal. Pituitary GH output came back and so did growth in length [6].
• Mother to fetus. Fiorotto and colleagues recorded a GHRH peptide crossing the placenta in the rat. This bears on where GHRH-class analogs travel in the body more broadly [7].
• Related analogs. Tang and colleagues described a family of human GHRH analogs with four swaps and a changed N-terminus, close cousins of the GRF(1-29) frame. Their work gives outside data linking structure to activity [18], [19].
• Another way to extend half-life. Youn and Lee attached PEG to chosen sites on GRF(1-29). It shows a parallel approach to longer half-life that fed into the design of CJC-1295 [26].

Safety

In animals

• Short-term doses given to rats and dogs caused no obvious organ damage at doses that gave the most GH release [1].
• In the mouse study with GHRH knocked out, which used the DAC form, growth in length was restored with no harmful effects reported over the length of the study [6].
• No formal LD50, the dose that kills half the test animals, has appeared in a peer-reviewed journal for the short-acting form.

In people

There is little human safety information on the short-acting form. The phase I study from 2006 used CJC-1295 with DAC. The side effects reported most often were brief reactions where the needle went in, and flushing. At the doses tested, the study drug was not blamed for any serious adverse event [2]. These results cannot be carried straight over to No DAC, because the body’s exposure to it over time is different.

What is not known

• Nobody has published long-term safety data in people for this form.
• There are no formal drug interaction studies. In theory there are concerns about use alongside other agents that act on GH, insulin, or corticosteroids.
• By analogy with approved GH therapies, switching on the GH system is not recommended in three settings. These are active or untreated cancer, diabetic retinopathy, and Prader-Willi syndrome when severe obesity is present.
• There is no data by sex, in children or in pregnancy.
• Purity from batch to batch is a real concern for research-grade peptide. Lab analysis of seized illegal material has found impurities and products that were not what they claimed to be [10].

Legal status in the US

• Not FDA approved. CJC-1295 No DAC has no approval as a treatment from the FDA. The same is true of the EMA in Europe and the MHRA in the UK.
• Banned in sport. WADA names CJC-1295 and GHRH analogs in section S2 of its Prohibited List. They are banned at all times, in competition and out of it [25].
• Research use. It is sold for laboratory research use only, not for human use.

Limits of the research

1. Two compounds, one label. Much sales and internet material says “CJC-1295” without stating whether DAC is present. So do some reviews that are otherwise of high quality. A reported half-life of days to weeks belongs to the DAC form. A reported half-life of minutes to hours belongs to No DAC.
2. Little direct human data. The main phase I work used the DAC-bound molecule. That covers Teichman and colleagues, Ionescu and Frohman, and Sackmann-Sala and colleagues. Human data on blood levels and GH effects for the No DAC form have not reached print at that standard.
3. Mostly rodent data. Evidence on how it works at the receptor is strong across species. Long-term outcome data are limited in every species.
4. One source. The drug research behind CJC-1295 was done mainly by one company group, ConjuChem. It worked with academic partners, among them Frohman, of the University of Illinois at Chicago. No outside group has published a repeat of the GH effects of the No DAC form in human subjects.
5. Informal sources and publication bias. A large share of the practical data on this form sits outside peer review. It is found in internet forums, anti-doping case reports and similar material. Published netnographic studies have cataloged it [8], [9]. It is not evidence that the compound works or is safe.
6. No randomized controlled trials. None is in print for this form against any treatment outcome. Current peer-reviewed papers support GHRH receptor binding and GH release. They cannot support claims of benefit beyond that.

The chemistry of CJC-1295 No DAC is well mapped. Nearly every human result under the CJC-1295 name belongs to the DAC form.

References

Selected peer-reviewed references. Ordered approximately by date of publication. Each entry links to PubMed or to the Crossref DOI record.

1. Jetté L, Léger R, Thibaudeau K, et al. (2005). 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, 146(7), 3052–3058. DOI: 10.1210/en.2004-1286. PMID: 15817669
2. Teichman SL, Neale A, Lawrence B, Gagnon C, Castaigne JP, Frohman LA. (2006). 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. Journal of Clinical Endocrinology & Metabolism, 91(3), 799–805. DOI: 10.1210/jc.2005-1536. PMID: 16352683
3. Sackmann-Sala L, Ding J, Frohman LA, Kopchick JJ. (2009). Activation of the GH/IGF-1 axis by CJC-1295, a long-acting GHRH analog, results in serum protein profile changes in normal adult subjects. Growth Hormone & IGF Research, 19(6), 471–477. DOI: 10.1016/j.ghir.2009.03.001. PMID: 19386527
4. Ionescu M, Frohman LA. (2006). Pulsatile secretion of growth hormone (GH) persists during continuous stimulation by CJC-1295, a long-acting GH-releasing hormone analog. Journal of Clinical Endocrinology & Metabolism, 91(12), 4792–4797. DOI: 10.1210/jc.2006-1702. PMID: 17018654
5. Sackmann-Sala L, Ding J, Frohman LA, Kopchick JJ. (2009). Activation of the GH/IGF-1 axis by CJC-1295, a long-acting GHRH analog, results in serum protein profile changes in normal adult subjects. Growth Hormone & IGF Research, 19(6), 471–477. PMID: 19386527
6. Alba M, Fintini D, Sagazio A, et al. (2006). Once-daily administration of CJC-1295, a long-acting growth hormone-releasing hormone (GHRH) analog, normalizes growth in the GHRH knockout mouse. American Journal of Physiology — Endocrinology and Metabolism, 291(6), E1290–E1294. DOI: 10.1152/ajpendo.00201.2006. PMID: 16822960
7. Fiorotto ML, Lopez R, Oliver WT, et al. (2006). Transplacental transfer of a growth hormone-releasing hormone peptide from mother to fetus in the rat. DNA and Cell Biology, 25(8), 429–437. DOI: 10.1089/dna.2006.25.429. PMID: 16907640
8. Van Hout MC, Hearne E. (2016). Netnography of female use of the synthetic growth hormone CJC-1295: pulses and potions. Substance Use & Misuse, 51(1), 73–84. DOI: 10.3109/10826084.2015.1082595. PMID: 26771670
9. Pineau T, Schopfer A, Grossrieder L, et al. (2016). The study of doping market: how to produce intelligence from Internet forums. Forensic Science International, 268, 103–115. DOI: 10.1016/j.forsciint.2016.09.017. PMID: 27710891
10. Henninge J, Pepaj M, Hullstein I, Hemmersbach P. (2010). Identification of CJC-1295, a growth-hormone-releasing peptide, in an unknown pharmaceutical preparation. Drug Testing and Analysis, 2(11-12), 647–650. DOI: 10.1002/dta.233. PMID: 21204297
11. Thomas A, Schänzer W, Delahaut P, Thevis M. (2012). Immunoaffinity purification of peptide hormones prior to liquid chromatography-mass spectrometry in doping controls. Methods, 56(2), 230–235. DOI: 10.1016/j.ymeth.2011.08.009. PMID: 21871962
12. Thevis M, Thomas A, Schänzer W. (2014). Detecting peptidic drugs, drug candidates and analogs in sports doping: current status and future directions. Expert Review of Proteomics, 11(6), 663–673. DOI: 10.1586/14789450.2014.965159. PMID: 25382550
13. Thomas A, Walpurgis K, Tretzel L, et al. (2015). Expanded test method for peptides >2 kDa employing immunoaffinity purification and LC-HRMS/MS. Drug Testing and Analysis, 7(11-12), 990–998. DOI: 10.1002/dta.1868. PMID: 26382721
14. Knoop A, Thomas A, Fichant E, et al. (2016). Qualitative identification of growth hormone-releasing hormones in human plasma by means of immunoaffinity purification and LC-HRMS/MS. Analytical and Bioanalytical Chemistry, 408(12), 3145–3153. DOI: 10.1007/s00216-016-9377-3. PMID: 26879649
15. Kwok WH, Ho EN, Lau MY, et al. (2013). Doping control analysis of seven bioactive peptides in horse plasma by liquid chromatography-mass spectrometry. Analytical and Bioanalytical Chemistry, 405(8), 2595–2606. DOI: 10.1007/s00216-012-6697-9. PMID: 23318763
16. Mayo KE. (1992). Molecular cloning and expression of a pituitary-specific receptor for growth hormone-releasing hormone. Molecular Endocrinology, 6(10), 1734–1744. DOI: 10.1210/mend.6.10.1333056. PMID: 1333056
17. Mayo KE, Miller T, DeAlmeida V, et al. (2000). Regulation of the pituitary somatotroph cell by GHRH and its receptor. Recent Progress in Hormone Research, 55, 237–266. PMID: 11036940
18. Tang SS, Du MH, Zhang XW, et al. (2006). Study on the constructions and activities of three novel hGHRH analogs with N-terminal prolyl modulation. Regulatory Peptides, 133(1-3), 20–26. DOI: 10.1016/j.regpep.2005.09.014. PMID: 16260050
19. Tang SS, Du MH, Zhang JH, et al. (2010). Structure and function relationships of three novel hGHRH-GGC analogs. Regulatory Peptides, 159(1-3), 87–92. DOI: 10.1016/j.regpep.2009.09.010. PMID: 19818814
20. Farhy LS, Bowers CY, Veldhuis JD. (2007). Model-projected mechanistic bases for sex differences in growth hormone regulation in humans. American Journal of Physiology — Regulatory, Integrative and Comparative Physiology, 292(4), R1577–R1593. DOI: 10.1152/ajpregu.00584.2006. PMID: 17185408
21. Laferrère B, Abraham C, Russell CD, Bowers CY. (2005). Growth hormone releasing peptide-2 (GHRP-2), like ghrelin, increases food intake in healthy men. Journal of Clinical Endocrinology & Metabolism, 90(2), 611–614. DOI: 10.1210/jc.2004-1719. PMID: 15699539
22. Timms M, Ganio K, Forbes G, et al. (2019). An immuno polymerase chain reaction screen for the detection of CJC-1295 and other growth-hormone-releasing hormone analogs in equine plasma. Drug Testing and Analysis, 11(6), 804–812. DOI: 10.1002/dta.2554. PMID: 30489688
23. Timms M, Ganio K, Steel R. (2019). A method for confirming CJC-1295 abuse in equine plasma samples by LC-MS/MS. Drug Testing and Analysis, 11(8), 1248–1257. DOI: 10.1002/dta.2599. PMID: 30938069
24. Coppieters G, Deventer K, Polet M, et al. (2022). An antibody-free, ultrafiltration-based assay for the detection of growth hormone-releasing hormones in urine at low pg/mL concentrations using nanoLC-HRMS/MS. Journal of Pharmaceutical and Biomedical Analysis, 214, 114726. DOI: 10.1016/j.jpba.2022.114726. PMID: 35298973
25. World Anti-Doping Agency. (2026). The Prohibited List — Section S2: Peptide Hormones, Growth Factors, Related Substances and Mimetics. Available from https://www.wada-ama.org/en/prohibited-list
26. Youn YS, Lee KC. (2007). Site-specific PEGylation for high-yield preparation of Lys(21)-amine PEGylated growth hormone-releasing factor (GRF) (1-29). Bioconjugate Chemistry, 18(2), 500–506. DOI: 10.1021/bc060173z. PMID: 17243755
27. Pont L, Alechaga É, Terrero A, et al. (2020). Comparison of magnetic bead surface functionalities for the immunopurification of growth hormone-releasing hormones prior to liquid chromatography-high resolution mass spectrometry. Journal of Chromatography A, 1631, 461548. DOI: 10.1016/j.chroma.2020.461548. PMID: 32971474
28. Memdouh S, Gavrilović I, Ng K, Cowan D. (2021). Advances in the detection of growth hormone releasing hormone synthetic analogs. Drug Testing and Analysis, 13(11-12), 1871–1887. DOI: 10.1002/dta.3183. PMID: 34665524