In stockBestseller
- Batch verified
- Temperature controlled
- Discreet packaging
- Purity
- 99.3%
- Form
- Lyophilised powder
- Molecular weight
- 3647.2 g/mol
- Storage
- -20°C, desiccated, protected from light
- Batch
- B-2408-108
For research use only · Not for human consumption
About this compound
5.8–8.1 d
Estimated half-life in healthy adults
subcutaneous · ascending-dose Phase 1 trials · ages 21–61 (1)
2–10×
Rise in mean plasma GH, sustained 6 days or more
single injection · dose-dependent · healthy adults (1)
1.5–3×
Rise in mean plasma IGF-I, sustained 9–11 days
single injection · dose-dependent · healthy adults (1)
7.5×
Rise in trough GH with pulse frequency unaltered
60 or 90 µg/kg · healthy men 20–40 · P < 0.0001 (2)
CJC-1295 is a synthetic analogue of growth hormone-releasing hormone. Jetté and colleagues identified it in Endocrinology in 2005 as the best of three maleimido derivatives of human GRF(1-29) that they synthesised and bioconjugated to human serum albumin (3).
The compound they selected is a tetrasubstituted form of hGRF(1-29) with an added N-epsilon-3-maleimidopropionamide derivative of lysine at the C terminus. That added group is the drug affinity complex — the DAC in this listing's subtitle — and it exists for a single chemical reaction: bioconjugation to the free thiol on Cys34 of serum albumin, which those authors describe as a useful tool for extending plasma half-life (3).
What the peptide acts on is the receptor the native hormone acts on. The title of that paper is the finding: hGRF(1-29)-albumin bioconjugates activate the GRF receptor on the anterior pituitary in rats. The conjugates were also bioactive in a growth hormone secretion assay in cultured rat anterior pituitary cells, and showed enhanced in vitro stability against dipeptidylpeptidase-IV (3). The albumin group changes how long the peptide is in circulation; it does not change which receptor it reaches.
CJC-1295 remains investigational. It holds no marketing authorisation in any jurisdiction, its published human record is two studies in healthy volunteers from 2006, and every figure on this page describes what a study measured in its own rats or its own volunteers rather than a protocol for anyone to follow.
What the design had to solve
DPP-IV
The enzyme that takes the peptide apart
Frohman and colleagues characterised the plasma enzyme responsible for the primary cleavage of growth hormone-releasing hormone at the 2-3 amino acid bond. Native GRH and the COOH-terminally shortened fragments — GRH(1-29)-NH2 among them — were rapidly cleaved; conversion to the metabolite was blocked by a competitive inhibitor of dipeptidylpeptidase IV, and D-amino acid substitution at either position 1 or 2 also prevented hydrolysis (8). Knoop and colleagues list the CJC-1295 backbone with a D-alanine at exactly position 2 (4).
Cys34
The bond that ties the peptide to albumin
The maleimide group at the C terminus exists for one reaction: bioconjugation to the free thiol on Cys34 of serum albumin. Given subcutaneously to normal male Sprague Dawley rats, CJC-1295 produced a four-fold increase in growth hormone area under the curve over a two-hour period compared with unmodified hGRF(1-29), and was found to be present in plasma beyond 72 hours (3).
GHRH-R
The receptor at the end of it
The receptor for growth hormone-releasing hormone, on the anterior pituitary — the same one the native hormone uses, and a different receptor from the one Ipamorelin acts on. Jetté and colleagues demonstrated that activation in rats and in cultured rat anterior pituitary cells (3). Every pharmacokinetic figure on this page describes how long the peptide lasts on the way to that receptor, not how hard it presses on it.
With DAC and without DAC
Two different materials are sold under this one name, and the difference between them is not a detail of nomenclature. The subtitle on this listing states which one is catalogued here: the DAC form.
Everything above concerns the conjugate. Remove the drug affinity complex — the added lysine derivative at the C terminus — and there is no maleimide group, nothing to react with Cys34, and no albumin to carry the peptide. What remains is the 29-residue backbone, in effect modified GRF(1-29).
That the bare name is applied in print to that unconjugated backbone is not a vendor invention. Knoop and colleagues, developing an anti-doping assay for growth hormone-releasing hormones in human plasma, list CJC-1295 as a 29-residue, C-terminally amidated peptide differing from sermorelin at four positions — D-alanine at 2, glutamine at 8, alanine at 15 and leucine at 27 — with no C-terminal lysine and no maleimide group named anywhere in the paper (4). Henninge and colleagues, analysing an unknown pharmaceutical preparation submitted by Norwegian police and customs authorities in 2009, reported a 29 amino acid peptide with a C-terminal amide whose proposed sequence was consistent with a peptide then marketed under the name CJC-1295 (5).
The consequence is a difference in duration of roughly three orders of magnitude, and it can be read off the literature on the unmodified peptides. Su and colleagues incubated GRF analogues in porcine plasma at 37 °C and followed them by HPLC: GRF(1-29)-NH2 had a half-life of 13 minutes and [Ala15]GRF(1-29)-NH2 one of 17 minutes (6). In people, Frohman and colleagues measured the half-life of GRH(1-44)-NH2 at 6.8 minutes after intravenous injection in normal subjects, with the inactive cleavage product detectable within one minute (7). Against those figures, Teichman and colleagues estimated the half-life of the albumin conjugate at 5.8 to 8.1 days (1).
Those comparators are not perfect. Two of them are in vitro and in porcine plasma, one is a longer peptide given by a different route, and none of them was measured on a preparation labelled CJC-1295 without DAC — no peer-reviewed pharmacokinetic study of such a preparation was located for this page. What can be said is narrower and still decisive: every multi-day figure on this page belongs to the albumin conjugate, and a peptide with no group to conjugate does not inherit them.
What the human studies reported
There are two of them. Both appeared in the Journal of Clinical Endocrinology and Metabolism in 2006, both were conducted in healthy volunteers, and together they are the whole published human record located for this page.
Teichman and colleagues ran two randomised, placebo-controlled, double-blind ascending-dose trials, of 28 and 49 days, at two investigational sites, in healthy subjects aged 21 to 61. The compound was given subcutaneously — in one of four ascending single doses in the first study, and in two or three weekly or biweekly doses in the second. After a single injection there were dose-dependent increases in mean plasma growth hormone concentrations of 2- to 10-fold for six days or more, and in mean plasma IGF-I concentrations of 1.5- to 3-fold for nine to eleven days. After multiple doses, mean IGF-I remained above baseline for up to 28 days. The estimated half-life was 5.8 to 8.1 days. The authors reported the compound safe and relatively well tolerated, particularly at doses of 30 or 60 µg/kg, and recorded no serious adverse reactions (1). That abstract states no participant count, so none is given anywhere on this page.
Ionescu and Frohman asked a narrower question: whether stimulating the pituitary continuously flattens the natural rhythm of growth hormone release. They sampled blood every 20 minutes across an overnight 12-hour period in healthy men aged 20 to 40, before and one week after a single injection of either 60 or 90 µg/kg. Pulse frequency and magnitude were unaltered. Basal, trough growth hormone rose 7.5-fold (P < 0.0001), mean growth hormone by 46% (P < 0.01) and IGF-I by 45% (P < 0.001), and no significant differences were observed between the responses to the two doses (2).
The doses named above are trial design, reported because the results above cannot be read without them. They are not instructions, and Peptio publishes no protocol for use in people.
The published record
- Molecular class
- A tetrasubstituted form of hGRF(1-29) with an added N-epsilon-3-maleimidopropionamide derivative of lysine at the C terminus (3)
- What the added group binds
- The free thiol on Cys34 of serum albumin (3)
- Receptor
- The GRF receptor on the anterior pituitary, demonstrated in rats and in cultured rat anterior pituitary cells (3)
- Preclinical characterisation, 2005
- Normal male Sprague Dawley rats, subcutaneous. Four-fold increase in growth hormone area under the curve over a two-hour period against unmodified hGRF(1-29); present in plasma beyond 72 hours; enhanced in vitro stability against dipeptidylpeptidase-IV (3)
- Ascending-dose trials in healthy adults, 2006
- Two randomised, placebo-controlled, double-blind trials of 28 and 49 days at two investigational sites, ages 21–61, subcutaneous. Mean plasma GH 2- to 10-fold for 6 days or more; mean plasma IGF-I 1.5- to 3-fold for 9–11 days; IGF-I above baseline for up to 28 days after multiple doses; estimated half-life 5.8–8.1 days (1)
- Pulsatility study, 2006
- Healthy men aged 20–40, 20-minute sampling across an overnight 12-hour period before and one week after a single 60 or 90 µg/kg dose. Trough GH 7.5-fold, mean GH 46%, IGF-I 45%; pulse frequency and magnitude unaltered (2)
- Tolerability as reported
- Safe and relatively well tolerated, particularly at 30 or 60 µg/kg, with no serious adverse reactions — in one programme of healthy volunteers over 28 and 49 days (1)
- The unconjugated backbone
- 29 residues, C-terminally amidated, differing from sermorelin at positions 2, 8, 15 and 27, with no C-terminal lysine (4). For unmodified peptides of that length, half-lives of 13 and 17 minutes in porcine plasma at 37 °C, in vitro (6)
- Phase 2 or later
- None published. No trial beyond the two 2006 studies was located for this page
- WADA Prohibited List 2026
- Section S2.2.4, named among GHRH analogues; prohibited at all times, in and out of competition (12)
- Marketing authorisation
- None, in any jurisdiction
Against the other muscle-growth peptide in this catalogue
CJC-1295 and Ipamorelin both make the anterior pituitary release growth hormone, and they reach it through different receptors and on very different timescales. No trial has compared them. The rows below are therefore qualitative: there is no shared endpoint on which a figure for one could fairly be set against a figure for the other, and no row reports an effect on muscle — no published trial measured one for either compound. The two half-life figures come from separate studies in healthy adults using different routes, and sit side by side for orientation only.
| Parameter | CJC-1295 | Ipamorelin |
|---|---|---|
| Molecular class | Analogue of growth hormone-releasing hormone: tetrasubstituted hGRF(1-29) carrying a drug affinity complex at the C terminus (3) | Synthetic pentapeptide, Aib-His-D-2-Nal-D-Phe-Lys-NH2 (9) |
| Receptor | Growth hormone-releasing hormone receptor, on the anterior pituitary (3) | The growth hormone secretagogue receptor — established as a GHRP-like receptor rather than the GHRH receptor (9), and named in the later trial literature as the ghrelin receptor (11) |
| Half-life reported in healthy adults | 5.8 to 8.1 days after subcutaneous dosing (1) | About 2 hours, terminal, after a 15-minute intravenous infusion (10) |
| Route in the cited human studies | Subcutaneous (1, 2) | Intravenous (10, 11) |
| Stage the published human evidence reached | Two randomised, placebo-controlled, double-blind ascending-dose trials in healthy adults, 28 and 49 days, and one pharmacodynamic study of growth hormone pulsatility. Nothing beyond (1, 2) | Phase 2 in postoperative ileus. The proof-of-concept trial reported no significant differences from placebo in the key and secondary efficacy analyses (11) |
| Selectivity finding cited here | None cited on this page | Growth hormone released with no rise in ACTH or cortisol, in conscious swine, at doses more than 200-fold above its ED50 for growth hormone release (9) |
| WADA Prohibited List 2026 | Section S2.2.4, named among GHRH analogues; prohibited at all times (12) | Section S2.2.4, named among growth hormone secretagogues; prohibited at all times (12) |
| Marketing authorisation | None in any jurisdiction | None in any jurisdiction |
Sources. (1) Teichman SL, Neale A, Lawrence B, et al. 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. (2) 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. (3) 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. (4) Knoop A, Thomas A, Fichant E, 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. (5) 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. (6) Su CM, Jensen LR, Heimer EP, et al. In vitro stability of growth hormone releasing factor (GRF) analogs in porcine plasma. Horm Metab Res. 1991;23(1):15–21. (7) Frohman LA, Downs TR, Williams TC, 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. (8) Frohman LA, Downs TR, Heimer EP, Felix AM. Dipeptidylpeptidase IV and trypsin-like enzymatic degradation of human growth hormone-releasing hormone in plasma. J Clin Invest. 1989;83(5):1533–1540. (9) Raun K, Hansen BS, Johansen NL, et al. Ipamorelin, the first selective growth hormone secretagogue. Eur J Endocrinol. 1998;139(5):552–561. (10) Gobburu JV, Agersø H, Jusko WJ, Ynddal L. Pharmacokinetic-pharmacodynamic modeling of ipamorelin, a growth hormone releasing peptide, in human volunteers. Pharm Res. 1999;16(9):1412–1416. (11) Beck DE, Sweeney WB, McCarter MD; Ipamorelin 201 Study Group. Prospective, randomized, controlled, proof-of-concept study of the Ghrelin mimetic ipamorelin for the management of postoperative ileus in bowel resection patients. Int J Colorectal Dis. 2014;29(12):1527–1534. (12) World Anti-Doping Agency. World Anti-Doping Code International Standard: Prohibited List 2026, in effect 1 January 2026, section S2.2.4. CJC-1295 is investigational and holds no marketing authorisation in any jurisdiction.
What the published work does not show
- No published human trial of muscle mass, strength or body composition was found for this page. The two human studies located measured plasma growth hormone and IGF-I concentrations, pharmacokinetic parameters and growth hormone pulsatility, and nothing else (1, 2).
- The published human record stops at ascending-dose studies in healthy volunteers. No Phase 2 or later trial of CJC-1295 was located, and the two 2006 papers remain the most recent human data cited here (1, 2).
- Neither 2006 abstract states how many people took part, so no participant count appears anywhere on this page.
- The four-fold growth hormone response and the presence in plasma beyond 72 hours were measured in normal male Sprague Dawley rats given the compound subcutaneously, not in people (3).
- The minute-scale half-lives quoted for unmodified peptides were measured in vitro in porcine plasma at 37 °C (6), or, for a longer GHRH peptide, after intravenous injection in normal subjects (7). No peer-reviewed pharmacokinetic study of a preparation sold as CJC-1295 without DAC was located for this page, so no half-life is published here for that material.
- No study cited on this page measured CJC-1295 and Ipamorelin in the same experiment. The comparison above is qualitative for that reason, and no figure for one is set against a figure for the other.
- CJC-1295 and Ipamorelin are both named on the 2026 WADA Prohibited List, in section S2.2.4, and are prohibited at all times, in and out of competition (12).
What Peptio ships
A sealed vial of lyophilised powder, in a 5 mg or a 10 mg size. Both are the same material; the difference is the mass in the vial, not the concentration — concentration is set later, by how much solvent is added.
Each batch is released against a certificate of analysis from an independent issuer, and the batch number printed on the vial matches the number on that certificate. Checking those two against each other is the most useful thing to do with a delivery. The purity, form, storage condition and molecular weight recorded for the current batch are in the specifications above.
Handling is the same as for every other compound in the catalogue. The handling protocol below covers storage temperatures, solvent choice and the concentration calculation.
Research use only
CJC-1295 is an investigational compound with no marketing authorisation in any jurisdiction. Peptio is not a pharmacy and supplies it for research use only — not for human or veterinary consumption. Everything reported on this page comes from published studies and describes their rats or their volunteers; none of it is guidance for use in people, and this page publishes no dose recommendation, protocol or schedule.
Handling and storage
Every compound Peptio ships arrives as a sealed vial of lyophilised powder. Freeze-drying is what keeps it stable in transit: with the water removed and the vial closed, the peptide keeps far longer than it would in solution. The protocol below applies to all of them, and it is the same protocol whichever compound is in the vial.
The steps that matter most happen in the first few minutes after a vial is opened, and in how the prepared solution is labelled afterwards. A vial with no recorded solvent volume is a vial with no known concentration, and no amount of care later recovers that.
From delivery to prepared solution
01
Inspect on arrival
Check that the crimp seal and stopper are intact and that the powder cake is dry and unbroken. Compare the batch number printed on the vial with the number on the certificate of analysis. A cake that has slumped into a film, or a vial that arrives loose in its packaging, is worth photographing before anything else is done to it.
02
Equilibrate before opening
Let a vial taken from cold storage stand sealed until it reaches room temperature. Opening cold glass in a warm room pulls condensation onto it, and moisture is the one thing a desiccated powder is being protected from.
03
Add the solvent
Direct the solvent slowly down the inner wall of the vial rather than onto the cake, then let it dissolve on its own and swirl gently until the solution runs clear. This takes a minute or two, and it is not helped by shaking.
04
Label, then refrigerate
Write the date, the solvent and the exact volume added onto the vial before it goes anywhere. Keep the prepared solution cold and out of direct light, and check that it is still clear each time it is used.
Quick reference
- Form
- Lyophilised powder in a sealed, stoppered vial
- Solvent
- Bacteriostatic water where the vial will be drawn from more than once; sterile water where it will not
- Typical reconstitution volume
- 1–3 mL, chosen to give the concentration the work calls for
- Storage before reconstitution
- −20 °C, desiccated and protected from light
- Storage after reconstitution
- 2–8 °C, protected from light, in the original stoppered vial
- In transit
- Short periods at 2–8 °C are expected; that is what the insulated mailer is for
- Once opened
- Record the date on the vial. How long a prepared solution stays usable depends on the solvent and the storage temperature, so the date is the only reliable reference point.
Handling
| Correct | Common mistake |
|---|---|
| Direct the solvent down the inner wall of the vial and let the cake dissolve on its own. | Drive the solvent onto the powder in a fast stream. |
| Swirl gently until the solution runs clear. | Shake or vortex the vial — mechanical agitation and foaming degrade peptide structure. |
| Let a vial from cold storage reach room temperature while it is still sealed. | Open a vial straight out of the freezer, and pull condensation into a product that is kept dry on purpose. |
| Label every prepared vial with the date, the solvent and the volume added. | Rely on memory — two vials that look identical at 2–8 °C can hold two different concentrations. |
| Draw through the stopper with a fresh sterile needle each time. | Prise off the crimp seal; an open vial cannot be kept sterile. |
| Keep prepared solution cold and shielded from light between uses. | Leave a reconstituted vial standing at room temperature on the bench. |
| Look at the solution before every use and confirm it is clear. | Use a solution that has turned cloudy or thrown a visible particle. |
Solvent volume sets the concentration
The mass of peptide in a vial is fixed at manufacture. The only variable is how much solvent goes in, and it changes every measurement that follows — 2 mL instead of 1 mL halves the concentration. Confirm the vial's usable capacity before adding anything, since a 2 mL vial will not take 3 mL, and write down the volume you actually added.
Working out the concentration
- Concentration (mg/mL) = peptide mass in the vial (mg) ÷ solvent volume added (mL).
- A 5 mg vial with 1 mL of solvent gives 5 mg/mL. The same vial with 2 mL gives 2.5 mg/mL.
- A 10 mg vial with 2 mL of solvent also gives 5 mg/mL — the same concentration from twice the mass.
- Volume (mL) = mass required (mg) ÷ concentration (mg/mL).
- 1 mg/mL is 1,000 micrograms per mL. Convert once, at the start, and hold one unit for the whole calculation.
Questions
About CJC-1295
Delivery
- One delivery option at checkout: standard, 3–5 working days.
- Orders ship in an insulated mailer.
- Delivery is free on orders over €150.00.
- See the Shipping page for the delivery terms in full.
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