CJC-1295 DAC 5mg Peptide

CJC-1295 DAC is a synthetic peptide analog of growth hormone-releasing hormone (GHRH) designed to enhance the release of growth hormone (GH) in research settings. It is characterized by the inclusion of a Drug Affinity Complex (DAC), which significantly extends its half-life, allowing for sustained GH release over an extended period. This modification is particularly advantageous in research focused on long-term modulation of the GH axis.

The peptide's design aims to mimic the natural pulsatile release of GH, which is crucial for its physiological effects. CJC-1295 DAC has been the subject of various studies exploring its potential applications in understanding growth hormone dynamics, muscle growth, and metabolic processes. However, it is important to note that CJC-1295 DAC is strictly for research purposes and not approved for human consumption.

CJC-1295 with DAC is a modified growth hormone releasing hormone analogue built on the GHRH(1-29) backbone, carrying four amino acid substitutions and, critically, a maleimidopropionyl group known as the Drug Affinity Complex. The four substitutions protect the peptide from enzymatic degradation, beginning with D-alanine at position 2, which blocks the dipeptidyl peptidase-4 cleavage that makes unmodified sermorelin short-acting.

The DAC moiety is what distinguishes this molecule from every other GHRH analogue. It is a reactive maleimide that forms a covalent bond with a free cysteine thiol on circulating albumin after administration. That bond is covalent rather than the reversible non-covalent binding used by acylated incretin analogues, which is why the resulting half-life is measured in days rather than hours and why the molecule produces a sustained elevation rather than a pulse.

At the receptor the molecule is a GHRH receptor agonist acting on pituitary somatotrophs through Gs and cyclic AMP. The pharmacologically important consequence of the DAC is not potency but exposure pattern: rather than a brief pulse of receptor activation, the somatotroph experiences continuous stimulation, which raises the question of receptor desensitisation and of whether sustained GHRH receptor activation reproduces the physiological pulsatile pattern or replaces it.

CJC-1295 DAC functions by binding to the growth hormone-releasing hormone receptor (GHRHR) on the pituitary gland, stimulating the release of growth hormone. The inclusion of the Drug Affinity Complex (DAC) in its structure allows for a prolonged half-life, which can exceed one week, as demonstrated in animal models. This extended half-life is achieved by reversible binding to serum albumin, which protects the peptide from rapid degradation.

Research indicates that this mechanism allows for a more sustained and physiologically relevant pattern of GH release, which is beneficial for studies aiming to replicate natural growth hormone secretion patterns. The ability to maintain elevated GH levels over extended periods without frequent dosing presents a significant advantage in experimental settings.

Studies have shown that CJC-1295 DAC exhibits a significantly longer half-life compared to traditional GHRH analogs due to its DAC modification. In rodent models, the half-life of CJC-1295 DAC has been reported to be approximately 8 days, which is substantially longer than that of non-DAC modified peptides. This prolonged duration of action is attributed to its ability to bind to albumin, reducing renal clearance and proteolytic degradation.

The stability of CJC-1295 DAC in biological systems makes it a valuable tool for research into sustained growth hormone release and its effects on various physiological processes. This stability ensures that the peptide remains active over the course of the study, providing consistent results.

CJC-1295 DAC has been extensively studied for its ability to modulate growth hormone release in research models. Studies in rodents have demonstrated that administration of CJC-1295 DAC leads to a significant increase in circulating levels of GH and insulin-like growth factor 1 (IGF-1), which are critical mediators of growth and metabolism.

The peptide's ability to sustain elevated GH levels without the need for frequent administration makes it a promising candidate for studies investigating the long-term effects of GH on muscle growth, fat metabolism, and overall metabolic health. However, these findings are limited to preclinical models, and further research is needed to fully understand its potential applications.

The unique properties of CJC-1295 DAC make it a valuable tool for a variety of research applications. Its ability to promote sustained GH release has been utilized in studies exploring muscle hypertrophy, recovery, and metabolic regulation. In particular, research in animal models has shown potential benefits in enhancing muscle mass and reducing adiposity.

Additionally, CJC-1295 DAC is being investigated for its role in studying age-related changes in GH secretion and its impact on age-associated diseases. The peptide's long-acting nature provides a model for understanding the chronic effects of GH modulation, which could inform future research directions in endocrinology and metabolism.

CJC-1295 with DAC and CJC-1295 without DAC are routinely sold under the same name with a suffix, which understates how different they are. The peptide backbone is the same tetrasubstituted GHRH(1-29) sequence. The DAC version additionally carries a maleimidopropionyl group that reacts covalently with albumin after administration.

The consequence is not incremental. Reported half-lives differ by roughly two orders of magnitude: minutes to about half an hour for the version without DAC, six to eight days for the version with it. A difference of that scale changes the pharmacology qualitatively, not just its duration.

The covalent chemistry also differs from the acylation used by semaglutide and tirzepatide. Those bind albumin reversibly through a fatty acid, so free drug is continuously released and re-bound. A maleimide-thiol bond does not dissociate, so the conjugate persists for the lifetime of the albumin molecule it attached to.

Endogenous growth hormone secretion is episodic, with pulses separated by troughs, and the trough periods appear to matter for downstream receptor signalling rather than being merely the gaps between pulses.

A GHRH analogue with a multi-day half-life produces continuous receptor stimulation instead. Whether that reproduces the physiological effect of growth hormone or produces something pharmacologically different is a real and unresolved question, and it is the principal theoretical objection raised against this construct relative to short-acting analogues.

The human study reported sustained elevation of growth hormone and IGF-1, which establishes that the exposure pattern is achieved. It does not establish that sustained exposure is preferable to pulsatile exposure for any outcome.

The human evidence consists principally of early-phase pharmacokinetic and pharmacodynamic work in healthy adults demonstrating sustained growth hormone and IGF-1 elevation. There are no adequately powered efficacy trials for any clinical outcome.

The compound has no marketing authorisation in any jurisdiction and appears on prohibited lists in competitive sport. Material supplied for research is for in-vitro laboratory use only and is not a medicine.

The maleimide group is chemically reactive by design, which has practical consequences. It reacts with free thiols, so any reducing agent or thiol-containing buffer component will consume it, converting the molecule to a form that can no longer conjugate to albumin.

This makes buffer composition a matter of identity rather than only stability for this compound. It also means that a certificate reporting the mass of the unconjugated peptide is describing the material as supplied, which is the correct thing to report, but the reactive group's integrity is not something a mass alone confirms.