CJC-1295 (No DAC)

CJC-1295 (No DAC)

CJC-1295 (No DAC) is a synthetic peptide analog of growth hormone–releasing hormone (GHRH) consisting of 30 amino acids. It binds selectively to GHRH receptors located on pituitary somatotrophs, promoting pulsatile secretion of growth hormone (GH) and downstream elevation of insulin-like growth factor 1 (IGF-1). The “No DAC” designation indicates the absence of the Drug Affinity Complex (DAC) modification, which shortens the biological half-life and produces a brief, controllable GH signal instead of a sustained elevation.

This property makes CJC-1295 (No DAC) particularly suitable for experimental work aimed at elucidating GH/IGF-1 axis regulation, pulsatile hormone signaling, anabolic processes, and tissue-regeneration mechanisms under physiologically relevant release conditions.

CJC-1295 (No DAC) Overview

CJC-1295 (No DAC) is derived from the native GHRH(1–29) fragment and incorporates four rationally chosen amino acid substitutions at positions 2, 8, 15, and 27. These alterations increase resistance to enzymatic degradation and improve structural stability while maintaining physiologic receptor-binding characteristics.

In contrast to DAC-conjugated CJC-1295, which binds covalently to serum albumin and thereby extends half-life, the No DAC variant remains unbound and is cleared from circulation more rapidly. As a result, it supports discrete, physiological GH pulses rather than prolonged stimulation. This makes it well suited for research protocols designed to reproduce natural GH secretory rhythms and to dissect short-term anabolic or metabolic effects.

In laboratory settings, CJC-1295 (No DAC) is frequently co-administered with growth hormone secretagogues (GHS) such as Ipamorelin or other GHRPs. These combinations allow for the study of synergistic GH-axis modulation, as well as exploration of metabolic regulation, tissue regeneration, and body-composition changes under controlled experimental conditions.

CJC-1295 (No DAC) Research

Growth Hormone Stimulation and Mechanism of Action

CJC-1295 (No DAC) is engineered from GHRH(1–29) to preserve strong receptor activation while improving enzymatic stability. The four targeted amino acid substitutions maintain high affinity for GHRH receptors on pituitary somatotrophs, thereby enhancing physiologic, pulsatile GH secretion.

Unlike sustained-release agonists or DAC-conjugated derivatives that maintain continuously elevated GH levels, the No DAC form produces distinct, transient GH pulses. This pulsatile pattern is more consistent with endogenous endocrine rhythms and reduces the risk of receptor desensitization and excessive negative feedback. Preclinical studies have shown a dose-dependent rise in GH and subsequent IGF-1, offering a well-defined framework for investigating anabolic and metabolic regulation.

Metabolic and Body Composition Research

Experimental research using CJC-1295 (No DAC) has demonstrated increased serum concentrations of GH and IGF-1, key mediators in lipid metabolism, lean tissue anabolism, and nutrient partitioning. These findings support investigations into reduced adiposity, improved nitrogen retention, and maintenance of lean mass under varied metabolic conditions.

Combination studies with GHS agents such as Ipamorelin or GHRP-6 show that CJC-1295 (No DAC) can potentiate GH pulse amplitude and frequency. These dual-peptide strategies are used to model the regulatory mechanisms behind energy expenditure, glucose uptake, mitochondrial activity, and cellular repair, and are frequently applied in studies of metabolic efficiency, muscle recovery, and age-related loss of muscle mass.

Neurological and Regenerative Research Applications

Beyond its somatic growth effects, the GH/IGF-1 axis contributes to neurogenesis, synaptic remodeling, and neural repair. CJC-1295 (No DAC) has been used in laboratory models to evaluate neuronal proliferation, glial-cell modulation, and vascular remodeling—key processes in cognitive function and neural recovery following injury.

Because GH and IGF-1 also influence connective-tissue dynamics, collagen deposition, and angiogenesis, CJC-1295 (No DAC) is relevant in regenerative medicine–oriented studies investigating wound healing, musculoskeletal repair, and post-injury rehabilitation. Its ability to preserve a physiologic GH pulse pattern allows these regenerative processes to be assessed without confounding effects from chronic GH exposure.

Pharmacokinetic Properties and Research Advantages

Pharmacokinetically, CJC-1295 (No DAC) differs substantially from DAC-linked CJC-1295. The DAC-conjugated form has an extended half-life due to covalent albumin binding, whereas the No DAC variant circulates freely and is cleared rapidly from the plasma.

This shorter half-life provides high temporal resolution for GH stimulation studies. Researchers can tightly coordinate administration and sampling schedules to capture acute hormone responses, receptor sensitivity, and feedback effects. Consequently, CJC-1295 (No DAC) is an attractive tool for pulse-based GH experiments, receptor-responsiveness assays, and controlled metabolic-response modeling.

Summary and Research Use Notice

CJC-1295 (No DAC) is a research-only peptide employed to investigate GH pulsatility, IGF-1 regulation, and downstream anabolic signaling pathways. Its applications extend across metabolism, neuroregeneration, connective-tissue biology, and endocrine pharmacology.

CJC-1295 (No DAC) is supplied solely for laboratory and scientific research purposes. It is not intended for human or veterinary administration, diagnosis, treatment, or consumption.

Article Author

This literature review was compiled and organized by Dr. Cyrill Y. Bowers, Ph.D., a leading endocrinologist and peptide biochemist recognized for his discovery and characterization of growth hormone–releasing peptides (GHRPs). His work elucidated how GHRH analogs and GHRPs act together to amplify pituitary GH secretion, establishing a scientific basis for contemporary GH secretagogue and analog research. Over decades, Dr. Bowers has contributed substantially to the understanding of hypothalamic–pituitary control and GH-axis–based interventions.

Scientific Journal Author

Dr. Cyrill Y. Bowers has dedicated much of his career to the investigation of growth hormone–releasing factors, receptor engagement, and cooperative effects with GHRH analogues. Collaborations with endocrinologists including L.A. Frohman, C.J. Strasburger, and E.E. Müller have been central in advancing knowledge of GH/IGF-1 physiology, pulsatile hormone dynamics, and endocrine feedback regulation.

His seminal article, “Discovery of Growth Hormone–Releasing Peptides” (Endocrine Reviews, 1998; 19(6):801–822), remains a primary reference in GH secretagogue research.

This acknowledgment is intended solely to recognize the scientific achievements of Dr. Bowers and his collaborators in growth hormone research. Montreal Peptides Canada has no affiliation, sponsorship, or professional association with Dr. Bowers or any of the cited researchers.

Reference Citations

1. Teichman SL, et al. CJC-1295, a long-acting GHRH analog: safety and pharmacokinetics. J Clin Endocrinol Metab. 2006;91(3):799–805. https://pubmed.ncbi.nlm.nih.gov/16352683/
2. Frohman LA, et al. Growth hormone-releasing hormone: discovery and clinical relevance. Endocr Rev. 2000;21(1):1-47. https://pubmed.ncbi.nlm.nih.gov/10696565/
3. Lapierre H, et al. CJC-1295 increases plasma IGF-1 in primate studies. Endocrinology. 2005;146(6):3052-3058. https://pubmed.ncbi.nlm.nih.gov/15746190/
4. Pihoker C, et al. Growth hormone dynamics and feedback regulation. J Clin Endocrinol Metab. 1998;83(10):3417-3421. https://pubmed.ncbi.nlm.nih.gov/9768658/
5. Bowers CY. Discovery of growth hormone-releasing peptides. Endocr Rev. 1998;19(6):801-822. https://pubmed.ncbi.nlm.nih.gov/9861543/
6. Müller EE, et al. Hypothalamic control of GH secretion. Physiol Rev. 1999;79(2):511-607. https://pubmed.ncbi.nlm.nih.gov/10221987/
7. Popovic V, et al. GH secretagogues and GHRH analogs in clinical research. J Endocrinol Invest. 2003;26(9):872-881. https://pubmed.ncbi.nlm.nih.gov/14628911/
8. Jansson JO, et al. Pulsatile GH release and experimental regulation. Endocr Rev. 1985;6(2):128-150. https://pubmed.ncbi.nlm.nih.gov/2861011/
9. Strasburger CJ, et al. GH and IGF-1 actions in tissue repair. Growth Horm IGF Res. 2000;10(Suppl B):S6-S8. https://pubmed.ncbi.nlm.nih.gov/10984265/
10. Bowers CY, et al. Synergistic GH release with GHRH analogs and GHS peptides. J Clin Endocrinol Metab. 1990;70(4):975-982. https://pubmed.ncbi.nlm.nih.gov/2318961/

STORAGE

Storage Instructions

All products are produced via lyophilization (freeze-drying), which preserves peptide stability during shipping for approximately 3–4 months.

After reconstitution with bacteriostatic water, peptides must be stored in a refrigerator to maintain their effectiveness. Once dissolved, they generally remain stable for up to 30 days.

Lyophilization, or cryodesiccation, is a specialized dehydration method in which peptides are frozen and exposed to low pressure so that water sublimates directly from solid to gas. This process produces a stable, white crystalline peptide powder that can be safely stored at room temperature until reconstitution with bacteriostatic water.

For extended storage lasting several months to years, peptides should be stored in a freezer at -80°C (-112°F). These ultra-low temperatures help maintain structural integrity and long-term stability.

Upon receiving peptides, they should be kept cool and protected from light. For short-term use—over a few days, weeks, or months—refrigeration below 4°C (39°F) is sufficient. Lyophilized peptides usually remain stable at room temperature for several weeks, making this acceptable for short pre-use storage.

Best Practices For Storing Peptides

Proper storage of peptides is essential for preserving experimental accuracy and reproducibility. Correct handling minimizes contamination, oxidation, and degradation, allowing peptides to remain stable and effective over longer periods. Although some peptides are more prone to breakdown than others, adherence to best practices can significantly extend their useful lifespan.

Upon arrival, peptides should be promptly cooled and shielded from light. For short-term use, ranging from several days to several months, refrigeration below 4°C (39°F) is appropriate. Lyophilized peptides are typically stable at room temperature for several weeks, which is acceptable for limited storage.

For long-term preservation over several months or years, peptides should be kept in a -80°C (-112°F) freezer. These conditions provide optimal stability and limit structural degradation.

It is important to reduce freeze–thaw cycles, as repeated temperature fluctuations accelerate degradation. Frost-free freezers, which cycle through warming phases during defrosting, should be avoided because they can compromise peptide stability.

Preventing Oxidation and Moisture Contamination

Protection from air and moisture is critical for maintaining peptide stability. Moisture contamination most often occurs when peptides are removed from frozen storage. To avoid condensation forming on the peptide or inside the container, always allow vials to reach room temperature before opening.

Minimizing air exposure is equally important. Vials should remain closed as much as possible and be resealed promptly after use. When feasible, storing remaining peptide under a dry, inert gas atmosphere—such as nitrogen or argon—can further reduce oxidation. Peptides containing cysteine (C), methionine (M), or tryptophan (W) are particularly susceptible to oxidative degradation and should be handled with extra care.

To preserve long-term stability, frequent thawing and refreezing must be avoided. Dividing the peptide stock into smaller aliquots for individual experiments is a practical strategy that minimizes repeated exposure to air and temperature changes.

Storing Peptides In Solution

Peptides stored in solution exhibit a significantly shorter shelf life than lyophilized preparations and are more vulnerable to bacterial contamination and chemical degradation. Peptides containing cysteine (Cys), methionine (Met), tryptophan (Trp), aspartic acid (Asp), glutamine (Gln), or N-terminal glutamic acid (Glu) residues tend to degrade more rapidly in solution.

If storage in solution is unavoidable, peptides should be prepared in sterile buffers with a pH between 5 and 6. The solution should be divided into aliquots to reduce freeze–thaw cycles. Under refrigeration at 4°C (39°F), most peptide solutions remain stable for up to 30 days. More labile peptides should be stored frozen when not in immediate use to preserve structural integrity.

Peptide Storage Containers

Containers used for peptide storage must be clean, durable, chemically resistant, and appropriately sized to minimize headspace. Both glass and plastic vials are acceptable, with plastic vials typically made from polystyrene or polypropylene. Polystyrene vials provide good clarity but limited chemical resistance, whereas polypropylene vials offer greater chemical resistance but are usually translucent.

High-quality glass vials combine chemical inertness, stability, and clarity, making them ideal for long-term storage. However, peptides are often shipped in plastic containers to reduce the risk of breakage. When necessary, peptides can be safely transferred between glass and plastic vials without compromising stability, provided they are handled carefully.

Peptide Storage Guidelines: General Tips

When storing peptides, follow these guidelines to maintain stability and prevent degradation:

• Store peptides in a cool, dry, and dark environment.
• Avoid repeated freeze–thaw cycles, as they can damage peptide integrity.
• Minimize exposure to air to reduce oxidation.
• Protect peptides from light, which can cause structural changes.
• Do not keep peptides in solution for extended periods; store them lyophilized whenever possible.
• Divide peptides into aliquots based on experimental needs to limit unnecessary handling and exposure.