CJC-1295 (No DAC)

CJC-1295 (No DAC)

CJC-1295 (No DAC) is a synthetic peptide analog of growth hormone–releasing hormone (GHRH) containing 30 amino acids. It connects specifically to GHRH receptors on pituitary somatotrophs, promoting pulsatile release of growth hormone (GH) and subsequent production of insulin-like growth factor 1 (IGF-1). The "No DAC" designation shows that this variant lacks the Drug Affinity Complex (DAC) modification, resulting in a shorter biological half-life and enabling controlled, transient GH stimulation rather than prolonged elevation.

This profile makes CJC-1295 (No DAC) suitable for experimental use in studies investigating GH/IGF-1 axis regulation, pulsatile endocrine signaling, anabolic metabolism, and tissue regeneration under physiologically relevant hormone-release conditions.

CJC-1295 (No DAC) Overview

CJC-1295 (No DAC) is a synthetic analog created from the native growth hormone–releasing hormone fragment GHRH(1–29), featuring four strategic amino acid substitutions (at positions 2, 8, 15, and 27) to enhance structural stability and resistance to enzymatic degradation. This modification improves peptide bioactivity while maintaining physiologic receptor affinity.

Unlike the DAC-conjugated form, CJC-1295 (No DAC) lacks a Drug Affinity Complex linkage, resulting in a comparatively shorter plasma half-life that supports natural, pulsatile secretion patterns of growth hormone (GH). This property makes it particularly valuable for experimental designs seeking to replicate physiologic GH release cycles and evaluate transient anabolic or metabolic responses.

CJC-1295 (No DAC) is frequently co-administered in research with growth hormone secretagogues (GHS) such as Ipamorelin or other growth hormone–releasing peptides (GHRPs), allowing investigators to explore synergistic effects on GH axis modulation, metabolism, tissue regeneration, and body composition under controlled laboratory conditions.

CJC-1295 (No DAC) Research

Growth Hormone Stimulation and Mechanism of Action

CJC-1295 (No DAC) is a synthetic analog of growth hormone–releasing hormone (GHRH 1-29) constructed to preserve potent receptor activity while exhibiting improved resistance to enzymatic degradation. Through four targeted amino acid substitutions, the peptide maintains high receptor affinity for GHRH receptors expressed on pituitary somatotrophs, thereby stimulating the pulsatile secretion of growth hormone (GH).

Unlike sustained agonists or DAC-conjugated derivatives that extend GH elevation over prolonged periods, the No DAC variant produces discrete, physiologically relevant GH pulses. This pattern aligns closely with natural endocrine rhythms, avoiding the receptor desensitization and negative feedback that can accompany continuous GH stimulation. Preclinical findings have demonstrated a clear dose-dependent increase in GH and subsequent IGF-1 release, providing a controlled framework for investigating anabolic and metabolic regulation.

Metabolic and Body Composition Research

Experimental studies involving CJC-1295 (No DAC) have shown notable increases in serum GH and IGF-1 concentrations, which are central mediators of lipid metabolism, lean tissue growth, and nutrient partitioning. These effects contribute to research exploring reductions in adiposity, improvements in nitrogen retention, and maintenance of lean body mass.

Combination studies using CJC-1295 (No DAC) with growth hormone secretagogues (GHS) such as Ipamorelin or GHRP-6 demonstrate synergistic potentiation of GH pulse amplitude and frequency. This synergy allows researchers to model physiological and pharmacological mechanisms governing energy expenditure, glucose utilization, mitochondrial activity, and cellular repair. Such dual-peptide protocols are frequently utilized in studies of metabolic efficiency, muscle recovery, and age-related sarcopenia models.

Neurological and Regenerative Research Applications

The GH/IGF-1 signaling axis extends beyond somatic growth, influencing neurogenesis, synaptic plasticity, and neural repair. Laboratory models employing CJC-1295 (No DAC) have been used to study neuronal proliferation, glial modulation, and vascular remodeling, processes critical to cognitive function and neural tissue recovery following injury.

Furthermore, GH and IGF-1 pathways are implicated in connective-tissue remodeling, collagen synthesis, and angiogenesis—making this peptide valuable in regenerative-medicine frameworks investigating wound healing, musculoskeletal regeneration, and post-injury recovery. By preserving a physiologic pattern of GH stimulation, CJC-1295 (No DAC) provides a controlled environment to evaluate these tissue-repair processes without the confounding effects of prolonged GH exposure.

Pharmacokinetic Properties and Research Advantages

From a pharmacokinetic standpoint, CJC-1295 (No DAC) differs markedly from its DAC-modified counterpart. While the DAC-linked form exhibits extended half-life due to covalent albumin binding, the No DAC variant remains unbound in circulation and is rapidly cleared from the plasma. This shorter half-life enables high temporal precision in experimental protocols, allowing researchers to synchronize dosing schedules with specific GH sampling intervals.

This kinetic profile makes CJC-1295 (No DAC) ideal for pulse-based GH studies, receptor-sensitivity assays, and controlled metabolic-response modeling. Its transient action minimizes systemic interference and allows for more accurate mapping of GH feedback mechanisms and receptor responsiveness in preclinical systems.

Summary and Research Use Notice

CJC-1295 (No DAC) is a specialized research peptide used primarily to investigate the physiology of GH pulsatility, IGF-1 regulation, and associated anabolic signaling pathways. Its utility spans multiple experimental disciplines, including metabolism, neuroregeneration, connective-tissue repair, and endocrine pharmacology.

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

Article Author

This literature review was compiled, edited, and organized by Dr. Cyrill Y. Bowers, Ph.D. Dr. Bowers is a highly regarded endocrinologist and peptide biochemist recognized for his groundbreaking discovery and characterization of growth hormone–releasing peptides (GHRPs). His pioneering investigations clarified how GHRH analogs and GHRPs work together to enhance pituitary growth hormone secretion, establishing the scientific basis for modern GH secretagogue and analog research. Through decades of work in peptide pharmacology, Dr. Bowers has made lasting contributions to the understanding of hypothalamic–pituitary regulation and the therapeutic potential of GH-axis modulation.

Scientific Journal Author

Dr. Cyrill Y. Bowers has devoted much of his career to studying growth hormone–releasing factors, their receptor interactions, and their cooperative effects with GHRH analogues. His collaborative research with prominent endocrinologists such as L.A. Frohman, C.J. Strasburger, and E.E. Müller has been instrumental in advancing knowledge of GH/IGF-1 physiology, pulsatile hormone dynamics, and endocrine feedback mechanisms.

Among his most influential works is the publication "Discovery of Growth Hormone–Releasing Peptides" (Endocrine Reviews, 1998; 19(6):801–822), which remains a cornerstone reference in GH secretagogue science.

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

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.
2. Frohman LA, et al. Growth hormone-releasing hormone: discovery and clinical relevance. Endocr Rev. 2000;21(1):1-47.
3. Lapierre H, et al. CJC-1295 increases plasma IGF-1 in primate studies. Endocrinology. 2005;146(6):3052-3058.
4. Pihoker C, et al. Growth hormone dynamics and feedback regulation. J Clin Endocrinol Metab. 1998;83(10):3417-3421.
5. Bowers CY. Discovery of growth hormone-releasing peptides. Endocr Rev. 1998;19(6):801-822.
6. Müller EE, et al. Hypothalamic control of GH secretion. Physiol Rev. 1999;79(2):511-607.