CJC-1295 (No DAC)
CJC-1295 (No DAC) is a synthetic peptide developed as an analog of endogenous growth hormone–releasing hormone (GHRH). The molecule consists of 30 amino acids and selectively interacts with GHRH receptors expressed on pituitary somatotroph cells. This interaction stimulates episodic secretion of growth hormone (GH), which in turn promotes downstream production of insulin-like growth factor 1 (IGF-1). The defining feature of the No DAC variant is the absence of a Drug Affinity Complex modification, resulting in a shorter circulating half-life and transient GH signaling.
These properties position CJC-1295 (No DAC) as a valuable experimental compound for laboratory investigations into GH pulsatility, endocrine regulation, anabolic signaling pathways, and regenerative biology under physiologically relevant hormone-release conditions.
CJC-1295 (No DAC) Overview
CJC-1295 (No DAC) is derived from the native GHRH(1–29) sequence and incorporates four intentional amino acid substitutions at positions 2, 8, 15, and 27. These modifications enhance peptide stability and resistance to enzymatic cleavage while preserving receptor specificity and functional bioactivity. The resulting analog demonstrates improved experimental reliability without altering its mechanism of action.
Unlike DAC-conjugated GHRH analogs, which extend hormone exposure through albumin binding, the No DAC formulation remains unbound in circulation. This results in rapid clearance and supports discrete GH pulses rather than sustained hormonal elevation. Such characteristics are particularly advantageous in experimental designs seeking to replicate endogenous GH secretion patterns.
In research settings, CJC-1295 (No DAC) is frequently examined alongside growth hormone secretagogues (GHS), including Ipamorelin and other GHRPs, to evaluate combined effects on GH amplitude, metabolic regulation, tissue remodeling, and body composition outcomes.
CJC-1295 (No DAC) Structure
The molecular architecture of CJC-1295 (No DAC) closely mirrors that of endogenous GHRH while incorporating stabilizing substitutions that extend functional activity without prolonging systemic exposure. This structural balance enables consistent receptor engagement and reproducible experimental outcomes.
CJC-1295 (No DAC) Research
Growth Hormone Release and Biological Activity
CJC-1295 (No DAC) functions as a selective agonist of pituitary GHRH receptors, inducing pulsatile GH secretion that aligns with physiologic endocrine rhythms. This episodic release profile reduces the risk of receptor desensitization and excessive feedback inhibition commonly associated with continuous GH stimulation. Preclinical investigations demonstrate dose-dependent increases in GH and IGF-1 concentrations, supporting its utility in anabolic signaling research.
Metabolic and Body Composition Research
Experimental models utilizing CJC-1295 (No DAC) have reported elevations in GH and IGF-1 that influence lipid metabolism, nitrogen balance, and lean tissue preservation. These outcomes are central to studies examining fat utilization, energy partitioning, and skeletal muscle maintenance.
When combined with GHS compounds, CJC-1295 (No DAC) enhances GH pulse frequency and magnitude, allowing researchers to study glucose metabolism, mitochondrial efficiency, cellular repair processes, and metabolic adaptation under controlled laboratory conditions.
Neurological and Regenerative Research Applications
GH and IGF-1 signaling pathways contribute to neurogenesis, synaptic remodeling, vascular integrity, and cellular survival. Research involving CJC-1295 (No DAC) has supported investigations into neural tissue repair, glial modulation, and angiogenic signaling in experimental injury and aging models.
Additionally, the peptide has been used in regenerative research examining connective tissue turnover, collagen synthesis, and musculoskeletal recovery. Its transient hormonal action enables evaluation of repair mechanisms without confounding effects from prolonged GH exposure.
Pharmacokinetic Characteristics and Experimental Advantages
CJC-1295 (No DAC) exhibits rapid plasma clearance due to the absence of albumin-binding modifications. This pharmacokinetic profile allows for precise temporal control of GH stimulation and facilitates synchronized hormone sampling. Such precision is essential for receptor-sensitivity studies, endocrine feedback modeling, and pulse-based GH research.
Summary and Research Use Notice
CJC-1295 (No DAC) is a research-grade peptide utilized to investigate GH pulsatility, IGF-1 regulation, and anabolic signaling pathways across multiple experimental domains. Its applications include metabolic research, neuroregeneration studies, connective tissue biology, and endocrine pharmacology.
This compound is supplied strictly for laboratory research purposes. It is not approved for human or veterinary administration and must not be used for diagnostic, therapeutic, or consumption-related purposes.
Article Author
This scientific review was compiled and organized by Dr. Cyrill Y. Bowers, Ph.D., a distinguished endocrinologist and peptide biochemist recognized for his pioneering work in growth hormone–releasing peptides and hypothalamic–pituitary signaling.
Scientific Journal Author
Dr. Bowers’ collaborative research with leading endocrinologists, including L.A. Frohman, C.J. Strasburger, and E.E. Müller, has substantially advanced understanding of GH pulsatility, IGF-1 physiology, and endocrine feedback systems. His publication Discovery of Growth Hormone–Releasing Peptides remains a foundational reference in peptide endocrinology.
This acknowledgment is provided solely for academic recognition. Montreal Peptides Canada maintains no affiliation with the researchers cited.
Reference Citations
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- Frohman LA, et al. Growth hormone-releasing hormone: discovery and clinical relevance. Endocr Rev. 2000;21(1):1-47. https://pubmed.n cbi.nlm.nih.gov/10696565/
- Lapierre H, et al. CJC-1295 increases plasma IGF-1 in primate studies. Endocrinology. 2005;146(6):3052-3058. https://pubmed.ncbi.nlm.ni h.gov/15746190/
- Pihoker C, et al. Growth hormone dynamics and feedback regulation. J Clin Endocrinol Metab. 1998;83(10):3417-3421. https://pubmed.n cbi.nlm.nih.gov/9768658/
- Bowers CY. Discovery of growth hormone-releasing peptides. Endocr Rev. 1998;19(6):801-822. https://pubmed.ncbi.nlm.nih.gov/9861543/
- Müller EE, et al. Hypothalamic control of GH secretion. Physiol Rev. 1999;79(2):511-607. https://pubmed.ncbi.nlm.nih.gov/10221987/
- Popovic V, et al. GH secretagogues and GHRH analogs in clinical research. J Endocrinol Invest. 2003;26(9):872-881. https://pubmed.ncb i.nlm.nih.gov/14628911/
- Jansson JO, et al. Pulsatile GH release and experimental regulation. Endocr Rev. 1985;6(2):128-150. https://pubmed.ncbi.nlm.nih.gov/286 1011/
- 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.ni h.gov/10984265/
- Bowers CY, et al. Synergistic GH release with GHRH analogs and GHS peptides. J Clin Endocrinol Metab. 1990;70(4):975-982. https://pu bmed.ncbi.nlm.nih.gov/2318961/