CJC-1295 with DAC

An Introduction to CJC-1295 with DAC

CJC-1295 with DAC (Drug Affinity Complex) is a synthetically manufactured peptide developed as an enhanced version of growth hormone–releasing hormone (GHRH). The compound has been optimized through molecular design to improve degradation resistance and extend the timeframe of biological activity within the body. The DAC technology enables binding to blood albumin proteins, reducing the rate of kidney-mediated elimination and enzymatic degradation. This mechanism results in a prolonged period of growth hormone stimulation that substantially exceeds the response duration of standard GHRH preparations, providing continuous endocrine support.

Understanding CJC-1295 with DAC: Biological Mechanism and Effects

CJC-1295 with a Drug Affinity Complex is an engineered, extended-acting analog of GHRH designed to maximize both chemical resilience and the duration of growth hormone (GH) stimulation effects. The peptide operates by activating GHRH receptors on pituitary cells, initiating biochemical processes that generate the characteristic pulsatile release of GH, mirroring natural hormonal secretion patterns.

When released into circulation, GH directs peripheral tissues and the hepatic system to produce and release insulin-like growth factor-1 (IGF-1), which serves as the primary agent driving anabolic responses, tissue recovery, and cellular proliferation. Together, GH and IGF-1 form a critical regulatory system controlling energy substrate metabolism, fat oxidation, and the synthesis of muscular proteins. Of particular relevance, GH mediates the mobilization of lipid deposits in both deep and superficial fat compartments while simultaneously maintaining skeletal muscle integrity.

The DAC modification confers a significant pharmacological benefit through establishment of a stable chemical bond with circulating albumin molecules. This interaction dramatically extends the peptide's half-life, supporting persistent receptor signaling and continuous GH secretion. Consequently, CJC-1295 with DAC preserves its biological activity across extended periods of days to weeks—far surpassing the brief activity windows of alternatives without DAC such as conventional CJC-1295 or native GHRH(1-29).

From a molecular perspective, CJC-1295 engagement with the GHRH receptor is postulated to activate cAMP-dependent signaling through stimulation of the enzyme adenylate cyclase. This triggers a cascade activating protein kinase A (PKA), which phosphorylates nuclear transcription factors to increase transcription of GH genes within pituitary somatotrophs. The sustained presence of the albumin-conjugated form perpetuates this signaling cascade, resulting in amplified cumulative GH secretion and higher IGF-1 levels compared to short-acting peptide variants.

In essence, CJC-1295 with DAC represents a valuable experimental tool for investigating sustained endocrine stimulation, understanding the regulatory mechanisms of the GH/IGF-1 system, and assessing the metabolic consequences associated with extended GH pulsatility.

CJC-1295 with DAC Peptide: Chemical Profile

Physicochemical Characteristics

Appearance: White freeze-dried powder

Molecular Formula: C₁₆₅H₂₇₁N₄₇O₄₆

Molecular Weight: Approximately 3647.9 g/mol

Sequence: GHRH(1–29) template with DAC modification attached

Purity Assessment: ≥ 98% per Certificate of Analysis documentation

CJC-1295 with DAC: Laboratory Research Applications

Optimal Storage and Maintenance Conditions

CJC-1295 with DAC is delivered as a purified, lyophilized preparation suitable for laboratory investigations. To ensure preservation of the molecular structure and biological functionality, storage at –20°C in the anhydrous powdered state is recommended. Following dissolution in aqueous solution, the peptide solution requires storage under sterile conditions at 2–8°C for short-term experimental use. These conditions maintain chemical integrity and minimize the risk of unwanted degradation or introduction of bacterial contamination during experimental manipulations.

Effects on Growth Hormone Release and Circulating Levels

Studies in human subjects and animal models show that administration of a single dose of CJC-1295 with DAC triggers sustained increases in circulating GH and IGF-1 that persist for approximately one week. This extended hormonal response contrasts notably with the brief response pattern observed with native GHRH(1-29) or earlier non-DAC peptide variants. Quantitative findings demonstrate approximately 2–3-fold increases in IGF-1 plasma levels paired with stable GH pulsatile secretion, demonstrating strong receptor activation and sustained bioavailability of the peptide within the bloodstream.

Metabolic Impact of CJC-1295 with DAC Treatment

Experimental data indicate that CJC-1295 with DAC triggers significant metabolic changes through mechanisms involving elevation of circulating GH and IGF-1. Research outcomes from preclinical investigations point to increases in fat breakdown, improved oxidative fat metabolism, and maintenance of lean muscle tissue, all consistent with GH's recognized anabolic and catabolic effects. The compound has been evaluated for its impact on protein biosynthesis, tissue regeneration and restoration processes, and whole-body energy utilization, establishing its utility for investigating the metabolic pathways regulated by growth hormone.

Bioavailability and Duration of Action

In distinction to faster-acting GHRH analogs, the DAC structural component of CJC-1295 enables covalent linkage with serum albumin, markedly decreasing renal excretion and resistance to enzymatic inactivation. The strong affinity between peptide and albumin substantially prolongs the time the molecule remains biochemically active in the bloodstream, sustaining receptor engagement and prolonged endocrine activation. Pharmacokinetic assessments estimate the elimination half-life at approximately 5.8 to 8.1 days, considerably longer than the minutes-to-hours clearance observed with non-albumin-binding variants, thereby reducing the need for frequent dosing schedules in experimental protocols.

Research Attribution and Scientific Expertise

Compilation and Editorial Coordination

This comprehensive literature review was gathered, evaluated, and organized by Dr. Stuart L. Teichman, M.D. A recognized authority in endocrinology and translational research, Dr. Teichman has pioneered investigations into extended-duration GHRH analogs, with specific emphasis on CJC-1295. His landmark research efforts have characterized the pharmacological features, safety profile, and potential therapeutic applications of GHRH-based compounds, demonstrating their efficacy in sustaining elevated GH and IGF-1 levels. Dr. Teichman's contributions have fundamentally shaped the field of peptide endocrinology and the development of prolonged-acting hormonal agents.

Research Contributions and Scientific Collaboration

Throughout his professional trajectory, Dr. Stuart L. Teichman has focused on the investigation of GH secretion stimulators, GHRH-based peptides, and hormone regulation via synthetic peptides. In conjunction with colleagues A. Neale, B. Lawrence, and C. Gagnon, Dr. Teichman has generated substantial scientific literature on the operational mechanisms of extended-duration GHRH analogs, their effects on GH/IGF-1 regulatory networks, and their systemic metabolic consequences. His accumulated scientific work provides a crucial knowledge base supporting the development of contemporary peptide-based medications targeting hormonal regulation and metabolic health optimization.

This attribution serves exclusively as scientific recognition and does not constitute a professional endorsement or marketing advertisement. Montreal Peptides Canada declares no organizational partnership, sponsorship arrangement, or collegial affiliation with Dr. Teichman or any of the acknowledged collaborators.

Academic Reference Sources

Teichman SL, Neale A, Lawrence B, Gagnon C, et al. Prolonged stimulation of GH and IGF-1 secretion by CJC-1295, a long-acting GHRH analog. J Clin Endocrinol Metab. 2006;91(3):799-805. https://pubmed.ncbi.nlm.nih.gov/16352683/

Broglio F, et al. Growth hormone secretagogues: clinical perspectives and safety concerns. Growth Horm IGF Res. 2009;19(1):1-9. https://pubmed.ncbi.nlm.nih.gov/19054601/

Ghigo E, et al. Growth hormone secretagogues: physiology and clinical applications. Endocr Rev. 2005;26(3):345-376. https://pubmed.ncbi.nlm.nih.gov/15814849/

Anderson-Baucum EK, et al. GH/IGF-1 axis and metabolic regulation. Mol Cell Endocrinol. 2018;469:1-14. https://pubmed.ncbi.nlm.nih.gov/29288913/

Wu Z, et al. Growth hormone and IGF-1 signaling in muscle metabolism. Front Endocrinol (Lausanne). 2020;11:607. https://pubmed.ncbi.nlm.nih.gov/33281526/

Ranke MB, Wit JM. Growth hormone-past, present and future. Nat Rev Endocrinol. 2018;14(5):285-300. https://pubmed.ncbi.nlm.nih.gov/29479014/

Strasburger CJ, et al. GH and IGF-1 in clinical practice: new insights. Eur J Endocrinol. 2021;185(6):R123-R136. https://pubmed.ncbi.nlm.nih.gov/34870144/

Smith TR, et al. The role of GH and IGF-1 in tissue repair and regeneration. Exp Gerontol. 2015;68:46-52. https://pubmed.ncbi.nlm.nih.gov/25987250/