Description
The nomenclature “CJC-1295 no DAC” is widely utilized within the research community to describe the peptide structurally defined as Modified GRF (1-29). While the native 29-amino-acid sequence of GHRH (Sermorelin) is fully bioactive, it is highly susceptible to rapid enzymatic cleavage by dipeptidyl peptidase-4 (DPP-4), resulting in an in vivo half-life of under 10 minutes.
To overcome this limitation in experimental models, Modified GRF (1-29) incorporates four strategic amino acid substitutions (D-Ala2, Gln8, Ala15, Leu27). These modifications prevent premature enzymatic degradation, successfully extending the peptide’s half-life to approximately 30 minutes. Crucially, because it lacks the Drug Affinity Complex (DAC) found in true CJC-1295 (which binds to serum albumin to extend the half-life to several days), “no DAC” maintains a kinetic profile that mimics the brief, acute, and natural physiological pulsatility of endogenous GH release, preventing the somatotroph receptor desensitization associated with continuous exposure.
Biochemical Characteristics
Chemically, CJC-1295 no DAC functions as an optimized synthetic secretagogue designed to interface directly with specialized G protein-coupled receptors on pituitary cell membranes.
- Sequence/Structure: 29-amino acid tetrasubstituted polypeptide (Modified GRF 1-29) engineered to resist DPP-4 cleavage.
- Receptor Affinity: Binds with high specificity to the growth hormone-releasing hormone receptor (GHRHR) on somatotrophs.
- Stability: Supplied as a lyophilized salt to ensure long-term stability and prevent hydrolytic or proteolytic degradation during storage.
- Specificity: Utilized to selectively stimulate acute endogenous GH secretory pathways without suppressing natural neuroendocrine feedback mechanisms in in vitro and in vivo models.
Chemical Properties
| Property |
Specification |
| Molecule Name |
Modified GRF (1-29) |
| Synonyms |
CJC-1295 without DAC; Tetrasubstituted GRF (1-29) |
| Form |
Lyophilized Powder |
| Purity |
≥99% (Verified via HPLC) |
| Solubility |
Soluble in water and organic solvents (refer to SDS) |
| Documentation |
COA available per lot; SDS available |
(Note: Exact Molecular Weights and Formulas should be verified per lot COA/SDS).
CJC-1295 no DAC is strictly for laboratory research and is commonly employed in the following investigational areas:
Episodic Somatotropic Axis Modulation
This compound is extensively utilized as a chemical probe to study the biophysics of pulsatile pituitary receptor activation. Researchers use it to quantify the dose-dependent stimulation of adenylate cyclase and the subsequent exocytosis of GH, focusing on how episodic (rather than continuous) signaling preserves receptor sensitivity in isolated neuroendocrine cellular models.
Cellular Aging and Endocrine Senescence
In experimental models of age-related endocrine decline, Modified GRF (1-29) is investigated for its capacity to restore youthful episodic GH secretion. Assays focus on how re-establishing the episodic GH/IGF-1 axis impacts cellular turnover, oxidative stress markers, and physiological senescence in mammalian tissue lines.
Metabolic Flux & Lipid Mobilization
Because endogenous GH secretion is highly lipolytic, experimental models utilize this compound to study the downstream metabolic consequences of restored GH pulsatility. Researchers quantify changes in lipid metabolism, nitrogen balance, and lean muscle mass preservation to understand the broader role of the targeted GHRH axis in metabolic reprogramming.
Pathway / Mechanistic Context
The primary mechanism of action for CJC-1295 no DAC in research settings revolves around the targeted, acute activation of the GHRH receptor.
- Receptor Activation: Under experimental conditions, the peptide binds to the GHRHR, a Gs protein-coupled receptor located on the anterior pituitary.
- Signal Transduction: This binding stimulates adenylate cyclase, leading to a rapid accumulation of intracellular cyclic AMP (cAMP) and the activation of Protein Kinase A (PKA).
- Resulting Flux: Elevated cAMP and PKA activation trigger the opening of voltage-dependent calcium channels. The resulting influx of Ca2+ drives the immediate, robust exocytosis of stored GH vesicles. Because the peptide’s half-life is ~30 minutes, this signaling cascade is self-limiting, allowing the cell to rapidly reset and maintain standard neuroendocrine feedback loops.
Preclinical Research Summary
Published preclinical literature documents investigations of Modified GRF (1-29) across multiple experimental models for pathway characterization:
- Receptor Sensitivity: Studies in isolated cellular models demonstrate that unlike continuous exposure to DAC-bound analogues (which can lead to rapid receptor downregulation and elevated trough GH levels), the ~30-minute half-life of Modified GRF (1-29) maintains optimal somatotroph responsiveness and physiological baseline levels.
- Pharmacokinetics: Research indicates that the tetrasubstituted modifications successfully shield the active sequence from DPP-4 enzymes, allowing for a biologically relevant window of receptor activation that is significantly longer than native GRF(1-29) but avoids the non-pulsatile sustained exposure of albumin-binding conjugates.
- Metabolic Impact: Administration in mammalian models successfully elevates episodic GH pulse amplitude and restores secondary IGF-1 concentrations to ranges observed in younger specimens without disrupting somatostatinergic tone.
Form & Analytical Testing
This material is produced via robust chemical synthesis and supplied as a lyophilized (freeze-dried) powder.
- Lyophilization: Removes water content under vacuum to maintain compound integrity and extend shelf-life.
- Identity Verification: Each lot undergoes Mass Spectrometry (MS) to confirm molecular weight and identity.
- Purity Verification: High-Performance Liquid Chromatography (HPLC) is performed to ensure the product meets the ≥99% purity standard required for reproducible research data.
Referenced Citations
References are provided for informational purposes only and are not clinical claims.
- Jetté, L., Léger, R., Thibaudeau, K., et al. (2005). Human growth hormone-releasing factor (hGRF)1-29-albumin bioconjugates activate the GRF receptor on the anterior pituitary in rats: identification of CJC-1295 as a long-lasting GRF analog. Endocrinology, 146(7), 3052–3058. https://doi.org/10.1210/en.2004-1286
- Teichman, S. L., Neale, A., Lawrence, B., et al. (2006). Prolonged Stimulation of Growth Hormone (GH) and Insulin-Like Growth Factor I Secretion by CJC-1295, a Long-Acting Analog of GH-Releasing Hormone, in Healthy Adults. The Journal of Clinical Endocrinology & Metabolism, 91(3), 799–805. https://doi.org/10.1210/jc.2005-1536
- Soule, S., King, J. A., Millar, R. P. (1994). Incorporation of D-Ala2 in growth hormone-releasing hormone-(1-29)-NH2 increases the half-life and decreases metabolic clearance in normal men. The Journal of Clinical Endocrinology & Metabolism, 79(4), 1208–1211. https://doi.org/10.1210/jcem.79.4.7962295
RESEARCH USE ONLY
This product is intended strictly for laboratory research use only. It is not for human or veterinary use. It is not intended for diagnosis, treatment, cure, or prevention of any disease. All purchases are subject to our Terms of Service and Purity Guarantee.
No COAs available for this product.
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