







CJC-1295 (NO DAC)
CJC-1295 (without DAC), widely recognized in scientific literature as Modified GRF 1-29, from Super Human Peptides UK is a highly advanced, synthetic Growth Hormone-Releasing Hormone (GHRH) analogue. In laboratory research, native GHRH is nearly useless for long-term modeling because it is rapidly cleaved and destroyed by the dipeptidyl peptidase-4 (DPP-4) enzyme within 5 minutes. Researchers utilize CJC-1295 (without DAC) because it features four specific amino acid substitutions (tetrasubstituted) that physically shield it from DPP-4 degradation.
This engineering extends its active biological half-life to approximately 30 minutes. Unlike the DAC version—which causes a continuous, unnatural "bleed" of growth hormone—this specific 30-minute window perfectly mimics the body's natural rhythm, triggering a massive but natural physiological pulse of Growth Hormone (GH). Produced under GMP-compliant conditions and verified for 99% purity or higher, it is an elite tool for advanced preclinical research into episodic GH secretion, slow-wave sleep architecture, and synergistic endocrine modeling.
- —Tetrasubstituted Engineering: Features four distinct amino acid replacements to prevent rapid enzymatic destruction by DPP-4.
- —Natural Pulsatile Rhythm: Maintains an optimal 30-minute half-life to trigger a massive, episodic GH spike that mimics natural pituitary function.
- —Prevents Receptor Desensitization: Because it clears the system rapidly, it prevents the down-regulation of GHRH receptors often seen with long-acting continuous agonists.
- —Synergistic Baseline: The premier GHRH utilized in combination modeling with Growth Hormone-Releasing Peptides (like Ipamorelin or GHRP-6) to bypass somatostatin blocks.
- —High Purity: 99% purity or higher (verified by HPLC and MS analysis).
- —Quality Standard: GMP / ISO certified manufacturing.
- —Episodic Pharmacokinetics: Studying the rapid onset, peak, and clearance of circulating Growth Hormone and IGF-1 to model natural circadian endocrinology.
- —Slow-Wave Sleep Architecture: Investigating the peptide's role in deepening the delta-wave sleep phase, which is the primary biological window for memory consolidation and tissue repair.
- —Receptor Up-Regulation: Measuring the sustained sensitivity of pituitary somatotrophs when exposed to intense, short-duration GHRH agonism versus continuous saturation.
- —Lipolysis and Visceral Fat: Preclinical models exploring the acute mobilization of free fatty acids from white adipose tissue immediately following an induced GH pulse.
- —Cellular Senescence: Evaluating the peptide's ability to maintain youthful metabolic turnover and protein synthesis in naturally aged animal models.
The development of Modified GRF 1-29 was a pivotal moment in peptide endocrinology. Originally, researchers isolated the active 29-amino-acid core of native Growth Hormone-Releasing Hormone (known as GRF 1-29 or Sermorelin). However, because Sermorelin is destroyed in less than 10 minutes by blood enzymes, it required constant, impractical administration to yield results.
By substituting four specific amino acids (at positions 2, 8, 15, and 27), researchers successfully blocked the DPP-4 enzyme from cleaving the chain. In laboratory and clinical modeling, this tetrasubstituted peptide—CJC-1295 without DAC—demonstrated the ability to safely survive in the bloodstream just long enough to reach the anterior pituitary and trigger a maximal GH release. Studies confirmed that this transient 30-minute activation is the exact biological duration required to stimulate intense tissue repair and lipolysis without disrupting the body's natural negative feedback loops.
- 1.Jette, L. et al., "Human growth hormone-releasing hormone (hGHRH) 1-29-albumin bioconjugates activate the GRF receptor on the anterior pituitary in rats," Endocrinology, 2005. (Details the structural substitutions required for stability).
- 2.Campbell, R.M. et al., "Enhanced stability and potency of novel growth hormone-releasing factor (GRF) analogues derived from rodent and human sequences," Peptides, 1991.
- 3.Martin, J.B., "Neural regulation of growth hormone secretion," The New England Journal of Medicine, 1973. (Contextual physiology of pulsatile GH).
- 4.Alba-Roth, J. et al., "Arginine stimulates growth hormone secretion by suppressing endogenous somatostatin secretion," The Journal of Clinical Endocrinology & Metabolism, 1988. "By clicking 'Add to Cart,' I certify that I am purchasing this product for laboratory research use only and agree to the Terms of Service regarding non-human consumption.".


