CJC-1295 DAC is a synthetic 29-amino-acid tetrasubstituted peptide derivative of growth hormone-releasing hormone (GHRH). Featuring a Drug Affinity Complex (DAC) maleimido derivative moiety, it covalently binds to endogenous serum albumin in preclinical models. This conjugation extends its biological half-life while selectively targeting GHRH receptors for tissue repair and metabolic research.
CJC-1295 DAC is a synthetic 29-amino-acid tetrasubstituted peptide derivative of growth hormone-releasing hormone (GHRH). Featuring a Drug Affinity Complex (DAC) maleimido derivative moiety, it covalently binds to endogenous serum albumin in preclinical models. This conjugation extends its biological half-life while selectively targeting GHRH receptors for tissue repair and metabolic research.
CJC-1295 DAC represents an advanced modification of the naturally occurring growth hormone-releasing hormone (GHRH 1-29) fragment, often referred to as modified GRF 1-29. The natural peptide sequence is susceptible to rapid enzymatic degradation in vivo, primarily by dipeptidyl peptidase IV (DPP-IV), resulting in an extremely short circulating half-life of mere minutes. To overcome this kinetic limitation in laboratory evaluation, researchers developed a tetrasubstituted variant containing specific amino acid substitutions at positions 2, 8, 15, and 27 (D-Ala2, Gln8, Ala15, and Leu27). These modifications significantly enhance resistance against cleavage by serum proteases.
The defining technical feature of CJC-1295 DAC is the addition of the Drug Affinity Complex (DAC) reactive group. This structure consists of a Lysine residue coupled to a 3-maleimidopropionic acid linker attached at the C-terminus of the modified peptide sequence. In biological matrices or culture media containing serum proteins, the maleimide group reacts specifically and irreversibly with the nucleophilic thiol group of Cys34 on circulating albumin. This bioconjugation process yields a stable peptide-albumin complex, dramatically extending the effective circulation kinetics from minutes to several days without compromising its target specificity.
At the cellular level, CJC-1295 DAC functions as a potent agonist at the growth hormone-releasing hormone receptor (GHRHR), a G-protein coupled receptor (GPCR) predominantly expressed on the somatotropes of the anterior pituitary gland. Upon ligand binding, the receptor undergoes a conformational change that activates the intracellular Gαs subunit. This subunit stimulates adenylyl cyclase, prompting an intracellular elevation of cyclic adenosine monophosphate (cAMP) and subsequent activation of protein kinase A (PKA).
The resulting signaling cascade triggers calcium influx through voltage-gated channels, facilitating the exocytosis of stored growth hormone (GH) secretory vesicles. Preclinical models demonstrate that because the albumin-bound conjugate remains present in systemic circulation over an extended period, it provides persistent, low-level stimulation of the GHRHR. This continuous receptor occupancy produces sustained elevations in basal GH concentration, which sequentially stimulates hepatic transcription and release of insulin-like growth factor 1 (IGF-1) for downstream tissue repair and cellular homeostasis investigations.
In animal models, particularly rodent and non-human primate studies, CJC-1295 DAC has been extensively evaluated to map its endocrine dynamics and systemic impacts. Quantitative assays demonstrate that a single administration of the compound leads to dose-dependent elevations in total plasma GH levels and serum IGF-1 concentrations lasting over 6 to 14 days, depending on the animal model utilized. Unlike unmodified GHRH analogs, which yield transient GH spikes that return to baseline within hours, the persistent bioavailability of CJC-1295 DAC alters the profile of GH secretion towards a elevated basal plateau.
Researchers investigating research peptides for regenerative tissue models focus on how continuous elevations of IGF-1 drive cellular proliferation, collagen synthesis, and protein accretion. In vitro cultures of osteocytes and chondrocytes exposed to GHRH-stimulated media show increased extracellular matrix deposition. Furthermore, rodent models evaluating metabolic activity demonstrate shifts in lipid oxidation and nitrogen retention when sustained GHRH signaling is maintained, making CJC-1295 DAC a valuable standard in metabolic and tissue repair research.
To understand the distinct research profile of CJC-1295 DAC, it is useful to compare it against other prominent growth hormone secretagogues evaluated in laboratory settings. The presence of the maleimide moiety differentiates it fundamentally from non-DAC analogs, altering clearance rates, receptor interaction dynamics, and experimental design parameters.
While CJC-1295 No DAC shares the same tetrasubstituted peptide sequence, its lack of the albumin-binding moiety results in a rapid clearance profile with a half-life of approximately 30 minutes, producing sharp, acute GH pulses. In contrast, Sermorelin, an unmodified 29-amino-acid sequence, exhibits even faster degradation. When compared to ghrelin receptor agonists like Ipamorelin, CJC-1295 DAC acts through an entirely separate biochemical pathway (GHRHR vs. GHSR-1a). Researchers often design dual-agonist protocols in vitro to study the synergistic activation of pituitary somatotropes via concurrent GHRH and ghrelin receptor stimulation.
Lyophilized CJC-1295 DAC requires proper laboratory handling and reconstitution protocols to maintain molecular integrity and prevent premature hydrolysis or aggregation. Prior to reconstitution, peptide vials should be stored at -20°C or -80°C in a desiccated environment. Upon removal from cold storage, vials must be allowed to equilibrate to room temperature before opening to minimize moisture condensation inside the container.
Reconstitution should be performed using sterile, laboratory-grade Bacteriostatic Water (0.9% benzyl alcohol) or Sterile Water for Injection, depending on the experimental assay requirements. The diluent should be introduced gently along the glass inner wall of the vial rather than sprayed directly onto the lyophilized cake. Gentle swirling or slow inversion is recommended to dissolve the powder completely; vigorous agitation, vortexing, or shaking must be strictly avoided as shear forces can cause peptide denaturation or aggregation. Once reconstituted, solutions should be aliquoted and stored at 2°C to 8°C for short-term use, or frozen at -80°C for extended experimental timelines.
Reliable scientific outcomes depend entirely on the purity and chemical fidelity of research reagents. When evaluating vendors for all research peptides, researchers must insist on comprehensive, lot-specific analytical documentation. High-performance liquid chromatography (RP-HPLC) is the gold standard method for determining chemical purity, ensuring that related peptide impurities, truncated sequences, or unreacted synthetic intermediates are quantified and minimized.
To verify molecular identity and structural correctness, liquid chromatography-mass spectrometry (LC-MS) or electrospray ionization mass spectrometry (ESI-MS) must be performed to confirm the exact monoisotopic mass of CJC-1295 DAC (typically 3647.95 Da). Furthermore, because bacterial contamination can alter cell culture signaling or induce non-specific inflammatory cytokines in preclinical models, reagents must undergo chromogenic LAL testing to verify low endotoxin levels (< 0.01 EU/mg). PX1 Research provides lot-traceable Certificate of Analysis (COA) documents verified by independent ISO 17025 accredited laboratories for every batch.
Sourcing high-purity research compounds requires a rigid supplier verification process. Laboratories must confirm that manufacturing occurs within cGMP-compliant facilities that maintain strict environmental controls, cleanroom standards, and standardized synthesis protocols. Synthetic peptides synthesized via automated solid-phase peptide synthesis (SPPS) require rigorous purification steps to eliminate residual solvents, counterions, and TFA salts that could interfere with sensitive cell viability assays.
At PX1 Research, all research compounds are manufactured in the USA under ISO 9001 and cGMP-compliant guidelines. Every lot is subjected to dual HPLC and MS testing, full endotoxin screening, and structural verification before release. For high-volume academic and institutional research facilities requiring consistent lot uniformity across longitudinal studies, specialized wholesale lab accounts are available to secure dedicated batch allocations with complete analytical traceability.
As research into peptide therapeutics and growth factor signaling evolves, long-acting GHRH derivatives like CJC-1295 DAC remain pivotal tools in understanding endocrine regulation, tissue remodeling, and cell turnover. Emerging preclinical studies are investigating how sustained GHRH signaling influences cardiac tissue repair post-ischemia, peripheral nerve regeneration, and age-related metabolic dysregulation in animal models.
Understanding the precise interplay between continuous GHRH receptor agonism and intracellular receptor desensitization or downregulation is an active area of investigation in our research library hub. By utilizing standardized, high-purity CJC-1295 DAC, investigators can continue to unearth fundamental biological insights into somatotrophic axis modulation without confounding variations introduced by inconsistent compound quality.
What is CJC-1295 DAC and how does it differ from standard CJC-1295?
CJC-1295 DAC includes a Drug Affinity Complex (DAC) maleimide reactive moiety that covalently binds to circulating serum albumin in vitro and in vivo. Standard CJC-1295 (without DAC) lacks this binding group, resulting in a much shorter biological half-life (~30 minutes vs. several days for the DAC variant).
What receptor target does CJC-1295 DAC bind to?
CJC-1295 DAC acts as a selective agonist at the growth hormone-releasing hormone receptor (GHRHR) located on pituitary somatotropes, stimulating intracellular cAMP production and downstream growth hormone release.
What is the monoisotopic molecular weight of CJC-1295 DAC?
The theoretical molecular weight of CJC-1295 DAC is approximately 3647.95 Da, which is verified via Mass Spectrometry (LC-MS / ESI-MS) on every PX1 Research Certificate of Analysis.
How should CJC-1295 DAC be stored upon delivery?
Lyophilized CJC-1295 DAC should be stored at -20°C or -80°C in a dry environment. Reconstituted solutions should be kept at 2°C to 8°C for short-term experiment windows or aliquoted and stored at -80°C to prevent freeze-thaw degradation.
What reconstituting solvents are recommended for laboratory use?
Sterile Bacteriostatic Water (0.9% benzyl alcohol) or standard Sterile Water for Injection are recommended diluents. Reconstitution should involve gentle swirling rather than shaking to avoid peptide denaturation.
Are PX1 Research compounds tested for endotoxins?
Yes. Every lot of CJC-1295 DAC undergoes chromogenic Limulus Amebocyte Lysate (LAL) testing conducted by an independent ISO 17025 accredited laboratory to ensure endotoxin levels remain strictly below required research thresholds.
Can CJC-1295 DAC be used alongside ghrelin receptor agonists in vitro?
Yes. In preclinical literature, researchers frequently co-administer GHRH analogs like CJC-1295 DAC with ghrelin receptor agonists (such as Ipamorelin) to study synergistic GH secretion via independent signaling pathways.
How does PX1 Research verify batch purity?
PX1 Research utilizes reverse-phase high-performance liquid chromatography (RP-HPLC) to verify chemical purity (≥98%) and mass spectrometry (MS) to confirm molecular weight and sequence identity for every lot.
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