What is CJC-1295 (NO DAC) + GHRP-6?
CJC-1295 (No DAC) + GHRP-6 is a combination preparation of two distinct synthetic research peptides that are frequently co-formulated because they act on complementary nodes of the somatotropic (growth hormone) signaling axis. The blend is classified as a research-grade peptide mixture in the "blends" category and is intended exclusively for laboratory research use.
CJC-1295 without DAC — also referred to in the literature as Modified GRF(1-29) — is a peptide analog corresponding to the biologically active N-terminal fragment of growth hormone-releasing hormone (GHRH). It carries amino-acid substitutions that improve enzymatic stability relative to native GHRH, and, unlike the DAC (Drug Affinity Complex) variant, it omits the maleimidopropionic acid linker used for albumin conjugation, giving it a shorter circulating profile in study models. GHRP-6 is a synthetic hexapeptide belonging to the growth hormone-releasing peptide (GHRP) class of ghrelin-receptor (GHS-R) ligands. The two molecules represent different structural families: one a GHRH-analog, the other a small secretagogue peptide.
Within the scientific literature, this pairing is studied as a model system for investigating the growth hormone / GHRH-receptor and ghrelin-receptor pathways in vitro and in controlled preclinical research settings. This reference page describes only the material's classification, structure, and handling characteristics; it makes no representation regarding physiological effects and provides no dosing, administration, or usage guidance of any kind.
Reconstitution & handling
As supplied, the blend is a lyophilized (freeze-dried) white-to-off-white powder. For laboratory reconstitution, researchers typically dissolve peptide powders of this type in bacteriostatic or sterile water; sterile physiological saline may also be used depending on the downstream assay. The diluent is introduced slowly and directed against the wall of the vial rather than injected directly onto the powder cake, and the vial is then swirled gently — not shaken or vortexed vigorously — to protect peptide bond integrity and minimize foaming or shear-induced aggregation. Dissolution is generally allowed to proceed at rest until the solution is clear and free of visible particulates.
Small peptides such as GHRP-6 dissolve readily in aqueous media, while GHRH-analog fragments are also water-soluble; the combined material is intended to yield a clear working solution. Reconstituted peptide solutions should be handled aseptically, kept cold during use, and protected from prolonged exposure to light and repeated warming, which can promote oxidation and hydrolysis. This section addresses solvent chemistry and physical handling only and does not describe concentrations, volumes, or any application protocol.
Storage & stability
In lyophilized form, the blend is stable for extended periods when stored sealed, desiccated, and protected from light — commonly at -20 degrees C for long-term storage, with short-term transport at ambient temperature tolerated due to the stability of the dry powder. Once reconstituted, the peptide solution is far less stable and should be refrigerated at approximately 2-8 degrees C for near-term use, or frozen in single-use aliquots for longer holding to avoid repeated freeze-thaw cycles, which degrade peptide integrity. Minimizing exposure to heat, light, and atmospheric moisture preserves purity across the storage period.
How it's tested
Identity and purity of the blend are verified analytically prior to release. Reversed-phase high-performance liquid chromatography (RP-HPLC) is used to quantify chromatographic purity, confirmed at ≥99%, and to resolve each peptide component and any related impurities. Mass spectrometry (MS) is used to confirm the molecular identity of the constituent peptides by matching observed masses to their expected values. A Certificate of Analysis (COA) documenting these results is available for the material, providing traceable verification of identity and purity for research recordkeeping.