For Research Use Only
CJC-1295 (DAC)
CJC-1295 (DAC) — research-grade peptide. ≥ 99% purity (HPLC), Certificate of Analysis with every batch. For laboratory research use only.
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Certificate of Analysis
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CJC-1295 (DAC) COA
All Banger Labs products are independently tested by accredited third-party laboratories. Results are batch-specific and provided for research transparency only. This product is not approved for human use.
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Research Overview Cited research summary, handling & references — tap to expand
CJC-1295 with DAC: A Research Compendium
What CJC-1295 with DAC Is
CJC-1295 with DAC is a synthetic, long-acting analog of growth hormone–releasing hormone (GHRH) built on the GHRH(1-29) core and bearing a Drug Affinity Complex (DAC) — a maleimido-propionyl lysine moiety engineered to form a covalent bond with circulating serum albumin. Native GHRH and its 1-29 fragment are cleared from plasma within minutes, primarily through enzymatic cleavage near the N-terminus; the DAC strategy was conceived to defeat that rapid clearance by anchoring the peptide to the body's most abundant plasma protein, which acts as a slow-release depot. In the controlled-study literature, this albumin tethering markedly extends the analog's effective half-life and produces a prolonged stimulation of growth hormone (GH) and insulin-like growth factor I (IGF-1) secretion from the anterior pituitary in healthy adults — the result that defines the compound's research profile.[1] Importantly, that prolonged drive does not flatten the secretory pattern: pulsatility persists during continuous stimulation, indicating that endogenous regulatory feedback remains engaged.[2] CJC-1295 with DAC is studied strictly as a reference standard and a pharmacological tool for probing what sustained, days-long GHRH-receptor occupancy does to the GH/IGF-1 axis, and all of the following concerns in-vitro and controlled research contexts only.
Areas Studied in the Research Literature
Published work on CJC-1295 with DAC centers on its long duration of action, the behavior of the GH/IGF-1 axis under sustained receptor drive, the persistence of pulsatile secretion, and the underlying GHRH-receptor biology shared across the analog class. Because its defining feature is pharmacokinetic rather than pharmacodynamic, much of the interpretive interest lies in how an extended exposure window reshapes axis output over time. The summaries below describe only what investigators measured in controlled settings.
Long-Acting GHRH Stimulation
The DAC modification was specifically designed to convert a minutes-long GHRH fragment into a multi-day stimulus. In a controlled study of healthy adults, administration produced a prolonged elevation of both GH and IGF-1 secretion, with the time-course extended well beyond what unmodified GHRH(1-29) achieves — the central pharmacodynamic finding for this compound and the reason it serves as the long-acting benchmark of the class.[1]
Pulsatile Secretion Maintained
A key safety-relevant research observation is that, even during continuous stimulation by the long-acting analog, GH secretion remained pulsatile rather than collapsing into a flat plateau. This was interpreted as preservation of the native secretory architecture, implying that somatostatin tone and feedback control continued to sculpt the GH profile despite the persistent GHRH-receptor drive.[2]
GH/IGF-1 Axis Markers
Activation of the GH/IGF-1 axis by the long-acting GHRH analog produced measurable changes in the serum protein profile of normal adult subjects. These proteomic shifts provide objective, downstream biomarkers confirming that the sustained receptor drive propagated through the axis, and they broaden the set of read-outs available for characterizing GHRH analogs in research.[3]
GHRH-Receptor Pharmacology
The analog acts entirely through the pituitary GHRH receptor, a Gs-coupled class-B GPCR. Reviews of GHRH biology frame how receptor engagement raises cAMP to govern both GH gene transcription and release, and how the 1-29 core preserves that activity — the mechanistic basis that the DAC chemistry leaves intact while extending duration.[4]
Comparative Context
Because the only difference between this compound and the no-DAC construct is the albumin anchor, the pair is frequently used together to dissociate the contribution of receptor pharmacology from the contribution of pharmacokinetics, with the DAC form serving as the long-duration arm in such comparisons.[5]
Reconstitution, Handling & Storage (Research)
The following reflect general peptide research-handling practice described in the literature for GHRH-analog reference standards; they are bench-handling notes for reference standards, not directions for use, and they apply to in-vitro and analytical work only. Exact parameters always defer to the supplier certificate of analysis and to the requirements of the specific assay being run.
Reconstitution
In published peptide-handling protocols, lyophilized CJC-1295 with DAC is brought to room temperature before opening to prevent condensation onto the hygroscopic powder, then solubilized by adding sterile or bacteriostatic water slowly down the inner vial wall. The vial is swirled gently or left to dissolve passively (never shaken) until the solution is clear; vortexing, sonication, and foaming are avoided because mechanical shear and large air–liquid interfaces can denature small peptides and drive surface adsorption losses. Diluent choice is recorded, since bacteriostatic preservatives and pH both influence how long the reconstituted reference solution remains usable on the bench.
Concentration
Working concentrations in the literature are calculated against the labeled net peptide mass rather than gross fill weight, because lyophilizates contain counter-ions, salts, and residual moisture that inflate apparent mass. The reconstitution volume is chosen so that the smallest aliquot the assay requires is still accurately pipettable, and concentration is expressed in molar terms when receptor-occupancy or potency comparisons are the experimental goal. Serial dilutions are prepared in low-binding tubes to limit peptide loss to plasticware.
Storage
Lyophilized material is reported to be most stable when kept desiccated, frozen (commonly −20 °C or colder for long-term, with −80 °C used for extended archival), and shielded from light. Once reconstituted, aqueous peptide is typically refrigerated at 2–8 °C and used within a short window; handling protocols recommend dividing the stock into single-use aliquots immediately after reconstitution so that the working material is never subjected to repeated freeze–thaw cycles, each of which can fragment or aggregate sensitive peptides and proteins.
Sterility & Records
Aseptic technique, single-use sterile needles and filters, clean-bench preparation, and logged lot, diluent, concentration, and date documentation are standard laboratory practice for reference standards. Carryover between unrelated compounds is avoided, and chain-of-custody notes accompany the vial. None of these handling notes describe, recommend, or imply administration to humans or animals; they pertain solely to in-vitro experimentation and analytical reference use by trained personnel.
Identity & Purity
Before a peptide reference standard is used in quantitative work, identity and purity are typically confirmed by analytical methods such as reversed-phase HPLC for purity and mass spectrometry for molecular-weight confirmation, with the certificate of analysis retained alongside the lot record. Verifying that the observed mass matches the theoretical mass for the intended sequence guards against truncated, oxidized, or mis-synthesized material that would confound downstream assays.
Quality-Control Notes
Visual inspection for clarity and the absence of particulates after reconstitution, confirmation that the powder fully dissolved without persistent haze, and consistency of behavior across lots are routine quality checks. Any deviation — discoloration, incomplete dissolution, or unexpected odor — is treated as a reason to set the material aside rather than risk corrupting an experiment. Where quantitative results depend on exact peptide content, an independent content assay against a characterized reference is preferred over relying on the label mass alone.
Disposal & Containment
Unused reconstituted solution, expired stock, and contaminated consumables are disposed of as laboratory waste in accordance with institutional and local regulations rather than being retained indefinitely. Work surfaces are decontaminated after use, and personal protective equipment appropriate to handling research biochemicals is worn throughout. These containment practices reinforce that the material is intended for a controlled laboratory workflow and nowhere else.
Stability & Half-Life Notes
The defining stability feature of the DAC form is covalent capture by serum albumin, which in published pharmacokinetic work translates into a substantially longer functional duration than non-DAC GHRH fragments — on the order of days rather than the minutes characteristic of native GHRH.[1] That extended in-vivo persistence is a property of the albumin-bound complex in circulation and is distinct from the chemical shelf-stability of the dry reagent: as a lyophilizate the peptide is still handled like other GHRH-analog reference standards, kept cold and desiccated, with reconstituted material regarded as time-limited, refrigerated, and aliquoted to avoid freeze–thaw damage.
Research Use Only — Not For Human Use
This material and all information presented here are provided strictly for in-vitro laboratory research and analytical reference. CJC-1295 with DAC is not a drug, dietary supplement, food, cosmetic, or medical device; it has not been evaluated or approved by any regulatory authority for the diagnosis, treatment, cure, or prevention of any condition; and it is not approved for human or veterinary use. Nothing in this overview is medical advice, a therapeutic claim, or any suggestion, instruction, or encouragement for use in or on the body of a human or animal. Every study summarized above was conducted by the cited investigators in controlled research or clinical-trial settings and is reported here only to document what exists in the peer-reviewed literature. Handling is restricted to qualified personnel operating in an appropriate research environment and in accordance with all applicable laws and institutional policies. By accessing this material the user accepts sole responsibility for its lawful, research-only use.
References
- Teichman SL, Ball SA, Sferruzzi G, et al. 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. J Clin Endocrinol Metab. 2006. PMID: 16352683
- Ionescu M, Frohman LA. Pulsatile secretion of growth hormone (GH) persists during continuous stimulation by CJC-1295, a long-acting GH-releasing hormone analog. J Clin Endocrinol Metab. 2006. PMID: 17018654
- Sackmann-Sala L, Ding J, Frohman LA, Kopchick JJ. Activation of the GH/IGF-1 axis by CJC-1295, a long-acting GHRH analog, results in serum protein profile changes in normal adult subjects. Growth Horm IGF Res. 2009. PMID: 19386527
- Grossman A. Growth hormone releasing hormone. Clin Endocrinol Metab. 1986. PMID: 2429796
- Camanni F, Ghigo E, Arvat E. Growth hormone-releasing peptides and their analogs. Front Neuroendocrinol. 1998. PMID: 9465289
Scientific References
Explore the published research literature on CJC-1295 (DAC). We link directly to independent, primary sources — we don't summarize or interpret findings. For research use only.
Links open external databases (pubmed.ncbi.nlm.nih.gov · clinicaltrials.gov). Banger Labs is not affiliated with these sources. For research use only — not medical advice.
Certificate of Analysis
CJC-1295 (DAC) · ≥99.4% purity (HPLC)