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CJC No DACGHRHGH SecretagoguesGrowth Hormone Releasing HormoneResearch Peptides

CJC No DAC: Molecular Structure, GHRH Receptor Pharmacology, and Research Overview

AminoLine Research Team·June 27, 2026·7 min read

What is CJC No DAC?

CJC No DAC is a synthetic peptide studied in research as an analog of growth hormone-releasing hormone (GHRH). It corresponds to the 29-amino-acid bioactive N-terminal region of native GHRH and is catalogued under CAS number 446036-97-1 with a molecular formula of C₁₅₂H₂₅₂N₄₄O₄₂ and a molecular weight of 3367.9 g/mol. The compound is supplied as a lyophilized powder and is intended solely for laboratory research purposes, not for human use.

In the GHRH analog literature, CJC No DAC occupies a defined position: it is the structurally minimal form in the CJC series, without the Drug Affinity Complex (DAC) modification that characterizes CJC-1295. This makes it a research probe for GHRH receptor activity in its shorter-circulating form, studied in contrast to DAC-containing analogs that exhibit a different pharmacokinetic profile. Understanding what the absence of the DAC modification means — structurally and in terms of research application — is central to interpreting the compound correctly.

What is the molecular structure of CJC No DAC?

CJC No DAC has a molecular weight of 3367.9 g/mol and the molecular formula C₁₅₂H₂₅₂N₄₄O₄₂. It is a 29-amino-acid peptide corresponding to the N-terminal sequence of native GHRH(1-44), which represents the bioactive region responsible for GHRH receptor binding and activation. The native GHRH sequence contains 44 amino acids, but the first 29 are sufficient for receptor binding, and synthetic analogs based on this region are characterized throughout the research literature.

Unlike CJC-1295, which appends a maleimidoproprionic acid-Lys(DAC) modification to enable covalent albumin binding, CJC No DAC carries no such modification. The peptide chain is the primary structural feature, without additional lipidation or reactive group attachment. This structural simplicity is also the reason its circulating half-life in research model systems differs markedly from DAC-containing analogs. The compound is produced through solid-phase peptide synthesis followed by purification and is held to a purity specification of 99.0% by HPLC, supplied as a white to off-white lyophilized powder.

How does CJC No DAC interact with the GHRH receptor?

The GHRH receptor is a class B G-protein-coupled receptor expressed primarily in anterior pituitary tissue in studied model systems. Class B GPCRs are characterized by a long extracellular N-terminal domain that participates directly in ligand recognition, and the GHRH receptor follows this structural pattern. CJC No DAC, as a synthetic GHRH(1-29) analog, engages the receptor through the same N-terminal binding interaction characterized for native GHRH.

Receptor activation by GHRH-class peptides triggers intracellular cAMP accumulation through Gαs coupling. This cAMP-mediated signaling cascade is the primary pathway studied in GHRH receptor agonist research. In somatotroph cell models, cAMP elevation is associated with the downstream signaling events that characterize the GHRH receptor's studied role in GH regulation research.

Concentration-response studies with CJC No DAC and related GHRH analogs characterize binding affinity (measured as the concentration required to produce half-maximal receptor activation, EC50) and the degree of receptor activation at different concentration points. These parameters are the primary outputs of GHRH receptor pharmacology research and determine how a given analog is positioned within the broader compound series.

How does CJC No DAC differ from CJC-1295 with DAC?

The defining structural difference is the presence or absence of the Drug Affinity Complex. CJC-1295 with DAC incorporates a lysine-linked maleimidoproprionic acid group that reacts with cysteine residues on circulating albumin, creating a covalent albumin-bound form of the peptide. This albumin binding is studied for its effect on circulating stability: bound peptide is not cleared at the same rate as free peptide, producing an extended half-life in the research model system.

CJC No DAC has no albumin-binding modification. It circulates in its free form, which subjects it to enzymatic cleavage — principally by dipeptidyl peptidase IV (DPP-IV), which cleaves the N-terminal Tyr-Ala bond present in GHRH sequences. The resulting pharmacokinetic profile in research systems is significantly shorter than DAC-containing analogs.

Property CJC No DAC CJC-1295 with DAC
CAS 446036-97-1 863288-34-0
Molecular weight 3367.9 g/mol 3647.28 g/mol
Formula C₁₅₂H₂₅₂N₄₄O₄₂
Albumin binding None Covalent via maleimide-DAC
Half-life profile in models Short (free peptide) Extended (albumin-bound)
Research application Pulsatile GHRH receptor studies Sustained receptor occupation studies

This difference in half-life profile is why the two analogs serve different research applications. CJC No DAC is the appropriate compound when research design calls for studying transient or pulsatile GHRH receptor activation; CJC-1295 with DAC is studied when sustained receptor occupation and extended kinetic windows are the focus. The two are not interchangeable, and substituting one for the other alters the experimental parameter being measured.

What does published research describe about CJC No DAC's pharmacokinetics in model systems?

Published research characterizes the half-life of unmodified GHRH(1-29) analogs as short in plasma, owing to DPP-IV-mediated N-terminal cleavage. The DPP-IV cleavage site at the Tyr-Ala N-terminus is the primary enzymatic vulnerability in this compound class, and the relationship between N-terminal structural modification and DPP-IV resistance has been extensively characterized across the GHRH analog series.

For CJC No DAC, the research literature uses it as a shorter-acting reference probe: its rapid clearance from the experimental system provides a defined kinetic window for studying acute GHRH receptor activation and the corresponding downstream signaling response. The contrast with longer-acting analogs — DAC-containing, or Tesamorelin with its N-terminal trans-3-hexenoic acid modification — provides the comparative data that characterizes the kinetic dimension of GHRH receptor pharmacology.

Concentration-response characterization of CJC No DAC at the GHRH receptor has been reported in in vitro receptor binding and cell-based activation assays. These studies establish the compound's EC50 and maximal efficacy (Emax) at the receptor — parameters used to position it relative to other analogs and to native GHRH. AminoLine does not make therapeutic or outcome claims regarding CJC No DAC; the compound is studied strictly at the level of receptor pharmacology in laboratory models.

How should CJC No DAC be stored and handled for research?

CJC No DAC is supplied as a lyophilized powder and is stored at −20°C to preserve structural integrity. As a peptide without albumin-binding modifications, it is sensitive to elevated temperatures, repeated freeze-thaw cycles, oxidation, and moisture. Research handling practices that protect reproducibility include maintaining cold storage throughout the experimental lifecycle, minimizing freeze-thaw exposure, and keeping the lyophilized material sealed against humidity.

The DPP-IV susceptibility that characterizes this compound class in plasma extends to degradation under suboptimal storage conditions: an intact N-terminal sequence is required for GHRH receptor binding, and any structural modification at the N-terminus alters the receptor interaction being studied. Compound integrity at the point of use depends on the integrity of the handling chain from manufacture through delivery.

Cold-chain shipping is relevant for the same reason. AminoLine ships all peptide compounds with cold-chain packaging as standard. This article does not provide preparation or reconstitution instructions; handling protocols are the researcher's responsibility and should be determined by experimental requirements and applicable regulations.

How does AminoLine source CJC No DAC?

AminoLine supplies CJC No DAC as a research-grade compound characterized to a purity specification of 99.0% by HPLC, with mass spectrometry identity confirmation. Every order ships with a batch-specific Certificate of Analysis, and all shipments are cold-chain packaged as standard. Operations are US-based.

Researchers can review specifications, available sizes, and pricing on the CJC No DAC product page. The full GH secretagogue catalog — including Ipamorelin, Sermorelin Acetate, Tesamorelin, and the CJC/IPA blend — is available at all compounds. For a broader overview of the GHRH and ghrelin receptor agonist research landscape, see GH Secretagogue Research Peptides: Category Overview. All material is for laboratory research use only and is not for human use.


This compound is a research chemical intended for laboratory and scientific research purposes only. It is not a drug, supplement, or food, and is not intended to diagnose, treat, cure, or prevent any disease. AminoLine does not sell products intended for human use. Researchers are responsible for compliance with all applicable local, state, and federal regulations.

AminoLine Research Team

Peptide Research Specialists

Specializing in GH secretagogue receptor pharmacology and growth hormone-releasing hormone analog research.