Research Spotlight

CJC-1295 without DAC: Research Overview

PūrTONIX Analytical TeamMarch 11, 20253 min read

Research Use Only — Regulatory Notice

All information contained in this article is derived exclusively from publicly available scientific literature, peer-reviewed academic publications, and publicly accessible research databases. This content is provided strictly for educational and informational purposes in the context of laboratory research.

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This article does not constitute medical advice. These compounds are sold by PūrTONIX strictly as laboratory research reagents for in vitro use only. They are not intended for human or veterinary administration, dietary supplementation, or any therapeutic application.

All citations reference publicly available research. PūrTONIX makes no representations regarding the replication, accuracy, or applicability of any referenced study.

Compound Overview

Full name: Modified GHRH(1-29) analog with Aib substitutions at positions 2, 8, 15, and 27 (without Drug Affinity Complex maleimide)
Molecular formula: C152H252N44O42
Molecular weight: 3367.93 g/mol
Sequence / class: 30-residue tetra-substituted GHRH(1-29) analog incorporating four aminoisobutyric-acid residues at positions 2, 8, 15, and 27
Receptor targets: Growth hormone-releasing hormone receptor (GHRHR), a class B G-protein-coupled receptor coupled to Gαs and cAMP/PKA signaling
Research classification: GHRH receptor analog research peptide without the C-terminal Drug Affinity Complex maleimide moiety
PubChem CID: 16133850

CJC-1295 without DAC is a modified GHRH(1-29) analog that carries four aminoisobutyric-acid (Aib) substitutions at positions 2, 8, 15, and 27 of the parent sequence. The compound does not carry the C-terminal maleimide moiety (Drug Affinity Complex, or DAC) that distinguishes the longer-acting variant of the molecule. The molecular formula is C152H252N44O42 with a calculated mass near 3368 daltons. The C-terminus carries a primary amide.

Published literature classifies CJC-1295 without DAC as a GHRH receptor analog research peptide. The Aib substitutions stabilize the molecule against dipeptidyl-peptidase-4 cleavage and against enzymatic degradation at several internal positions in published in vitro biochemistry studies, while the absence of the DAC maleimide produces a shorter functional half-life compared with the DAC-modified variant.

Research published in the peer-reviewed literature has used CJC-1295 without DAC as an analytical reference compound in studies of GHRHR pharmacology. The compound engages the GHRH receptor, a class B G-protein-coupled receptor coupled to Gαs, with downstream cAMP accumulation and PKA-cascade activation in cellular reporter systems.

The shorter functional half-life relative to the DAC-modified variant has made CJC-1295 without DAC a useful comparator in time-resolved in vitro signaling studies, where investigators have characterized desensitization kinetics, receptor internalization biochemistry, and the temporal pattern of intracellular cAMP responses under matched analytical conditions.

Molecular Structure

CJC-1295 without DAC

C152H252N44O42

Molecular weight 3367.93 g/mol

Structure reference: Public domain chemical databases (PubChem CID 16133850).

In Vitro Research Applications

The following applications reflect published in vitro and preclinical research only. None of these applications constitute approved medical use.

Published in vitro applications of CJC-1295 without DAC include its use as a reference agonist in GHRHR reporter cell lines, primary pituitary cell preparations from published animal research, and cAMP-accumulation assays that read out the proximal Gαs signaling event. Investigators have used the peptide to characterize EC50 values and signaling kinetics under defined cellular assay conditions.

Comparative in vitro literature has paired CJC-1295 without DAC with the DAC-modified variant to characterize how the C-terminal maleimide moiety influences functional half-life and signaling-cascade kinetics in cellular models. Side-by-side panels with native GHRH and with tesamorelin provide additional analytical context for receptor-engagement studies.

Co-administration in vitro panels with selective ghrelin-receptor pentapeptides such as ipamorelin have appeared in published research that examines dual GHRH/GHS-R1a receptor signaling in cellular reporter systems under matched conditions.

Published Research Highlights

[1]A study published in Endocrinology (2005) examined GHRH analog biochemistry and the role of Aib substitutions in stabilizing GHRH(1-29) sequences in publicly available in vitro studies.
[2]A study published in Journal of Endocrinology (2008) investigated the cAMP signaling kinetics of modified GHRH analogs in pituitary cell reporter systems.
[3]A study published in Peptides (2011) reviewed publicly available literature on tetra-substituted GHRH(1-29) research peptides and their in vitro receptor pharmacology.

The above represents a non-exhaustive summary of publicly available research. PūrTONIX does not endorse, validate, or make claims based on any referenced study.

Analytical Considerations for Laboratory Use

Published chemical property data indicate that CJC-1295 without DAC is soluble in water and in standard aqueous assay buffers. The lyophilized peptide is stored at -20°C under inert atmosphere with reconstituted stocks held in single-use aliquots. The Aib substitutions confer enhanced stability against dipeptidyl-peptidase-4 cleavage in cellular media compared with native GHRH(1-29).

Reconstitution in bacteriostatic water or in assay-matched buffer is standard for GHRHR pharmacology assays. Analytical characterization commonly includes reverse-phase HPLC purity analysis, electrospray mass spectrometry confirming the 30-residue sequence with intact Aib substitutions, and residual solvent screening per ICH Q3C.

Handling recommendations are based on published chemical property data and are intended for qualified laboratory personnel only.

Research-Grade Sourcing Standards

GHRHR cAMP assays at sub-nanomolar agonist concentrations depend on high chromatographic purity to resolve cleanly. Mass-spectral data confirming intact Aib substitutions at positions 2, 8, 15, and 27 are typically reported in analytical documentation for this compound.

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