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SAGA
Research Library
07

CJC-1295 (NO DAC)

All information below is drawn from preclinical research literature and is provided for educational and informational purposes only. It does not constitute medical advice, imply therapeutic outcomes, or endorse any specific application.

Chemical Identification

Property

Value

CAS Number446033-06-3
PubChem CID91971820
ClassificationModified Growth Hormone-Releasing Hormone (GHRH) analog
Molecular FormulaC165H269N47O46

Reference Studies

Overview

General Research Context

CJC-1295 (NO DAC) is a synthetic tetrasubstituted analogue of endogenous Growth Hormone-Releasing Hormone (GHRH). It is utilized in neuroendocrine research to study receptor binding kinetics within the anterior pituitary gland and to examine the somatotropic axis in preclinical models.

The "NO DAC" designation indicates that this molecular variant lacks the maleimidopropionic acid moiety found in standard CJC-1295 that is designed to covalently bind to blood albumin.

Areas of Investigation

Observed Interactions and Background

Endogenous GHRH possesses a short biological half-life, which limits its utility in prolonged in vitro observation. CJC-1295 (NO DAC) was designed with four amino acid substitutions intended to reduce susceptibility to dipeptidyl peptidase-4 (DPP-4) enzymatic cleavage.

In laboratory assays, the compound has been observed to bind to GHRH receptors on isolated somatotroph cells, engaging the cyclic AMP (cAMP) second messenger system. Because it lacks the DAC modification, its pharmacokinetic profile in animal models differs from albumin-bound CJC-1295 variants. These observations are derived from preclinical research settings.

Laboratory Notes

Synthesis and Stability Notes

Manufactured via standard continuous-flow or advanced microwave-assisted SPPS, the synthesis is relatively straightforward despite its length. The lack of the highly reactive DAC moiety significantly simplifies the RP-HPLC purification process and prevents unwanted chemical dimerization or rapid degradation during the final lyophilization phase. Standard laboratory reconstitution protocols utilizing bacteriostatic water at cold temperatures are strictly required to maintain the fragile secondary alpha-helical structure of the peptide.

Disclaimer: All information provided herein is strictly for educational and laboratory research reference purposes only. Saga does not endorse, interpret, or evaluate these preclinical studies for any specific in vivo application or human therapeutic outcome.

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