CJC-1295 With DAC

CJC-1295 With DAC is a synthetic 30-residue analog of growth-hormone-releasing hormone (GHRH) engineered with a Drug Affinity Complex (DAC) modification. The DAC component is a maleimidopropionic acid (MPA) linker attached at the C-terminal lysine, which forms a covalent bond with a free cysteine residue on circulating serum albumin in research models. This albumin-bioconjugate design extends plasma residency from minutes for native GHRH(1-29) to several days in laboratory species, making CJC-1295 With DAC an investigational laboratory peptide for GHRH-receptor signaling research and somatotropic-axis research models.

Laboratory research studies have positioned CJC-1295 With DAC as a reference compound for examining sustained engagement of GHRH receptors on pituitary somatotroph cells. Research models have characterized its binding kinetics, downstream adenylyl-cyclase and cyclic-AMP signaling, and the resulting modulation of growth-hormone-pathway investigation, providing comparative data versus shorter-acting GHRH analogs such as sermorelin and Mod GRF (1-29) (Jetté et al., 2005, Endocrinology).

Beyond pituitary receptor pharmacology, CJC-1295 With DAC is investigated in cellular and animal research models that explore somatotropic-axis signal transduction, hepatic IGF-1 expression research, hypothalamic-pituitary feedback regulation, and age-associated changes in GHRH-receptor responsiveness. The peptide's albumin-binding side chain is also a frequent subject of pharmacokinetics and protein-binding research, including comparative studies versus non-acylated GHRH(1-29) analogs.

The peptide is supplied as a lyophilized powder to ensure optimal stability during storage and handling.

Growth-hormone-releasing hormone is a 44-residue hypothalamic peptide that engages the GHRH receptor, a class B G-protein-coupled receptor expressed on pituitary somatotroph cells, and participates in growth-hormone-pathway investigation. For many years, research on GHRH analogs was limited by the very short plasma half-life of native GHRH(1-29), which is rapidly inactivated by dipeptidyl peptidase-IV (DPP-IV) cleavage and other proteolytic mechanisms. This kinetic limitation constrained laboratory investigations of sustained somatotropic-axis signaling and motivated the design of structurally modified analogs with improved plasma stability.

CJC-1295 With DAC was developed as a synthetic GHRH(1-29) analog incorporating four amino-acid substitutions (D-Ala², Gln⁸, Ala¹⁵, Leu²⁷) that confer resistance to proteolytic degradation, together with a C-terminal lysine bearing a maleimidopropionic acid (MPA) Drug Affinity Complex. The MPA group reacts selectively with the free cysteine-34 residue of serum albumin to form a stable covalent bioconjugate in research models, anchoring the peptide to a circulating carrier protein.

This dual structural strategy, sequence stabilization combined with albumin bioconjugation, has made CJC-1295 With DAC a widely studied reference compound for laboratory investigations of GHRH-receptor signaling kinetics, prolonged somatotropic-axis engagement, hepatic IGF-1 expression dynamics, and pharmacokinetic modeling of acylated peptide analogs. Research interest spans pituitary somatotroph signaling models, endocrine feedback research, and comparative pharmacology versus non-DAC GHRH analogs.

Synonyms: CJC-1295 (DAC-conjugated), DAC:GRF

1. GHRH-Receptor Engagement on Pituitary Somatotrophs

CJC-1295 With DAC engages the GHRH receptor on pituitary somatotroph cells, a class B G-protein-coupled receptor. Research models indicate that this engagement modulates Gαs-coupled signaling and adenylyl-cyclase activity, producing intracellular responses that have been compared with native GHRH(1-29) in laboratory studies (Jetté et al., 2005, Endocrinology).

2. Modulation of Cyclic AMP and Downstream Kinases

Upon receptor engagement, CJC-1295 With DAC modulates intracellular cyclic AMP accumulation. Downstream, this is associated with protein kinase A activation and CREB-mediated transcription, both of which are extensively studied in somatotropic-axis research as upstream regulators of growth-hormone gene expression in pituitary somatotroph models.

3. Albumin Bioconjugation and Extended Plasma Residency

The Nε-maleimidopropionyl-lysine modification enables covalent binding to the free cysteine-34 residue of serum albumin in research models. This structural feature is investigated in pharmacokinetics research as the basis for the peptide's extended plasma residency in laboratory species and is a frequent subject of comparative research versus non-acylated GHRH analogs.

4. Preserved Pulsatile Signaling Pattern

Laboratory research studies have characterized CJC-1295 With DAC as engaging the GHRH receptor in a manner that preserves the underlying pulsatile pattern of growth-hormone secretion in research models, rather than producing constant tonic stimulation. This pulsatile-preservation profile is an active area of structure-activity research.

Research Applications

Conclusion

CJC-1295 With DAC represents a structurally engineered GHRH(1-29) analog that has become a reference compound in somatotropic-axis research. Its combination of sequence-level stabilization (four amino-acid substitutions) and albumin bioconjugation through a maleimidopropionyl linker makes it a valuable investigational laboratory peptide for studying class B G-protein-coupled receptor pharmacology, growth-hormone-pathway investigation, and extended-residency peptide design.

Research Use Disclaimer

This product is intended for research and laboratory use only. It is designed exclusively for in vitro research purposes. All information provided is for educational and research reference only. This product is not intended for human or animal use. It is not a drug, food, or cosmetic and must not be marketed, labeled, or used as such. Use and handling are restricted to trained and qualified professionals.