CJC-1295 No DAC 10 mg

CJC-1295 No DAC, also known as Modified GRF (1-29) or Mod GRF (1-29), is a synthetic 29-residue analog of growth-hormone-releasing hormone (GHRH) engineered without the Drug Affinity Complex (DAC) albumin-binding linker found in the DAC-conjugated variant. The peptide incorporates four amino-acid substitutions (D-Ala², Gln⁸, Ala¹⁵, Leu²⁷) on the GHRH(1-29) backbone that confer enhanced enzymatic stability against dipeptidyl peptidase-IV (DPP-IV) cleavage and other proteolytic mechanisms in research models. It is supplied as an investigational laboratory peptide for GHRH-receptor signaling research and somatotropic-axis research models that require a shorter, pulse-preserving plasma residency profile distinct from the DAC-conjugated analog.

Laboratory research studies have positioned CJC-1295 No DAC as a reference compound for examining pulsatile engagement of GHRH receptors on pituitary somatotroph cells. Research models have characterized its receptor binding kinetics, downstream adenylyl-cyclase and cyclic-AMP signaling, and the resulting modulation of growth-hormone-pathway investigation, with particular interest in how the absence of albumin bioconjugation produces a shorter residency window that more closely approximates the native pulsatile GHRH signaling pattern (Ionescu & Frohman, 2006, Journal of Clinical Endocrinology & Metabolism).

Beyond pituitary receptor pharmacology, CJC-1295 No DAC is investigated in cellular and animal research models that explore somatotropic-axis signal transduction, hypothalamic-pituitary feedback regulation, hepatic IGF-1 expression research, and comparative pharmacokinetics versus DAC-conjugated GHRH analogs. The four-substitution stabilization strategy without albumin tethering is also a frequent subject of structure-activity research on GHRH analog design.

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

Growth-hormone-releasing hormone is a 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. Native GHRH(1-29), also known as sermorelin, retains full receptor engagement in research models but is rapidly inactivated by dipeptidyl peptidase-IV (DPP-IV) cleavage at the N-terminal Tyr-Ala bond and by other proteolytic mechanisms, producing a plasma residency window of only a few minutes. This kinetic constraint limited laboratory investigations of GHRH-receptor signaling dynamics and motivated the design of sequence-stabilized analogs.

CJC-1295 No DAC was developed as a synthetic GHRH(1-29) analog incorporating four amino-acid substitutions: D-Ala at position 2 (DPP-IV resistance), Gln at position 8 (asparagine-rearrangement resistance), Ala at position 15 (enhanced receptor engagement), and Leu at position 27 (methionine-oxidation resistance). Unlike the DAC-conjugated variant, CJC-1295 No DAC lacks the C-terminal maleimidopropionyl-lysine albumin-binding linker, producing a plasma residency window of approximately 30 minutes, substantially longer than native GHRH(1-29) but much shorter than the multi-day window of the DAC-conjugated analog.

This intermediate-residency profile has made CJC-1295 No DAC a widely studied reference compound for laboratory investigations of pulsatile GHRH-receptor engagement, somatotropic-axis pulse-amplitude research, and comparative pharmacology versus both native GHRH(1-29) and the DAC-conjugated analog. Research interest spans pituitary somatotroph signaling models, hypothalamic-pituitary feedback research, and structure-activity studies on GHRH analog design.

CJC-1295 No DAC Structure

1. GHRH-Receptor Engagement on Pituitary Somatotrophs

CJC-1295 No 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 comparable to native GHRH(1-29) but with extended plasma residency due to the sequence-level modifications (Ionescu & Frohman, 2006, JCEM).

2. Modulation of Cyclic AMP and Downstream Kinases

Upon receptor engagement, CJC-1295 No 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. Sequence-Stabilized Plasma Residency

The four amino-acid substitutions confer resistance to DPP-IV cleavage and other proteolytic mechanisms, extending plasma residency from minutes for native GHRH(1-29) to approximately 30 minutes in research models, without the multi-day extension produced by albumin bioconjugation in the DAC-conjugated variant.

4. Pulsatile-Preserving Signaling Pattern

Laboratory research studies have characterized CJC-1295 No DAC as engaging the GHRH receptor in a manner that produces discrete pulse-amplitude signaling in research models, rather than the prolonged tonic engagement profile of the DAC-conjugated analog. This pulse-preserving profile is an active area of structure-activity research and is investigated as a contributor to comparative somatotropic-axis dynamics versus longer-residency analogs.

Research Applications

Conclusion

CJC-1295 No DAC represents a sequence-stabilized GHRH(1-29) analog that occupies an intermediate-residency position between native GHRH(1-29) and the DAC-conjugated variant. Its four amino-acid substitutions confer resistance to proteolytic degradation without the multi-day extension of albumin bioconjugation, making it a valuable investigational laboratory peptide for studying pulsatile GHRH-receptor engagement, somatotropic-axis pulse dynamics, and structure-activity relationships in GHRH analog 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.