CJC-1295 (No DAC) is a growth hormone-releasing hormone (GHRH) analog studied for its ability to stimulate pulsatile growth hormone release through selective activation of the GHRH receptor. Its relatively short duration of activity makes it useful for research into GH secretion dynamics, receptor signaling, and combination secretagogue models.

CJC-1295 (No DAC) is a synthetic analog of the first 29 amino acids of growth hormone-releasing hormone (GHRH), the minimal sequence required for full biological activity at the GHRH receptor. It is commonly referred to in research literature and peptide research contexts as Modified GRF (1-29).

Unlike DAC-containing CJC-1295, the No DAC form does not contain the Drug Affinity Complex designed for covalent albumin binding and prolonged systemic exposure. This distinction gives CJC-1295 (No DAC) a substantially shorter duration of activity and makes it particularly relevant to research involving transient GHRHR activation and pulsatile GH secretion.

The peptide incorporates amino-acid substitutions intended to improve resistance to enzymatic degradation relative to native GRF (1-29). Native GHRH fragments are rapidly degraded by dipeptidyl peptidase IV (DPP-IV), whereas the modified sequence provides greater stability while retaining potent GHRH receptor agonist activity.

CJC-1295 (No DAC) is also frequently investigated alongside growth hormone secretagogues that act through GHS-R1a, such as Ipamorelin. Because GHRHR and GHS-R1a activate distinct intracellular signaling pathways within pituitary somatotrophs, simultaneous activation can produce greater GH release than either pathway alone in experimental systems. This makes CJC-1295 (No DAC) valuable for studying receptor cross-talk, secretagogue synergy, and GH-axis signaling.

• CAS Number: 446036-97-1
• Molecular Weight: ~3367.9 g/mol
• Purity: ≥99%
• Also Known As: Modified GRF (1-29), Mod GRF 1-29, CJC-1295 without DAC
• Chemical Formula: C₁₅₂H₂₅₂N₄₄O₄₂

In cell-based and preclinical models, CJC-1295 (No DAC) acts as an agonist at the growth hormone-releasing hormone receptor (GHRHR), a Gs-coupled G protein-coupled receptor expressed prominently on anterior pituitary somatotroph cells.

GHRHR activation stimulates adenylyl cyclase, increasing intracellular cyclic AMP (cAMP) and activating protein kinase A (PKA). This signaling cascade promotes calcium-dependent exocytosis of stored growth hormone while also influencing pathways involved in GH synthesis and somatotroph function.

This mechanism is distinct from that of GHS-R1a agonists such as Ipamorelin, which primarily engage Gq/11-mediated phospholipase C and intracellular calcium signaling. The complementary signaling pathways provide the mechanistic basis for studying CJC-1295 (No DAC) and GHS-R1a agonists together in dual-secretagogue experimental models.

Because the No DAC form lacks the albumin-binding Drug Affinity Complex found in long-acting CJC-1295, its receptor activation is comparatively transient. This characteristic makes it particularly useful for investigating short-duration GHRHR stimulation, GH pulse dynamics, and the relationship between secretagogue exposure and pulsatile endocrine signaling.

• GHRH Receptor Activation and Binding Studies
• GH Secretion and Somatotroph Signaling Research
• Pulsatile Growth Hormone Release Modeling
• GHRH Analog Stability and Degradation Studies
• cAMP/PKA Signaling Pathway Research
• Dual-Secretagogue Combination Studies
• GHRHR and GHS-R1a Signaling Synergy Research
• Growth Hormone Axis Pharmacology and Comparative Peptide Research