
CJC-1295 (No DAC)
Research Peptide | Lyophilized Powder | Batch Tested
For laboratory research use only. Not for human or animal consumption. Insulated shipping · Styrofoam box available.
Product Overview
CJC-1295 (No DAC), also known as Modified GRF (1-29), is a short-acting GHRH analog with amino-acid substitutions that improve its stability over native GHRH while keeping a brief, pulse-like duration of action. It is a staple of growth-hormone-axis research.
| Test | Result | Status |
|---|---|---|
| Purity | 98.87% | Passed ✓ |
| Weight | 10.13mg | Passed ✓ |
| Test | Result | Status |
|---|---|---|
| Purity | 99.0% | Passed ✓ |
| Test | Result | Status |
|---|---|---|
| Purity | 99.0% | Passed ✓ |
| Test | Result | Status |
|---|---|---|
| Purity | 99.2% | Passed ✓ |
Research Information
This analog is studied for GHRH-receptor activation that produces discrete GH pulses in laboratory models. It is very commonly combined with a ghrelin-receptor agonist such as Ipamorelin so researchers can study the amplified, synergistic GH release produced by stimulating both pathways at once. Supplied strictly for in-vitro and laboratory research use only — not for human or animal consumption.
CJC-1295 (No DAC) Research & Studies
What is CJC-1295 (No DAC)?
CJC-1295 (No DAC), also designated Modified GRF (1-29), is a synthetic tetracosapeptide analog of growth-hormone-releasing hormone (GHRH). Amino-acid substitutions at selected positions enhance resistance to enzymatic degradation relative to native GHRH(1-29) while preserving a short plasma half-life that yields discrete, pulse-like receptor stimulation. The compound is supplied exclusively for controlled laboratory investigation of the growth-hormone axis and is not intended for any form of administration outside research settings.
Mechanism of Action
In experimental systems, CJC-1295 (No DAC) binds the GHRH receptor (GHRHR) expressed on somatotroph cells, activating Gs-protein-coupled adenylate-cyclase signaling and elevating intracellular cyclic AMP. The resulting cascade promotes transcription and acute release of growth hormone (GH) in a pattern that closely mimics endogenous pulsatile secretion. Because the analog lacks a drug-affinity complex (DAC) moiety, its receptor occupancy remains brief, allowing researchers to isolate the effects of short-duration GHRH-receptor engagement.
Primary Areas of Research
Laboratory studies focus on the peptide’s capacity to elicit discrete GH pulses in cell-culture and isolated-tissue models of the hypothalamic-pituitary axis. Investigators also examine co-administration with ghrelin-receptor agonists such as Ipamorelin to characterize synergistic amplification of GH release through simultaneous activation of GHRH and GH secretagogue pathways. Additional work explores receptor desensitization kinetics, second-messenger dynamics, and downstream IGF-1 gene expression under tightly controlled in-vitro conditions.
Key Research Findings
Published in-vitro and ex-vivo data indicate that Modified GRF (1-29) retains high binding affinity for the GHRH receptor while exhibiting improved proteolytic stability compared with the native sequence. When applied in pulse protocols, the analog produces measurable GH secretion peaks without sustained receptor occupancy. Combination experiments with Ipamorelin consistently demonstrate greater GH output than either ligand alone, supporting the utility of dual-pathway stimulation models for dissecting GH-axis regulation.
Research Handling & Considerations
CJC-1295 (No DAC) is typically supplied as a lyophilized powder requiring reconstitution in sterile bacteriostatic water or appropriate buffer under aseptic laboratory conditions. Solutions should be aliquoted and stored at recommended low temperatures to minimize freeze-thaw degradation. All experimental use must remain confined to qualified research facilities; the material is strictly designated for in-vitro and laboratory investigation and is not for human or animal consumption.
Frequently Asked Questions
“No DAC” indicates the absence of a Drug Affinity Complex moiety, resulting in a short-acting profile that produces brief GHRH-receptor stimulation rather than prolonged exposure.
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