CJC-1295 No DAC Research Peptide
Peptora Compound Research Library
CJC-1295 No DAC Research Peptide Overview
CJC-1295 No DAC Research Peptide is a name widely used for Modified GRF (1-29), a synthetic 29-amino-acid analogue related to the biologically active N-terminal region of growth hormone-releasing hormone (GHRH). Research surrounding this peptide family examines GHRH-receptor signalling, pituitary growth-hormone release and the structural changes used to improve resistance to peptide degradation.
Compound overview
What Is CJC-1295 No DAC Research Peptide?
CJC-1295 No DAC is commonly used as a commercial name for Modified GRF (1-29), also written Mod GRF 1-29.
The peptide is based on the first 29 amino acids of growth hormone-releasing hormone, historically also called growth hormone-releasing factor or GRF. This N-terminal region contains the biological activity required for interaction with the GHRH receptor.
Modified GRF (1-29) introduces amino-acid substitutions into this 29-residue framework to increase resistance to enzymatic degradation while retaining GHRH-receptor activity.
The Naming Distinction Matters
Modified GRF (1-29): a modified 29-amino-acid GHRH-related peptide lacking an albumin-binding Drug Affinity Complex.
CJC-1295 No DAC: the name widely used in the research-material market for Modified GRF (1-29).
CJC-1295 with DAC: a related but chemically distinct albumin-binding analogue developed for prolonged circulation.
These names should not be treated as interchangeable without specifying whether the DAC modification is present.
Structural research
CJC-1295 No DAC and Modified GRF (1-29)
The Modified GRF (1-29) backbone commonly associated with CJC-1295 No DAC contains four substitutions relative to native GRF/GHRH(1-29).
Position 2
A D-alanine substitution is used at position 2, a region important to resistance against rapid enzymatic cleavage.
Position 8
Glutamine is incorporated at position 8 within the modified 29-residue sequence.
Position 15
Alanine is incorporated at position 15 as part of the tetrasubstituted GRF structure.
Position 27
Leucine is incorporated at position 27 within Modified GRF (1-29).
29 Residues
The peptide retains the 29-residue framework derived from the active N-terminal region of GHRH.
No Albumin-Binding Group
The No-DAC material lacks the Drug Affinity Complex used in long-acting CJC-1295.
GHRH biology
CJC-1295 No DAC Research Peptide and GHRH
Growth hormone-releasing hormone is a hypothalamic signalling peptide involved in regulation of growth-hormone secretion from anterior-pituitary somatotroph cells.
The first 29 amino acids of GHRH contain the receptor-activating portion of the molecule. This observation led to extensive research involving GHRH(1-29) and structurally modified analogues.
Hypothalamic Signal
Native GHRH functions as part of the physiological signalling network controlling pituitary growth-hormone release.
GHRH Receptor
GHRH-related peptides are studied for interaction with the GHRH receptor on pituitary somatotroph cells.
29-Residue Region
The N-terminal 1–29 region retains the receptor-related biological activity that made it a focus of analogue development.
Analogue Research
Structural modifications have been investigated to alter stability while maintaining receptor signalling.
Enzymatic stability
Why Modified GRF (1-29) Uses Amino-Acid Substitutions
Native GHRH-derived fragments can be rapidly degraded by circulating peptidases. One important pathway involves dipeptidyl peptidase IV, also known as DPP-4.
Modification near the N-terminus can reduce susceptibility to this cleavage pathway. Modified GRF (1-29) therefore provides a useful research model for examining how sequence changes influence peptide stability and receptor activity.
For broader discussion of degradation and handling variables, see Understanding Peptide Stability.
DAC comparison
CJC-1295 No DAC vs CJC-1295 With DAC
The presence or absence of the Drug Affinity Complex is one of the most important distinctions when interpreting CJC-1295 literature.
| Feature | CJC-1295 No DAC / Modified GRF (1-29) | CJC-1295 With DAC |
|---|---|---|
| Core peptide | Modified GHRH/GRF(1-29) analogue | Modified GHRH-related peptide incorporated into an albumin-binding design |
| Drug Affinity Complex | Absent | Present |
| Albumin binding | No DAC-mediated albumin conjugation | Designed for covalent association with circulating albumin |
| Research profile | Shorter-duration GHRH-receptor research model | Designed for substantially prolonged exposure |
| Human CJC-1295 PK literature | Should not be inferred from DAC studies | Human pharmacokinetic studies reported prolonged GH and IGF-1 responses |
Receptor signalling
CJC-1295 No DAC and GHRH-Receptor Research
The GHRH receptor is a G-protein-coupled receptor expressed prominently on pituitary somatotroph cells. Activation of this receptor initiates intracellular signalling associated with growth-hormone secretion.
Modified GHRH analogues are therefore useful experimental tools for studying the relationship between peptide structure, receptor activation and downstream endocrine signalling.
Receptor Activation Is Not the Same as Clinical Benefit
Demonstrating that a peptide interacts with a receptor or influences a hormone-related pathway provides mechanistic information.
It does not independently establish a clinical outcome, treatment indication, long-term safety profile or appropriate use in humans.
GH and IGF-1 research
Growth-Hormone and IGF-1 Research Context
GHRH analogues are commonly studied through growth-hormone and downstream insulin-like growth factor 1 signalling.
Human studies of the long-acting DAC-containing CJC-1295 molecule reported prolonged increases in circulating GH and IGF-1. Those findings are useful for understanding the DAC platform but should not be presented as direct pharmacokinetic evidence for CJC-1295 No DAC.
For the No-DAC material, the more defensible scientific framework is the broader literature involving GHRH(1-29), Modified GRF analogues, receptor activation and peptide stability.
Why the Literature Must Be Separated
The DAC modification changes how the molecule interacts with serum albumin and therefore substantially changes its pharmacokinetic behaviour.
A result obtained with an albumin-binding molecule cannot automatically be transferred to an otherwise related peptide that lacks that modification.
Related compound
CJC-1295 No DAC and Ipamorelin Research
CJC-1295 No DAC and ipamorelin are frequently discussed together, but they belong to different peptide signalling systems.
Modified GRF (1-29) is studied through the GHRH receptor. Ipamorelin is a growth-hormone secretagogue investigated through the ghrelin/GHS-R1a receptor.
The planned Ipamorelin Research Peptide Overview examines that compound independently so that evidence for the two receptor systems remains clearly separated.
Related GHRH analogue
CJC-1295 No DAC, Sermorelin and GHRH(1-29)
Sermorelin provides another useful comparison because it is based on GHRH(1-29) without the same four substitutions associated with Modified GRF (1-29).
Comparing these compounds helps illustrate how small changes in amino-acid sequence can influence susceptibility to enzymatic degradation while preserving a common receptor-related research framework.
| Material | General Structure | Research Distinction |
|---|---|---|
| Native GHRH | Endogenous hypothalamic peptide | Physiological reference molecule |
| GHRH(1-29) / Sermorelin | N-terminal 29-residue GHRH fragment | Retains GHRH-receptor activity but remains susceptible to rapid degradation |
| Modified GRF (1-29) | Tetrasubstituted 29-residue analogue | Designed for increased resistance to enzymatic degradation |
| CJC-1295 with DAC | Modified GHRH-related structure with albumin-binding modification | Designed for markedly prolonged exposure |
Our planned Sermorelin Research Peptide Overview will examine GHRH(1-29) separately.
Evidence interpretation
Understanding CJC-1295 No DAC Research Evidence
The terminology surrounding CJC-1295 creates an unusual evidence problem: studies using related GHRH analogues are sometimes discussed as though they all involve the same molecule.
Analytical documentation
CJC-1295 No DAC Research Peptide: Identity and Batch Testing
The naming ambiguity surrounding CJC-1295 makes analytical identity particularly important for laboratory research.
A label saying only “CJC-1295” does not by itself establish whether a material contains a DAC modification. Researchers should evaluate the stated compound identity together with batch-specific analytical documentation.
For the analytical framework, read Peptide Purity & Certificates of Analysis (COAs) Explained and Peptora's Testing & COAs.
Research network
Continue Exploring CJC-1295 No DAC Research
This overview connects CJC-1295 No DAC with Peptora's broader educational network covering related compounds, peptide stability, analytical documentation and research-material identity.
Related Peptide Research Resources
Continue into related compound overviews and foundational research education.
CJC-1295 No DAC FAQ
CJC-1295 No DAC Research Peptide: Frequently Asked Questions
Common research questions about CJC-1295 No DAC, Modified GRF (1-29), GHRH signalling and the Drug Affinity Complex distinction.
What is CJC-1295 No DAC?
CJC-1295 No DAC is a name widely used for Modified GRF (1-29), a synthetic 29-amino-acid GHRH-related peptide containing four substitutions and lacking the albumin-binding Drug Affinity Complex.
Is CJC-1295 No DAC the same as Modified GRF (1-29)?
The names are widely used interchangeably in the research-material market. Modified GRF (1-29) more directly describes the tetrasubstituted 29-residue GHRH-related peptide lacking DAC.
What does No DAC mean?
No DAC means that the material does not contain the Drug Affinity Complex albumin-binding modification associated with long-acting CJC-1295.
Is CJC-1295 No DAC the same as CJC-1295 with DAC?
No. The DAC-containing molecule incorporates an albumin-binding modification that substantially changes its pharmacokinetic behaviour. Findings involving that form should not automatically be attributed to the No-DAC material.
What receptor is associated with Modified GRF (1-29)?
Modified GRF (1-29) is a GHRH-related analogue studied through the growth hormone-releasing hormone receptor.
How is CJC-1295 No DAC different from ipamorelin?
They involve different receptor systems. Modified GRF (1-29) is studied through the GHRH receptor, while ipamorelin is a growth-hormone secretagogue associated with the ghrelin/GHS-R1a receptor.
Can CJC-1295 with DAC human studies be applied directly to No DAC?
No. The DAC modification produces albumin binding and substantially alters exposure. Human pharmacokinetic findings from DAC-containing CJC-1295 should therefore not be presented as direct evidence for the No-DAC material.
Does published research verify a specific CJC-1295 No DAC batch?
No. A specific laboratory batch must be evaluated using the analytical documentation associated with that batch.
Research use only
CJC-1295 No DAC for Controlled Laboratory Research
This overview provides educational information about Modified GRF (1-29), CJC-1295 terminology and GHRH-related experimental research. Findings involving native GHRH, other GHRH analogues or DAC-containing CJC-1295 should not automatically be interpreted as findings involving CJC-1295 No DAC.
Peptora Peptide Labs research products are intended solely for controlled non-clinical laboratory research. They are not intended for human or veterinary consumption, compounding or clinical use. Nothing on this page provides medical advice, dosing or administration guidance, or representations concerning diagnosis, treatment, cure or prevention of disease.
CJC-1295 and GHRH Scientific Resources
- PubMed — Prolonged stimulation of GH and IGF-I by CJC-1295 in healthy adults
- PubMed — Analytical identification of CJC-1295-related material
- PubMed — Analytical detection of GHRH and related analogues
- Peptora — What Are Research Peptides?
- Peptora — Understanding Peptide Stability
- Peptora — Peptide Purity & Certificates of Analysis Explained
- Peptora — Testing & COAs