Tesofensine (400 mcg, 60 units)
CJC-1295 No DAC Peptide (10MG)
This batch of CJC-1295 No DAC has been third party lab tested and verified for quality.
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purity
weight
endotoxins(lps)
$68.00
| Quantity | Price | |
|---|---|---|
| 0% | 1 - 4 | $68.00 |
| 10% | 5 - 9 | $61.20 |
| 20% | 10 - 19 | $54.40 |
| 30% | 20 + | $47.60 |
This product comes as lyophilized powder and is not reconstituted. All products and materials sold on this site are for Research Use Only and not for human use; subject to our Terms and Conditions.
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| Peptide vial specifications | Results | |
|---|---|---|
Not reconstituted | ||
Bottle type: | Vial - sealed - flip top | |
Form: | Powder (lyophilized) | |
Vial size: | 3ML | |
CJC-1295 No DAC Certificate of Analysis (COA) Test Result
| Date Tested: | |
|---|---|
| Purity: | 99.083% |
| Weight: | 10.81mg |
| Endotoxins (LPS): | Pass |
| Batch #: | CJND05260910I |
| Testing Lab: | Janoshik |
| Testing Methods: | HPLC, LAL, TAMC/YAMC USP <71> |
Mod GRF (1-29) Specifications: Molecular Weight, CAS Number & Sequence
Mod GRF (CAS 863288-34-0) is a research peptide with the molecular formula C152H252N44O42 and a molecular weight of 3367.9 g/mol.
| Form: | Powder (lyophilized) |
|---|---|
| Weight: | 10mg |
| Appearance: | White lyophilized powder |
| CAS Number: | 863288-34-0 |
| Molecular Formula: | C152H252N44O42 |
| Molecular Weight: | 3367.9 g/mol |
| PubChem CID: | 56841945 |
| Sequence: | Tyr-D-Ala-Asp-Ala-Ile-Phe-Thr-Gln-Ser-Tyr-Arg-Lys-Val-Leu-Ala-Gln-Leu-Ser-Ala-Arg-Lys-Leu-Leu-Gln-Asp-Ile-Leu-Ser-Arg-NH2 |
| Other Names: | MOD-GRF(1-29), Mod GRF, CJC-1295 without DAC, Tetrasubstituted GRF(1-29), Modified GRF, CJC1295 NO DAC, CJC-1295 No DAC |
| Terms: | Subject to our Terms and Conditions. This material is sold for laboratory research use only. Not for human consumption, animal, or medical use. |
CJC No DAC Molecular Structure
CJC No DAC Amino Acid Sequence
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What is CJC-1295 No DAC (MOD-GRF 1-29)?
CJC-1295 No DAC, also known as MOD-GRF(1-29) or Modified GRF 1-29, is a synthetic analog of the GHRH 1-29 peptide sequence. It was engineered to enhance the peptide’s α-helical stability and receptor affinity, leading to a stronger and more sustained growth hormone (GH)–releasing effect in research models. Unlike CJC-1295 with DAC (Drug Affinity Complex), this version does not contain the albumin-binding modification, resulting in a shorter half-life and more pulsatile growth hormone release that closely mimics natural GH secretion patterns. MOD-GRF(1-29) incorporates strategic alanine substitutions at key positions that stabilize its α-helical structure, dramatically enhancing receptor binding affinity and biological potency compared to natural GHRH. This makes it an optimized synthetic analog for research applications requiring precise, short-acting GH stimulation.
CJC-1295 No DAC Research Studies
Peer-reviewed scientific research findings
📚 Peer-Reviewed Study
Published Study: GHRH analogues with much improved in vitro growth hormone-releasing potencies in rat pituitary cells
Background on GHRH Peptides and Structure-Activity Studies
GHRH peptides are 44-residue hormones that stimulate growth hormone (GH) release through specific receptor binding. Nearly all biological activity resides in the GHRH 1-29 core sequence, which forms the foundation for most structure-activity studies. The GHRH 1-29 peptide adopts an amphiphilic α-helical structure in its receptor-bound conformation, an arrangement critical for activity and receptor affinity.
This helical pattern enables proper alignment of hydrophilic and hydrophobic residues, promoting optimal receptor interaction. Previous research showed that truncated analogs retaining this α-helix maintain full in vitro and in vivo potency, underscoring the structural efficiency of the GHRH 1-29 region as a functional hormone mimetic.
Objective of the Study
This investigation sought to determine whether specific alanine substitutions could strengthen the α-helical structure of GHRH peptides, thereby improving their biological potency. Using computational modeling and experimental assays, researchers focused on positions 8, 9, and 15 of the GHRH 1-29 sequence. These residues influence local folding and amphiphilicity.
Substituting alanine at these positions was hypothesized to promote a more stable helical conformation and increase receptor binding affinity. The study also examined combinations of these substitutions, including D-Ala², to evaluate additive effects on GH-releasing potency.
Peptide Synthesis and Analytical Methods
Each synthetic analog of GHRH 1-29 was prepared using solid-phase peptide synthesis on methylbenzhydrylamine resin, followed by cleavage with hydrogen fluoride and purification through Sephadex G-50 and reverse-phase HPLC. Analytical validation demonstrated ≥97% purity, confirmed via amino acid analysis and fast atom bombardment (FAB) mass spectrometry. The resulting peptides were verified to match their calculated molecular weights and expected amino acid compositions, ensuring structural accuracy for biological testing.
Chou-Fasman Computational Analysis
To predict the structural consequences of residue substitutions, the team applied Chou-Fasman analysis, assessing probabilities of α-helix and β-turn formation. In native GHRH 1-29, regions near residues 8–9 and 15 exhibited lower helix stability. Replacement of Gly¹⁵ with Ala¹⁵ increased predicted α-helix probability from 0.987 to 1.169, while Ala⁸ and Ala⁹ substitutions further raised stability and reduced β-bend tendencies.
These findings indicated that alanine residues reinforce the amphiphilic α-helix, aligning with the experimental hypothesis that helical reinforcement correlates with receptor affinity and GH-release potency.
In Vitro Assay Design
Biological potency was assessed using primary rat pituitary monolayer cultures, an established system sensitive to receptor-mediated GH release. The dispersed pituitary cells were incubated for three hours with each GHRH peptide analogue in the presence of somatostatin to standardize basal inhibition. After incubation, GH concentration in the culture medium was measured using a double-antibody radioimmunoassay (RIA). Potency values were expressed relative to unmodified GHRH 1-29 NH₂, used as the internal standard.
CJC1295 No DAC Key Findings and Potency Enhancements
Results demonstrated pronounced, additive potency gains with alanine substitution:
- [Ala¹⁵]GHRH-(1-29)NH₂: 5× more potent than native peptide
- [Ala⁸] and [Ala⁹] analogues: ~4× potency increase each
- [Ala⁸,¹⁵]GHRH-(1-29)NH₂: 15× more potent
- [D-Ala², Ala⁸,¹⁵]GHRH-(1-29)NH₂: 27× increase
- [D-Ala², Ala⁸,⁹,¹⁵]GHRH-(1-29)NH₂: 49× more potent — the most powerful in vitro analogue reported
Structure-Function Relationships
The enhanced activity of these GHRH peptides correlated with their increased α-helicity and optimized amphiphilic geometry. Substitutions of alanine at strategic positions stabilized the helix without disrupting the hydrophilic–hydrophobic balance necessary for receptor interaction. Incorporating D-Ala² improved protease resistance and peptide rigidity, enhancing durability in biological environments.
In contrast, excessive hydrophobic substitutions—such as replacing Thr⁷ with Leu—diminished potency, indicating that fine structural precision is essential. The study thus revealed that potency is maximized when helical enhancement aligns with balanced surface polarity.
Impact on GRH Antagonists
Helix-stabilizing alanine substitutions also improved the efficacy of GRH antagonists. The unmodified antagonist [D-Arg²,Leu²⁷]GHRH-(1-29)NH₂ displayed an inhibitory IC₅₀ of 2.2 × 10⁻⁷ M, while the [D-Arg², Ala⁸,¹⁵] variant achieved 5.9 × 10⁻⁸ M. Addition of Ala⁹ further improved inhibition to 1.7 × 10⁻⁸ M, nearly a threefold gain.
These results paralleled the potency increases observed in agonist analogs, implying that enhanced α-helicity improves receptor binding regardless of agonist or antagonist function.
Discussion and Implications for Synthetic Analog Development
This research demonstrates that rational alanine substitution is an effective method for fine-tuning the GHRH peptide conformation to increase potency. Each substitution incrementally stabilized the α-helix and improved receptor affinity, confirming an additive structure-activity relationship. Small side-chain modifications can thus yield significant biological gains without altering peptide sequence length or charge.
The results highlight a blueprint for designing synthetic analogs with predictable improvements in potency, receptor selectivity, and enzymatic stability—features critical for advancing peptide-based research compounds like MOD-GRF(1-29).
CJC-1295 No DAC Study Conclusion
Alanine-optimized GHRH 1-29 analogues exhibit substantial increases in GH-releasing potency in vitro. The combined substitutions at D-Ala², Ala⁸, Ala⁹, and Ala¹⁵ produced the strongest effects by reinforcing α-helicity and reducing conformational flexibility. The most active analogue, [D-Ala², Ala⁸,⁹,¹⁵]GHRH-(1-29)NH₂, was nearly 50× more potent than native GHRH in rat pituitary assays.
These findings form the structural foundation for designing next-generation synthetic analogs that maximize receptor interaction, stability, and biological activity.
Frequently Asked Questions
What are GHRH peptides used for in research?
GHRH peptides are used to study the regulation of growth hormone secretion and receptor binding dynamics in cell and animal models.
How does GHRH 1-29 compare to full-length GHRH?
GHRH 1-29 retains full biological potency of the 44-residue hormone, making it the preferred form for structure-activity and analog studies.
Why are alanine residues important in peptide engineering?
Alanine promotes α-helical formation without introducing steric hindrance, stabilizing peptide conformation and improving receptor affinity.
What defines a synthetic analog in peptide design?
A synthetic analog is a modified peptide created by substituting specific amino acids to enhance stability, potency, or selectivity compared to the natural sequence.
What is the structure and purpose of GHRH 1-29?
It is a 29-amino-acid fragment of GHRH forming an amphiphilic α-helix responsible for binding to GH receptors and stimulating hormone release.
How do alanine substitutions enhance peptide potency?
Alanine stabilizes helical regions and decreases β-turn formation, strengthening receptor binding and signal transduction efficiency.
Which alanine positions were most effective in GHRH analogues?
Positions 8, 9, and 15 were most impactful, especially when combined with D-Ala², yielding additive potency effects.
How do D-amino acid substitutions influence peptide conformation and stability?
D-Amino acids, such as D-Ala², confer resistance to enzymatic degradation and promote stable secondary structures that prolong biological activity.
Can similar modifications enhance peptide antagonists?
Yes. The same alanine substitutions increased antagonist potency by improving receptor binding affinity, reducing IC₅₀ values significantly.
Study References
Coy DH, Hocart SJ, Murphy WA. Growth hormone-releasing hormone analogues with much improved in vitro growth hormone-releasing potencies in rat pituitary cells. Eur J Pharmacol. 1991;204(2):179-185. doi:10.1016/0014-2999(91)90703-s
https://pubmed.ncbi.nlm.nih.gov/1806385/