Description

CAS Number: 170851-70-4 (Ipamoreln) / 863288-34-0 (CJC-1295 No DAC)

Molecular Formula:

• Ipamoreln: C₃₈H₄₉N₉O₅
• CJC-1295 No DAC: C₁₅₂H₂₅₂N₄₄O₄₂

Molecular Weight:

• Ipamoreln: 711.85 g/mol
• CJC-1295 No DAC: 3367.95 g/mol

Sequence:

• Ipamoreln: Aib-His-D-2-Nal-D-Phe-Lys-NH₂
• CJC-1295 No DAC: 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

Form: Lyophilized powder (not reconstituted)

Purity: ~99% HPLC

Storage: Store at -20°C. Protect from light and moisture.

Vial: 3mL sealed vial with flip-top cap

Total Content: 10mg (5mg Ipamoreln + 5mg CJC-1295 No DAC)

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FULL PRODUCT DESCRIPTION:

Ipamoreln + CJC-1295 No DAC Research Peptide Blend

Peptide Minds offers a high-purity research peptide blend combining Ipamoreln and CJC-1295 No DAC (Modified GRF 1-29) in equal 5mg proportions. This lyophilized powder formulation is manufactured for laboratory research applications only.

Molecular Profile

This research blend combines two distinct peptide sequences with complementary structural characteristics. Ipamoreln is a pentapeptide (Aib-His-D-2-Nal-D-Phe-Lys-NH₂) with a molecular weight of 711.85 g/mol, containing aminoisobutyric acid (Aib) at the N-terminus and D-amino acid substitutions. CJC-1295 No DAC, also designated as Modified GRF(1-29), is a 29-amino acid synthetic peptide analog with a molecular weight of 3367.95 g/mol, featuring strategic amino acid substitutions at positions 2, 8, 9, and 15 compared to native growth hormone-releasing hormone.

The structural modifications in both peptides were designed through systematic optimization studies. CJC-1295 No DAC incorporates D-Ala at position 2 and helix-favoring alanine substitutions at positions 8, 9, and 15, which enhance α-helical conformation based on Chou-Fasman conformational analysis. Ipamoreln’s structure emerged from modification of earlier growth hormone-releasing peptide analogs, incorporating Aib and D-amino acids to modulate stability and selectivity characteristics.

Research Applications

These peptides have been investigated in laboratory settings examining neuroendocrine signaling pathways. CJC-1295 No DAC functions as a growth hormone-releasing hormone (GHRH) receptor agonist, while Ipamoreln acts through the ghrelin receptor (GHS-R1a). Research studies have examined these compounds individually and in combination across multiple experimental models including rat pituitary cell cultures, swine models, and various in vivo systems.

Preclinical research has characterized the distinct receptor-mediated mechanisms of these peptides. GHRH receptor activation couples primarily to Gs protein signaling and adenylyl cyclase activation, while ghrelin receptor engagement couples to Gq proteins and phospholipase C pathways. Studies have documented that combined administration of GHRH analogs with growth hormone-releasing peptides produces effects exceeding individual compound responses in experimental models, reflecting convergent signaling through complementary intracellular pathways.

Quality Specifications

Each vial contains lyophilized powder with the following quality parameters:

• Purity: ~99% by HPLC analysis
• Composition: 5mg Ipamoreln + 5mg CJC-1295 No DAC
• Form: Sterile lyophilized powder
• Reconstitution: Supplied in powder form; requires reconstitution with appropriate solvent for research use
• Third-Party Testing: Each batch undergoes independent laboratory analysis for purity, identity, sterility, and endotoxin content

Storage and Handling

Store unopened vials at -20°C protected from light and moisture. Once reconstituted, peptide solutions should be stored at 2-8°C and used within the timeframe established by stability studies for your specific research protocol. Avoid repeated freeze-thaw cycles. Handle using aseptic technique in appropriate laboratory settings.

Important Research Use Information

This product is manufactured and supplied exclusively for laboratory research purposes. It is not intended for human consumption, veterinary use, or any clinical applications. Researchers should follow all applicable institutional guidelines, biosafety protocols, and regulatory requirements when handling research peptides.

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Research Background: Complementary Mechanisms in Neuroendocrine Signaling

The combination of Ipamoreln and CJC-1295 No DAC represents a research model for investigating dual-pathway activation in growth hormone secretagogue systems. These peptides engage distinct receptor families—GHRH receptors (class II G-protein coupled receptors) and ghrelin receptors (GHS-R1a)—that regulate somatotroph function through complementary intracellular signaling cascades.

CJC-1295 No DAC: Optimized GHRH Analog

CJC-1295 No DAC was developed through structure-activity relationship studies aimed at enhancing the α-helical conformation critical for GHRH receptor binding. Native GHRH exhibits suboptimal helix probability at certain positions, which reduces receptor affinity. By incorporating helix-favoring alanine residues at positions 8, 9, and 15, along with D-Ala² substitution for proteolytic protection, researchers created a modified peptide designated as [D-Ala²,Ala⁸’⁹’¹⁵]GHRH-(1-29)NH₂.

In rat pituitary cell culture assays, CJC-1295 No DAC demonstrated 49-fold greater potency compared to native GHRH (EC₅₀ = 0.31 nmol/L vs 15 nmol/L). The D-amino acid at position 2 provides resistance to dipeptidylpeptidase IV (DPP-IV) degradation, while the alanine substitutions stabilize the bioactive helical structure, reducing the entropic cost of receptor binding. These structural modifications result in enhanced intrinsic activity at the GHRH receptor without the half-life extension provided by drug affinity complex (DAC) conjugation, distinguishing this “No DAC” variant from extended-release formulations.

Ipamoreln: Selective Growth Hormone Secretagogue

Ipamoreln (Aib-His-D-2-Nal-D-Phe-Lys-NH₂) was characterized as the first growth hormone-releasing peptide demonstrating selectivity for growth hormone release comparable to GHRH itself. Earlier GHRP compounds including GHRP-6 and GHRP-2 produced dose-dependent stimulation of adrenocorticotropic hormone (ACTH) and cortisol alongside growth hormone, with GHRP-2 elevating ACTH to 350% of GHRH levels at maximally effective doses in swine studies.

Ipamoreln’s development involved removing the central Ala-Trp dipeptide from GHRP-1 and optimizing the N-terminus with aminoisobutyric acid (Aib). Pharmacological characterization demonstrated potency comparable to GHRP-6 (EC₅₀ = 1.3 nmol/L in rat pituitary cells; ED₅₀ = 2.3 nmol/kg in conscious swine), but with fundamentally different selectivity. Even at doses exceeding 200-fold its growth hormone ED₅₀, Ipamoreln produced ACTH and cortisol levels statistically indistinguishable from GHRH, without significant effects on follicle-stimulating hormone, luteinizing hormone, prolactin, or thyroid-stimulating hormone.

Synergistic Interaction: Convergent Signaling Pathways

Multiple research studies have documented synergistic interactions when GHRH analogs are combined with growth hormone-releasing peptides in experimental systems. In dispersed rat pituitary cell cultures—the same in vitro model used to characterize both CJC-1295 No DAC and Ipamoreln—co-administration of GHRH with GHRP-6 produced growth hormone release significantly exceeding the sum of individual responses, confirming that the interaction occurs at the somatotroph level independent of hypothalamic factors.

In vivo studies in rats, dogs, and swine have demonstrated that combined GHRH+GHRP administration produces peak growth hormone levels 2- to 5-fold higher than predicted from additive effects. The mechanistic basis for this synergy lies in the complementary nature of the signaling pathways. GHRH receptor activation couples primarily to Gs proteins, stimulating adenylyl cyclase to increase cyclic AMP (cAMP) production. Elevated cAMP activates protein kinase A (PKA), which phosphorylates voltage-gated calcium channels and transcription factors including CREB.

Ghrelin receptor (GHS-R1a) activation by Ipamoreln couples primarily to Gq proteins, activating phospholipase C to generate inositol 1,4,5-trisphosphate (IP₃) and diacylglycerol (DAG). IP₃ triggers release of calcium from intracellular stores, while DAG activates protein kinase C (PKC). These pathways converge on calcium signaling through different mechanisms: GHRH enhances calcium channel activity via PKA phosphorylation, while GHRPs mobilize intracellular calcium stores via IP₃. The combined calcium elevation from both sources produces synergistic secretory responses documented across multiple experimental models.

Temporal Dynamics and Pulsatile Patterns

Research examining the temporal relationship between GHRH and GHRP administration indicates that simultaneous or near-simultaneous administration produces maximal synergistic effects, with synergy declining as the interval between administrations exceeds 15-30 minutes. This temporal sensitivity reflects the kinetics of receptor-mediated signaling cascades and the transient nature of intracellular second messenger elevations.

CJC-1295 No DAC, lacking the DAC component that extends half-life, demonstrates relatively rapid onset with peak effects occurring within 15-30 minutes following administration in animal studies, with duration typically lasting 2-3 hours based on GHRH analog pharmacology. Ipamoreln similarly demonstrates rapid onset, with peak responses at 10-15 minutes in swine studies and return to baseline within 120 minutes. This matched temporal profile makes these compounds well-suited for investigating coordinated dual-pathway activation in research models.

The relatively short duration of both peptides allows for experimental protocols involving multiple daily administrations that can recreate pulsatile patterns. Natural growth hormone secretion occurs in discrete pulses with species-specific frequency, with pulse amplitude varying based on metabolic state and other factors. This pulsatility is generated by coordinated hypothalamic release of GHRH (stimulatory) and somatostatin (inhibitory), with endogenous ghrelin providing additional modulatory input.

Selectivity Considerations in Research Models

A distinguishing feature of the Ipamoreln + CJC-1295 No DAC combination is the preserved hormonal selectivity compared to combinations involving non-selective GHRPs. While GHRP-6 and GHRP-2 elevated ACTH to 300-350% of GHRH levels at growth hormone-releasing doses, Ipamoreln produced ACTH and cortisol levels indistinguishable from GHRH administration even at doses greatly exceeding its growth hormone ED₅₀ in swine studies.

This selectivity profile is relevant for research protocols where chronic or repeated administration might be examined, as sustained hypothalamic-pituitary-adrenal (HPA) axis activation could confound experimental outcomes. Neither CJC-1295 No DAC nor Ipamoreln significantly affects other pituitary hormones including FSH, LH, prolactin, or TSH based on preclinical characterization, supporting genuine selectivity for growth hormone-regulatory pathways.

Structural Optimization and Stability

Both peptides incorporate structural modifications designed to enhance stability and activity compared to native peptide hormones. The D-Ala² substitution in CJC-1295 No DAC provides protection against DPP-IV-mediated degradation, while the alanine substitutions at positions 8, 9, and 15 enhance α-helical structure through increased helix propensity at these positions based on Chou-Fasman analysis.

Ipamoreln’s Aib (aminoisobutyric acid) N-terminal substitution provides both conformational constraint and metabolic stability through its gem-dimethyl alpha carbon, which resists proteolytic attack. The incorporation of D-amino acids (D-2-Nal, D-Phe) further enhances resistance to enzymatic degradation while maintaining receptor binding characteristics that confer the compound’s unique selectivity profile.

These structural features collectively contribute to the stability of lyophilized peptide formulations and reconstituted solutions used in research applications, though specific stability parameters should be determined empirically for individual research protocols and storage conditions.

Applications in Neuroendocrine Research

This peptide blend serves as a research tool for investigating:

• Complementary GHRH and ghrelin receptor signaling pathways
• Synergistic interactions between distinct growth hormone secretagogue mechanisms
• Convergent second messenger systems (cAMP vs. calcium mobilization)
• Pulsatile hormone secretion patterns in experimental models
• Selective vs. non-selective growth hormone-releasing peptide effects
• Structure-activity relationships in peptide hormone analogs
• Somatotroph cell biology and receptor pharmacology

Researchers utilizing this blend should implement appropriate experimental controls, employ validated analytical methods for outcome assessment, and interpret results within the context of established neuroendocrine physiology principles.

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References

1. Coy DH, Hocart SJ, Murphy WA. Human 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. https://doi.org/10.1016/0014-2999(91)90703-s
2. Raun K, Hansen BS, Johansen NL, et al. Ipamorelin, the first selective growth hormone secretagogue. Eur J Endocrinol. 1998;139(5):552-561. https://doi.org/10.1530/eje.0.1390552

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Regulatory Compliance Statement

FOR RESEARCH USE ONLY. NOT FOR HUMAN CONSUMPTION OR VETERINARY USE.

This product is sold exclusively for laboratory research applications conducted by qualified researchers in appropriate institutional settings. It is not approved by the FDA for human use, clinical applications, or therapeutic purposes. Purchasers assume full responsibility for compliance with all applicable federal, state, and local regulations governing the purchase, possession, and use of research peptides.

This product is not intended to diagnose, treat, cure, or prevent any disease in humans or animals. It is the sole responsibility of the purchaser to ensure proper handling, storage, and use in accordance with institutional biosafety protocols and regulatory requirements.

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ABOUT PEPTIDE MINDS

Peptide Minds provides high-purity research peptides manufactured to rigorous quality standards. Every batch undergoes third-party laboratory testing for purity (HPLC), identity (mass spectrometry), sterility, and endotoxin content. We maintain transparent quality documentation with batch-specific Certificates of Analysis available upon request.

Our commitment to the research community includes:

• ≥99% peptide purity by HPLC
• Comprehensive third-party testing (purity, sterility, endotoxins)
• Batch traceability with documented CoA
• Proper cold-chain shipping with ice packs
• Expert technical support for research applications