cjc 1295 amino acid sequence

Self-Contained Primary Sequence Overview

The canonical cjc 1295 amino acid sequence (specifically CJC-1295 without DAC, also known as Modified GRF 1-29) is a 29-amino-acid synthetic peptide amide with the primary 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. It features four strategic amino acid substitutions compared to native mammalian GHRH 1-29: D-alanine at position 2, glutamine at position 8, alanine at position 15, and leucine at position 27.

In contrast, the CJC-1295 with DAC variant appends a Lysine residue at position 30 bound to a Maleimidopropionic acid linker (Lys(DAC)), allowing covalent binding to serum albumin in vivo. In laboratory studies, both variants function as synthetic growth hormone-releasing hormone (GHRH) receptor agonists designed to evaluate pituitary somatotroph stimulation and downstream IGF-1 expression without rapid enzymatic inactivation.

Detailed Chemical Structure and Substitutions in CJC-1295

Native GHRH (1-29) amide exhibits a short biological half-life in physiological media due to rapid cleavage by dipeptidyl peptidase IV (DPP-IV) between the N-terminal Tyr1 and Ala2 residues. To overcome this limitation in bench research, structural biochemists modified the native core. Examining the cjc 1295 amino acid sequence reveals four precise substitutions designed to preserve alpha-helical conformation while blocking enzymatic degrading pathways.

The first key substitution is D-Alanine at position 2 (D-Ala2). Replacing the naturally occurring L-Alanine isomer alters the spatial stereochemistry at the cleavage site, preventing DPP-IV recognition without diminishing affinity for the GHRH receptor. The second substitution, Glutamine at position 8 (Gln8), improves secondary structural stability. The third alteration, Alanine at position 15 (Ala15), enhances resistance against endopeptidase activity. Finally, Leucine at position 27 (Leu27) optimizes hydrophobic interaction within the receptor-binding pocket.

Together, these four amino acid modifications transform the fragile native peptide sequence into a highly stable molecular tool. Researchers studying growth factor kinetics utilize these structural improvements to conduct extended assays without requiring continuous replenishment of the culture media.

CJC-1295 No DAC vs. CJC-1295 With DAC: Structural Comparison

When evaluating GHRH analogs, investigators frequently compare CJC-1295 No DAC (Modified GRF 1-29) to CJC-1295 with DAC. While both share the core 29-amino-acid tetrasubstituted backbone, their terminal C-protein modifications alter their functional pharmacokinetics in animal models.

CJC-1295 No DAC features a C-terminal carboxamide group (-NH2) at position 29 (Arg29-NH2). This structural termination mimics native GHRH cleavage products, offering a half-life of approximately 30 minutes in plasma assays. This short-acting profile allows laboratory models to simulate natural, pulsatile growth hormone secretion.

Conversely, CJC-1295 with DAC incorporates a 30th amino acid residue—a Lysine adduct conjugated to Maleimidopropionic acid (Lys(MPA)). This Drug Affinity Complex (DAC) reactive group forms a irreversible covalent bioconjugate with the free Cys34 thiol group of circulating albumin. This structural modification extends the systemic half-life in rodent models to several days, shifting growth hormone release from a pulsatile pattern to sustained baseline elevation. Choosing between these variants depends strictly on whether a pulse-amplification or baseline-elevation experimental design is required.

Comparing GHRH Analogs and Structural Motifs Across Peptide Classes

In biochemical research, classifying peptides by sequence homology and receptor target provides key insights into secretagogue mechanics. Within the GHRH receptor agonist class, the cjc 1295 amino acid sequence shares structural lineage with Sermorelin, which represents the exact un-substituted native 1-29 amino acid sequence of Human GHRH. While Sermorelin retains identical receptor binding kinetics, its lack of D-Ala2 substitution renders it subject to rapid enzymatic hydrolysis by DPP-IV in vitro.

Beyond GHRH analogs, researchers frequently investigate dual-pathway growth hormone secretagogue regimens by pairing GHRH analogs with ghrelin receptor (GHS-R1a) agonists like Ipamorelin. Ipamorelin is a pentapeptide (Aib-His-D-2-Nal-D-Phe-Lys-NH2) with no sequence homology to GHRH, operating through an entirely distinct signaling cascade to achieve synergistic somatotroph activation.

In contrast, non-hormonal regulatory peptides such as Thymulin—a nonapeptide (Pyr-Glu-Ala-Lys-Ser-Gln-Gly-Gly-Ser-Asn-OH) derived from the thymus gland—exhibit zero sequence overlap with GHRH secretagogues. While GHRH analogs focus on somatotropic signaling and downstream IGF-1 expression for tissue repair research, thymic peptides target T-cell differentiation and cytokine modulation pathways. Understanding these distinct primary structures prevents cross-reactivity and ensures proper design of multi-compound experimental matrices.

Mechanism of Action in Preclinical Tissue Repair Models

In preclinical research, GHRH analogs containing the modified cjc 1295 amino acid sequence bind selectively to the GHRH cell-surface receptor on pituitary somatotrophs. Activation of this G-protein coupled receptor triggers intracellular adenylate cyclase, elevating cyclic adenosine monophosphate (cAMP) and activating protein kinase A (PKA). This signaling cascade drives intracellular calcium influx and stimulates transcription of endogenous growth hormone.

Preclinical animal studies indicate that sustained stimulation of the GHRH receptor leads to proportional increases in circulating Insulin-like Growth Factor 1 (IGF-1). Researchers utilize this pathway to investigate localized tissue repair, cellular regeneration, protein synthesis, and collagen cross-linking in wound healing models.

Because Modified GRF 1-29 preserves pulsatile signaling mechanisms when administered without DAC, it allows researchers to study physiological growth hormone release dynamics without exhausting pituitary reserve or inducing receptor desensitization in cell culture protocols.

Analytical Verification: RP-HPLC, Mass Spectrometry, and Endotoxin Testing

Maintaining absolute structural fidelity in synthetic peptides requires rigorous multi-step analytical testing. Because amino acid substitutions can suffer from incomplete coupling or racemization during solid-phase peptide synthesis (SPPS), verification of the final cjc 1295 amino acid sequence is mandatory for reproducible research.

PX1 Research ensures that every batch undergoes Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC) to verify chromatographic purity exceeds 98.0%. In addition, Electrospray Ionization Mass Spectrometry (ESI-MS) is conducted to confirm exact molecular mass (Theoretical MW: 3367.9 Da for Modified GRF 1-29), verifying that all 29 amino acid residues are present in correct stoichometry without deletion sequences.

To protect cell cultures and animal models from confounding inflammatory artifacts, all lots undergo Chromogenic LAL Endotoxin Testing to ensure levels remain under strict limits (<0.01 EU/mg). Complete lot-specific Certificate of Analysis (COA) documentation is available directly through our research library hub.

Laboratory Reconstitution and Handling Protocols

Proper reconstitution techniques are critical to prevent structural aggregation or hydrolytic degradation of the cjc 1295 amino acid sequence. Standard laboratory protocols specify the use of Bacteriostatic Water (0.9% benzyl alcohol) or sterile water for injection depending on assay requirements.

When reconstituting lyophilized peptide vials, direct jetting of solvent onto the lyophilized cake should be avoided. Instead, allow the solvent to flow gently down the inner glass wall of the vial. Gently swirl or roll the vial until complete dissolution is achieved; never vortex or vigorously shake peptide solutions, as mechanical shear forces can disrupt alpha-helical tertiary structure.

For quantitative concentration calculations across varied dilution volumes, researchers should consult our standardized reconstitution calculator guide to maintain precise molarities during in vitro pipetting.

Storage and Stability Guidelines for Lyophilized Peptides

Lyophilized CJC-1295 powder exhibits high stability when maintained under controlled storage conditions. Unreconstituted vials should be stored at -20°C for short-to-medium term storage, or at -80°C for extended archival storage to prevent moisture degradation and peptide hydrolysis.

Once reconstituted into aqueous solution, peptide aliquots should be stored at 2°C to 8°C and utilized within 14 to 28 days depending on the solvent system. To avoid repetitive freeze-thaw cycles—which cause physical shear stress and sequence degradation—reconstituted solutions should be divided into single-use working aliquots prior to freezing.

For detailed technical insights into peptide handling, degradation kinetics, and analytical verification methods, explore our comprehensive peptide purity testing guide.

Institutional Procurement and Quality Assurance Standards

Procuring research-grade peptides for university, biotechnology, and corporate research facilities requires absolute transparency, batch consistency, and reliable supply chains. Substandard peptide sequences containing truncation artifacts or residual trifluoroacetate (TFA) salts yield inconsistent binding assays and invalid experimental data.

PX1 Research manufactures all compounds in ISO 17025 accredited and GMP-compliant USA facilities. Every batch undergoes rigorous third-party testing, ensuring that researchers receive fully verified sequences free of contaminants.

Principal investigators and laboratory procurement managers seeking bulk quantities, custom synthesis options, or recurring institutional billing accounts can review parameters on our wholesale lab account portal or explore our full line of compounds in the all peptides catalog.