CJC-1295 + Ipamorelin Molecular Weight, Sequence & CAS Reference

Introduction to Co-Formulated CJC-1295 and Ipamorelin Research Compounds

In biomedical research, co-formulations of growth hormone secretagogues are frequently utilized to evaluate synergistic somatotropic axis signaling in vitro and in animal models. The combination of CJC-1295 and Ipamorelin pairs a synthetic growth hormone-releasing hormone (GHRH) analog with a selective growth hormone secretagogue receptor (GHSR-1a) agonist. Investigating these molecules simultaneously allows researchers to explore dual-pathway activation of pituitary somatotrophs.

When evaluating a co-lyophilized research vial such as the CJC-1295 No DAC / Ipamorelin 10mg Blend, principal investigators must treat the constituents as distinct molecular entities. Because a single combined CAS number or unified molecular weight does not exist for co-packaged chemical mixtures, laboratory quantification requires a granular understanding of each compound's individual structural identity, sequence modifications, monoisotopic mass, and salt counterion mass contribution.

PX1 Research provides fully characterized, USA-manufactured research peptides accompanied by high-performance liquid chromatography (HPLC) and mass spectrometry (MS) documentation. Researchers seeking catalog specifications across our full inventory can review our comprehensive catalog of all peptides for analytical benchmarks.

Primary Molecular Specifications and Chemical Registry Overview

Because CJC-1295 and Ipamorelin belong to different peptide classes—a modified peptide hormone fragment and a synthetic pentapeptide, respectively—their physical properties, primary sequences, and molecular weights differ significantly. A combined vial containing both compounds represents a physical mixture of two discrete chemical species rather than a single conjugated molecule.

The table of core metrics for each standard component in laboratory research settings includes: • CJC-1295 Without DAC (Mod GRF 1-29): - Chemical Name: Tetrasubstituted Growth Hormone Releasing Hormone (1-29) Amide - CAS Registry Number: 863288-34-0 - Molecular Formula: C152H252N44O42 - Formula Weight (Average): 3367.97 g/mol - Monoisotopic Mass: 3365.89 Da • CJC-1295 With DAC (Drug Affinity Complex): - Chemical Name: N-epsilon-(3-maleimidopropionyl)-Lys30-CJC-1295 Amide - CAS Registry Number: 446036-97-1 - Molecular Formula: C165H269N47O46 - Formula Weight (Average): 3647.28 g/mol • Ipamorelin Free Base: - Chemical Name: Aib-His-D-2-Nal-D-Phe-Lys-NH2 - CAS Registry Number: 170851-70-4 - Molecular Formula: C38H49N9O5 - Formula Weight (Average): 711.85 g/mol - Monoisotopic Mass: 711.38 Da

It is important to note that commercial supplier designations for a unified blend do not represent an official IUPAC or CAS single chemical registry entity. Analytical chemists must quantify each chromatographic peak independently using appropriate molecular standards.

CJC-1295 (Mod GRF 1-29) Amino Acid Sequence and Structural Substitutions

CJC-1295 without DAC—frequently designated in literature as Modified GRF (1-29) or Mod GRF 1-29—is a synthetic 29-amino-acid peptide derived from the functional N-terminal region of human endogenous GHRH (1-44). Native GHRH (1-29) is prone to rapid enzymatic cleavage in physiological environments, particularly by dipeptidyl peptidase-IV (DPP-IV), which targets the Ala2 position.

To enhance metabolic stability during preclinical research, four specific amino acid substitutions were engineered into the native sequence: • D-Ala at Position 2: Replaces L-alanine to confer resistance against DPP-IV enzymatic cleavage. • Gln at Position 8: Replaces L-asparagine to minimize deamidation pathways. • Ala at Position 15: Replaces L-glycine to increase alpha-helical structural stability. • Leu at Position 27: Replaces L-methionine to prevent oxidative degradation of the thioether side chain.

The resulting 29-residue primary amino acid sequence for CJC-1295 No DAC is: 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

The C-terminus is fully amidated (-NH2), which neutralizes the negative charge of a terminal carboxylate group, stabilizing the peptide against carboxypeptidase degradation during cell culture or in vitro enzyme stability assays.

CJC-1295 with DAC: Structural Additions and Maleimide Linker Chemistry

In studies requiring extended pharmacokinetics, CJC-1295 is synthesized with a Drug Affinity Complex (DAC) reactive affinity moiety attached at the C-terminus. The structural variation adds a lysine residue linked to a maleimidopropionic acid group: Lys(maleimidopropionyl)-NH2.

The complete primary sequence for CJC-1295 DAC is: 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-Lys(Maleimidopropionyl)-NH2

The maleimide functionality is specifically designed to undergo a stable bioconjugate addition reaction with free thiol groups—specifically Cys34 of circulating serum albumin. This irreversible covalent bond increases the operational molecular weight from 3.64 kDa to approximately 70 kDa in biological matrices, extending the elimination half-life in rodent models from minutes to several days.

When designing protocols, researchers must distinguish between CJC-1295 No DAC (Mod GRF 1-29, MW 3367.97 g/mol) and CJC-1295 DAC (MW 3647.28 g/mol). Utilizing the incorrect formula weight will result in systematic errors during molar concentration calculations.

Ipamorelin Amino Acid Sequence and Non-Canonical Residues

Ipamorelin is a synthetic pentapeptide belonging to the growth hormone secretagogue (GHS) class. Unlike larger peptide hormones, Ipamorelin's sequence incorporates non-canonical (non-proteinogenic) amino acids engineered to optimize selectivity for the growth hormone secretagogue receptor 1a (GHSR-1a) without activating receptors for adrenocorticotropic hormone (ACTH) or prolactin.

The primary amino acid sequence of Ipamorelin is: Aib-His-D-2-Nal-D-Phe-Lys-NH2

Structural analysis of these constituent residues reveals key functional characteristics: • Aib (alpha-aminoisobutyric acid / 2-aminoisobutyric acid): Located at the N-terminus, this sterically hindered, dialkylated amino acid protects against aminopeptidase degradation. • His (L-histidine): Occupies position 2, contributing imidazole ring interactions crucial for receptor contact. • D-2-Nal (D-2-naphthylalanine): A bulky, aromatic unnatural amino acid at position 3 that enforces a specific spatial conformation. • D-Phe (D-phenylalanine): Provides additional aromatic and stereochemical specificity at position 4. • Lys-NH2 (L-lysine amide): Formulates the amidated C-terminus, conferring a positive charge at physiological pH.

With a compact molecular formula of C38H49N9O5 and an exact average mass of 711.85 g/mol, Ipamorelin exhibits rapid receptor binding kinetics in vitro compared to larger peptide structures.

Salt Forms, TFA Counterions, and Net Peptide Content Calculations

A critical consideration in laboratory research is distinguishing total dry mass (lyophilate weight) from actual net peptide mass. Solid-phase peptide synthesis (SPPS) yields peptides as salt complexes. The chemical purification process typically employs trifluoroacetic acid (TFA) in the mobile phase, yielding peptides as trifluoroacetate salts.

In a lyophilized sample of CJC-1295 or Ipamorelin, positive charges on basic amino acid residues (such as Arg, Lys, His, and the N-terminus) are balanced by TFA counterions (CF3COO-, formula mass 113.01 g/mol) or acetate counterions (CH3COO-, formula mass 59.04 g/mol), along with residual structural water of hydration.

Net peptide content (NPC) typically ranges between 70% and 85% of total dry powder mass. To calculate true molarity in quantitative assay preparation, researchers must consult the lot-specific Certificate of Analysis (COA) for Elemental Analysis (CHN) or Amino Acid Analysis (AAA) data.

For example, if a research sample of Ipamorelin TFA salt exhibits an 80% net peptide content by AAA, a 1.0 mg vial of lyophilized powder contains 0.80 mg of active peptide free base (1.12 micromoles) and 0.20 mg of combined TFA counterions and moisture. High-precision quantitative work requires adjusting reconstitution volumes to reflect net peptide content rather than uncorrected gross mass.

For accurate lab volumetric calculations, investigators can utilize our online reconstitution calculator to align target concentrations with verified mass purity values.

Mechanistic Roles: GHRH Analog vs. GHSR-1a Agonist Receptor Dynamics

Co-formulating CJC-1295 and Ipamorelin targets two distinct endogenous pathways regulating growth hormone secretion from anterior pituitary somatotrophs. Preclinical studies suggest that simultaneous stimulation of these pathways produces a synergistic increase in pulsatile growth hormone release while maintaining physiological feedback mechanisms.

CJC-1295 acts as a selective GHRH receptor agonist. Upon binding the GHRH receptor (a G-protein coupled receptor linked to Gs), it activates adenylyl cyclase, raising intracellular cyclic AMP (cAMP) levels and triggering protein kinase A (PKA) signaling cascades. This pathway stimulates both the transcription of the GH gene and secretagogue granule exocytosis.

Conversely, Ipamorelin acts as a selective agonist of the GHSR-1a (ghrelin receptor), which couples through the Gq/11 protein pathway. Activation of GHSR-1a stimulates phospholipase C (PLC), resulting in the generation of inositol trisphosphate (IP3) and diacylglycerol (DAG). IP3 triggers intracellular calcium release from the endoplasmic reticulum, facilitating vesicle fusion and GH secretion.

In vitro assays demonstrate that co-application of GHRH analogs and GHSR agonists yields a greater total somatotroph secretagogue response than the additive mathematical sum of either compound administered individually. Furthermore, animal models indicate that CJC-1295 sustains baseline growth hormone and downstream insulin-like growth factor 1 (IGF-1) concentrations over extended periods, making the pair a valuable model for tissue repair and metabolic research.

Analytical Verification: HPLC Mass Spectrometry and Lot-Specific COAs

Ensuring precise molecular weight, sequence fidelity, and chemical purity requires rigorous analytical validation. PX1 Research subjects every production lot to independent third-party laboratory verification using standard analytical methodologies:

1. Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC): RP-HPLC measures chromatographic purity by passing the peptide mixture through a C18 hydrophobic stationary phase using an acetonitrile/water gradient containing TFA. The resulting chromatogram establishes purity percentages by measuring peak area integration at 214 nm or 220 nm. Individual peaks for CJC-1295 and Ipamorelin must exhibit sharp peak symmetry with zero detectable high-molecular-weight aggregates or micro-degradation products.

2. Electrospray Ionization Mass Spectrometry (ESI-MS): ESI-MS verifies the monoisotopic and average molecular weights of each constituent. ESI produces multiply charged ions ([M+nH]n+), allowing precise mass assignment for larger peptides like CJC-1295 (MW 3367.97 Da) as well as smaller molecules like Ipamorelin (MW 711.85 Da). Observed m/z spectra must match calculated theoretical mass profiles within tight tolerance margins (typically ± 0.5 Da).

3. Endotoxin and Bioburden Testing: In cell culture models and preclinical tissue research, lipopolysaccharide (LPS) bacterial endotoxins interfere with baseline cell signaling. PX1 Research compounds are verified endotoxin-tested using Kinetic Chromogenic LAL assays, ensuring suitability for sensitive in vitro assays.

Comprehensive documentation for all parameters is available through our dedicated research laboratory portal for COA lookup.

Comparative Structural Analysis Across Somatotropic Peptides

Evaluating secretagogue options requires comparing CJC-1295 and Ipamorelin against other synthetic peptides within the GHRH and GHRP classes. Structural variations impact enzymatic half-life, receptor binding affinity, and secondary signaling cascades in laboratory models.

When compared to early-generation short-acting GHRH fragments like Sermorelin (GRF 1-29 amide, MW 3357.88 g/mol), CJC-1295 No DAC incorporates four strategic amino acid substitutions that significantly prolong plasma stability against DPP-IV cleavage. Similarly, within the GHRP receptor agonist family, Ipamorelin exhibits distinct receptor selectivity compared to older compounds such as GHRP-2 (MW 818.0 Da) or Hexarelin (MW 887.04 Da).

While GHRP-2 and Hexarelin demonstrate high potency, in vitro and animal models show they can induce non-selective elevations in cortisol and prolactin by activating broader neuroendocrine pathways. Ipamorelin's specific pentapeptide sequence (Aib-His-D-2-Nal-D-Phe-Lys-NH2) limits off-target binding, maintaining high somatotroph selectivity without activating systemic stress pathways.

Researchers building specialized research protocols across distinct growth factor classes can reference our complete catalog of research peptides or establish institutional supply lines through our dedicated wholesale laboratory program.

Laboratory Storage Protocols and Reconstitution Dynamics

Maintaining structural integrity and preventing chemical degradation (such as hydrolysis, oxidation, or aggregation) requires adherence to standard laboratory peptide handling procedures.

1. Lyophilized Powder Storage: Upon receipt, unopened vials of lyophilized CJC-1295 / Ipamorelin co-blends should be stored at -20°C for short-to-medium term storage, or -80°C for long-term storage. Lyophilates stored at sub-zero temperatures with desiccant remain stable for extended periods.

2. Reconstitution Protocol: Allow vials to equilibrate to room temperature prior to reconstitution to prevent atmospheric moisture condensation on the cake. Reconstitute using Bacteriostatic Water (0.9% Benzyl Alcohol) or Sterile Water for Injection, depending on assay requirements. Gently stream the solvent along the glass inner wall rather than directly onto the peptide cake, followed by gentle swirling. Avoid mechanical vortexing or vigorous agitation, which can induce physical shear stress and peptide aggregation.

3. Reconstituted Solution Stability: Once solubilized, store aliquots at 2°C to 8°C. For prolonged experimental timelines, store reconstituted stock solutions in single-use aliquots at -80°C to minimize repeated freeze-thaw cycles. Micro-aliquoting minimizes enzymatic hydrolysis and chemical oxidation over time.