2X Blend CJC-1295 Without DAC (5mg) / Ipamorelin (5mg)

$80.00

SKU: YPB.238 Categories: ,

Description

A 1:1 blend by mass of CJC-1295 (No DAC) and Ipamorelin supplied for controlled research environments. This co-formulation is suitable for studies exploring GHRH-receptor and ghrelin (GHS-R1a)–receptor signaling pathways when evaluated together in model systems.


Composition

• CJC-1295 (Without DAC)
• Ipamorelin
Appearance: Lyophilized powder in a sealed research vial


Research Focus (non-clinical)

• Comparative and combined pathway evaluation of GHRH analog + GHS agonist in in-vitro or ex-vivo models
• Assessment of assay development, including chromatographic separation of co-formulated peptides
• Stability characterization of a two-analyte lyophilized blend under laboratory storage conditions

For qualified research professionals and institutional laboratories. Not for human use.


Documentation & Quality Assurance

Each lot is sourced through our verified global supply chain with emphasis on traceability and quality control. We work diligently to obtain and maintain third-party analytical reports (HPLC/LC-MS) and Certificates of Analysis for each batch, as part of our ongoing quality process. These documents are reviewed internally and displayed as they become available. Independent third-party testing is also performed on select lots to confirm identity, purity, and alignment with our internal specifications.


Important Notice

This product is intended for laboratory research use only. It is not intended for human or veterinary use, and must not be used for diagnostic, therapeutic, or clinical purposes.
This material is not a drug, medical device, or dietary supplement, and has not been evaluated by the U.S. Food and Drug Administration.


Quality & Manufacturing

All materials are sourced from carefully vetted domestic and international manufacturing partners who follow quality systems consistent with ISO and cGMP principles. Each supplier is reviewed for reliability, documentation integrity, and transparency in testing.

We require a verified purity of 99% or higher and perform independent third-party spot testing to confirm that select lots meet our internal standards for identity, purity, and composition. Where available, endotoxin testing results are included on Certificates of Analysis to verify laboratory purity; their inclusion is for research quality assessment only and does not imply suitability for human or veterinary use.

All research materials are sealed for integrity and packaged for stability during storage and transport from manufacturing through final delivery.

Additional information

Weight 0.2 lbs

Storage Instructions

All our research peptides are manufactured using a lyophilization (freeze-drying) process. This method is designed to maintain product integrity and allows vials to remain stable during shipping for approximately 3–4 months.

Once a vial is reconstituted with bacteriostatic water, it should be stored in the refrigerator to help maintain stability. Under these conditions, reconstituted material is generally considered stable for up to 30 days.

Lyophilization is a dehydration technique in which compounds are frozen and then exposed to low pressure. This causes the water in the vial to sublimate directly from solid to gas, leaving behind a stable, crystalline white structure. This powder can be kept at room temperature until reconstitution.

Upon receipt, products should be stored away from heat and light. For short-term use, refrigeration at approximately 4°C (39°F) is suitable. For long-term storage (several months to years), vials may be placed in a freezer at approximately -80°C (-112°F). Freezing is the preferred method for preserving product stability over extended periods.

⚠️ Important Notice: These products are intended for research use only. Not for human consumption.

Certificate of Analysis

Every batch undergoes rigorous third-party laboratory testing to verify identity, purity (≥98%), and quality before release.

View Certificate of Analysis
Third-Party Verified ≥98% Purity HPLC & MS Tested

Research Use Only

These studies reference research-grade peptides for laboratory and scientific investigation only. Not for human consumption. Not intended to diagnose, treat, cure, or prevent any disease.

Published Scientific Research

Peer-reviewed laboratory research investigating growth hormone peptides from leading scientific databases

Molecular Analysis
PubMed

Ghrelin gene products and the regulation of food intake and gut motility.

Pharmacological reviews 2009

A breakthrough using "reverse pharmacology" identified and characterized acyl ghrelin from the stomach as the endogenous cognate ligand for the growth hormone (GH) secretagogue receptor (GHS-R) 1a. To date, ghrelin is the only protein to be octanylated, and inhibition of GOAT may have effects only on the stomach and is unlikely to affect the synthesis of other proteins.

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In Vitro Study
PubMed

Ghrelin: from a GH-secretagogue to the regulation of food intake, sleep and anxiety.

Pediatric endocrinology reviews : PER 2004

Grhelin is an endogenous ligand for the growth hormone secretagogue receptor from the stomach. Ghrelin has other significant actions, including control of acid secretion, influences on sleep and on the regulation of anxiety.

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In Vitro Study
PubMed

The role of ghrelin and growth hormone secretagogues receptor on rat adipogenesis.

Endocrinology 2003

Recent research progress indicates a close link between ghrelin, a natural ligand of GH secretagogues receptor (GHS-R), and both the metabolic balance and body composition. To clarify the involvement of ghrelin and GHS-R in the process of adipogenesis, we measured the expression of GHS-R and peroxisome proliferator-activated receptor gamma 2 (PPAR-gamma 2) mRNA in rat adipocytes using semiquantitative RT-PCR methods.

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Molecular Analysis
PubMed

Ghrelin -- a new endogenous growth hormone secretagogue.

Physiological research 2002

Ghrelin is a new endogenous peptide, discovered in 1999 by Kojima et al., as the result of a search for an endogenous ligand for an orphan receptor of known structure and function. Its discovery is related to the development of a new hypothesis regarding the regulation of growth hormone secretion.

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Molecular Analysis
PubMed

Biologic activities of growth hormone secretagogues in humans.

Endocrine 2001

GHSs release GH via actions on specific receptors (GHS-R) at the pituitary and, mainly, at the hypothalamic levels. Estrogens play a major role in enhancing the GH response to GHSs at puberty, which GHRH hypoactivity, somatostatinergic hyperactivity and impaired activity of the putative GHS-like ligand and receptors probably explain the reduced GH-releasing effect of GHSs in aging.

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Molecular Analysis
PubMed

Physiology and possible pathology of growth hormone secretagogues.

Journal of pediatric endocrinology & metabolism : JPEM 2001

Recently an endogenous ligand for the GHS receptor, ghrelin, was discovered, suggesting that this may be the third factor in the control of GH secretion. Moreover, the presence of ghrelin in rat and human placenta has been reported, suggesting a possible role of this peptide in the local modulation of GH release and in maternal and fetal pituitary secretion.

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