Blend CJC 1295 NO DAC 5mg with Ipamorelin 5mg

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Buy 2 Get 1 Free Blend CJC 1295 NO DAC 5MG with Ipamorelin 5MG :
| Unit Size | 10 mg/vial |
| Unit Quantity | 1 vial |
| Purity (Mass Spectrometry and UV) | 99.75% Nominal Target: 5 mg CJC 1295 NO DAC + 5 mg Ipamorelin |
| Sequence (CJC 1295 NO DAC) | H-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 |
| Sequence (IPAMORELIN) | Aib-His-D-2-Nal-D-Phe-Lys-NH2 |
| Molecular Formula (CJC 1295 NO DAC) |
C152H252N44O42 |
| Molecular Formula (IPAMORELIN) | C38H49N9O5 |
| Appearance | Lyophilized White Powder |
| Source | Chemical Synthesis |
| Storage | Lyophilized Blend CJC 1295 NO DAC with Ipamorelin is stable at roomTemperature for 90 days, however it is best to store in a freezer below - 8c for any extended period of time. |
| Terms | The products we offer are intended for laboratory research use only. Please familiarize yourself with our terms of service prior to ordering. |
Blend CJC-1295 NO-DAC 5mg with Ipamorelin 5mg
View Research Overview & References
This blend combines two synthetic peptides for use in in vitro laboratory research on growth-related receptor signaling. CJC-1295 NO-DAC is an analog of human growth hormone-releasing hormone (GHRH), sharing a modified version of the first 29 amino acids of the 44-amino-acid GHRH sequence.
Ipamorelin is a structurally distinct five-amino-acid peptide that mimics ghrelin and acts on a separate receptor, the growth hormone secretagogue receptor (GHS-R). The two peptides are studied together because they engage complementary receptor pathways in laboratory receptor-signaling research.
GHRH Receptor Binding Research
Computational and structural research has characterized the dynamic properties of the GHRH receptor and the molecular determinants involved in GHRH binding, providing a receptor-level basis for studying how GHRH analogs such as CJC-1295 NO-DAC engage this receptor.1
Peptide Stability Research
Native GHRH is understood to be rapidly degraded in plasma through enzymatic cleavage by dipeptidyl peptidase IV (DPP-IV) near the N-terminus, along with chemical rearrangement and oxidation at other positions in the sequence.
These degradation pathways are the chemical rationale researchers cite for the stabilizing amino acid substitutions present in long-acting GHRH analogs such as CJC-1295 NO-DAC, which are designed to resist these specific routes of enzymatic and chemical inactivation.
Ipamorelin Structural Considerations
Ipamorelin's structure incorporates D-2-naphthylalanine, a bulky non-natural amino acid studied for its contribution to GHS-R binding affinity through improved hydrophobic contact within the receptor's binding pocket, a structural feature it shares with the related peptide GHRP-2.
Analytical Verification for Blended Products
For a two-component blend, analytical verification is understood to require confirmation of both the individual identity and purity of each peptide and the ratio between them, since a single aggregate purity figure could not distinguish a properly balanced blend from one skewed toward one component.
Researchers reviewing documentation for this blend are encouraged to look for individual HPLC or mass spectrometry data for CJC-1295 NO-DAC and Ipamorelin separately.
Storage and Handling in the Laboratory Setting
As with the individual peptides, the lyophilized blend is stored under sub-zero freezer conditions to preserve the stability of both components, consistent with standard handling practices for combination research peptide products.
Important Notice
These peptides are synthesized, combined, and distributed strictly for in vitro research purposes only. They are not intended for human consumption, medical use, or diagnostic use, and have not been evaluated for safety or efficacy in humans.
Product Information
This combination is provided as a white lyophilized powder, with a concentration of 10 mg per vial (5 mg of each peptide).
References
1. Matsoukas MT, Spyroulias GA. Dynamic properties of the growth hormone-releasing hormone receptor (GHRHR) and molecular determinants of GHRH binding. Mol Biosyst. 2017;13(7):1313-1322.
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