ReferenceFeaturedGHK-Cu
Copper tripeptide complex — HPLC-verified, COA per lot.
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Custom blend
Two-peptide research blend — HPLC-verified.
Custom blendSize
Price
$68.00
SKU CJC1295-IPAM-5-5
Complimentary shipping over $200
For research use only. Not for human consumption.
Every lot is third-party assayed by HPLC. A lot-specific COA ships with the product and is mirrored to the buyer account.
Real COAs are published per lot when shipments begin. Sample COA available on request.
Scientific Details
This research blend combines two structurally distinct growth-hormone-axis research peptides — CJC-1295 (the modified GRF 1-29 variant) and Ipamorelin — supplied together as a single lyophilized reference material for studies of complementary GH-axis signaling. The peer-reviewed literature catalogs this combination class within paradigms that examine GHRH-receptor agonism alongside ghrelin-receptor (GHS-R1a) agonism in the same experimental session, allowing investigators to dissect the contributions of each receptor family to downstream growth-hormone-axis dynamics. Each component's molecular identity is characterized individually on the supplier's Certificate of Analysis. Component-level details (sequence, molecular weight, CAS, PubChem CID) are documented on the individual reference-standard PDPs linked from the composition panel above. The blend is supplied for laboratory characterization, in-vitro receptor-binding work, and in-cell signaling studies only. For research use only; not for human consumption, medical use, or veterinary application.
The blend's combined molecular profile is the sum of two distinct peptide architectures documented across the published literature. CJC-1295 (without DAC) is a 29-residue GHRH analog with backbone-stabilizing substitutions that preserve N-terminal GHRH-receptor engagement while resisting dipeptidyl peptidase IV cleavage; it engages the class B GPCR GHRH receptor and activates Gs-coupled cAMP signaling. Ipamorelin is a non-natural-residue-containing pentapeptide that engages the growth-hormone secretagogue receptor type 1a (GHS-R1a), activating Gq/PLC calcium signaling. The two components engage non-overlapping receptor families documented in the literature as showing additive or synergistic effects on somatotroph activation in feedback-loop modeling. Pharmacokinetic descriptors for each component are short systemic half-lives under standard parenteral paradigms. All activity descriptors here are framed as documented in published research.
Experimental domains documented in the published literature for combined GHRH-and-GHRP research paradigms include comparative receptor-engagement studies parsing GHRH-receptor agonism from GHS-R1a agonism, somatotroph-cell calcium-and-cAMP dual-signaling assays, feedback-loop modeling under combined receptor stimulation, and structure-activity work probing how the two receptor families integrate downstream growth-hormone-axis dynamics. Investigators use blended research materials of this kind to study the additive-versus-synergistic question — whether engaging GHRH and ghrelin receptors simultaneously produces effects distinct from either alone — without managing two separate vials. Use in laboratory research extends to mechanism-elucidation paradigms where the blend serves as a defined dual-mechanism GH-axis reference. The blend is supplied for these and equivalent in-vitro experimental contexts only, with no associated guidance for human, clinical, or veterinary application.
Each component of the blend is characterized individually before combination. Reverse-phase HPLC is performed on the lyophilized blend to verify the relative composition ratio of the two components, with each component identified by its characteristic retention time and confirmed by mass spectrometry molecular-ion match against the empirical formulas reported on the COAs. Purity is reported as combined HPLC-area composition on the blend's Certificate of Analysis, alongside the molecular-weight match for each component within instrument tolerance. Peptide content where applicable is determined by amino-acid analysis or nitrogen-content assay following the analytical method specified on the COA. The COA records the lot identifier, the relative amount of each component as supplied, the manufacturing date, and analytical method versions used. Researchers requiring component-level analytical detail should reference the component PDPs linked from the composition panel above and the COA distributed with the supplied blend.
For laboratory storage, the lyophilized blend should be held at −20°C in its sealed, light-protected container until ready for analytical use. Allow vials to equilibrate to ambient temperature before opening to avoid moisture condensation on the lyophile. Reconstitution for in-vitro experimental use is typically performed in bacteriostatic water or a researcher-selected buffer compatible with the downstream assay; once reconstituted, store the working solution at 2–8°C and characterize stability in the relevant buffer prior to extended storage. Combined-peptide blends may exhibit aggregation or differential-stability behavior in some buffer systems — assay-specific stability characterization for both components is recommended. Avoid repeated freeze-thaw cycles of reconstituted material — single-use aliquots are preferred for experiments where blend composition stability is assay-critical. These handling parameters reflect general best-practice for combined lyophilized peptide reference materials and do not constitute preparation guidance for human or veterinary application.
A selection of reference standards from the catalog.
ReferenceFeaturedCopper tripeptide complex — HPLC-verified, COA per lot.
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