AHK-Cu

AHK-Cu is a copper-complexed tripeptide — alanyl-L-histidyl-L-lysine coordinated to a copper(II) ion — in the copper-peptide research family alongside GHK-Cu. Investigators study it as a structurally defined research material for dermal-matrix, angiogenesis, and hair-follicle research models where copper-peptide coordination chemistry is the experimental variable. The peer-reviewed literature catalogs copper tripeptides in extracellular-matrix signaling studies and comparative structure-activity work across the copper-peptide class. Its molecular identity is fixed by structural confirmation against PubChem CID 168431292, empirical formula C15H24ClCuN6O4−. The reference material supplied here is intended for laboratory characterization, in-vitro coordination-chemistry work, and in-cell signaling studies only. For research use only; not for human consumption, medical use, or veterinary application. Researchers should consult primary literature for context-specific experimental conditions.

AHK-Cu is a short linear tripeptide whose copper(II) ion is coordinated through the imidazole nitrogen of the histidine residue together with backbone donor atoms, forming the square-planar copper-peptide geometry documented for this class. The lysine side chain contributes cationic character that the literature associates with the tripeptide’s affinity for anionic extracellular-matrix components. Copper-peptide complexes of this family are documented in the published literature as modulators of angiogenesis-associated signaling and matrix-remodeling pathways in research models. Relative to the more extensively studied GHK-Cu, AHK-Cu is described as a distinct copper-tripeptide with its own coordination and side-chain profile. All activity descriptors here are framed as documented in published research rather than as effects of the supplied product. Structural confirmation is established by mass spectrometry and HPLC-validated purity on each Certificate of Analysis.

Experimental domains documented in the published literature include copper-coordination-chemistry characterization, angiogenesis-signaling assays in endothelial-cell models, extracellular-matrix and collagen-remodeling research, hair-follicle dermal-papilla cell studies, and comparative structure-activity investigations across the copper-tripeptide class alongside GHK-Cu. Investigators use copper-peptide research materials to parse the contribution of the metal-coordination geometry versus the peptide sequence to documented signaling behavior. Use in laboratory research extends to mechanism-elucidation paradigms where the complex serves as a defined copper-tripeptide reference. The reference standard is supplied for these and equivalent in-vitro experimental contexts only, with no associated guidance for human, clinical, or cosmetic use.

Each lot is characterized by reverse-phase HPLC for chromatographic purity and by mass spectrometry for molecular-ion confirmation of the copper-complex against the reported empirical formula. Copper stoichiometry is confirmed by the characteristic complex mass and, where included in the release specification, by elemental copper determination. Purity is reported as an HPLC-area percentage on the Certificate of Analysis distributed with every lot, alongside the molecular-weight match within instrument tolerance. Peptide content and residual water are reported categorically when these parameters are part of the lot release specification. The COA records the lot identifier, manufacturing date, and analytical method versions used, providing a traceable provenance chain from synthesis through release. Researchers requiring batch-level analytical detail should reference the COA distributed with the supplied material.

For laboratory storage, the lyophilized copper-peptide reference standard should be held at −20°C in its sealed, light-protected container until ready for analytical use — copper complexes are light- and oxidation-sensitive, so protection from light is emphasized. 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; avoid strong chelating buffers that would strip the coordinated copper unless the assay specifically requires it. Once reconstituted, store the working solution at 2–8°C, protect from light, and characterize stability in the relevant buffer prior to extended storage. Avoid repeated freeze-thaw cycles of reconstituted material. These handling parameters reflect general best-practice for copper-peptide reference standards and do not constitute preparation guidance for human or cosmetic use.