📄 Certificate of Analysis available on request
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Series-3 Research Bundle is supplied as a set of laboratory research compounds with defined reference identities. The set contains Epithalon, GHK-Cu, NAD+, each in its own vial.
This listing is limited to product identity, analytical documentation, and research-use status. Each component is provided for qualified laboratory research only and is not intended for human or veterinary use. Each batch is independently tested for identity, purity, and consistency, with a lot-specific Certificate of Analysis provided for documentation and internal research records.
Each compound in this set has been characterised in preclinical laboratory models. The primary studies below, in animal and in-vitro models, examined cellular, biochemical, and mechanistic endpoints. The literature is preclinical: it describes the compounds, not any outcome in humans.
Animal modelEffect of epitalon on the lifespan increase in Drosophila melanogasterIn the Drosophila melanogaster model, the peptide was studied for an imago-lifespan endpoint, a geroprotection readout in an invertebrate model.Read the study ↗
In vitroEpitalon-activated telomerase enhance bovine oocyte maturation rate and post-thawed embryo developmentIn bovine cumulus-oocyte complexes in vitro, the peptide acted as a telomerase activator, linking cumulus-cell telomerase activity to oocyte-maturation endpoints.Read the study ↗
In vitroStimulation of collagen synthesis in fibroblast cultures by the tripeptide-copper complex glycyl-L-histidyl-L-lysine-Cu2+In cultured fibroblasts, the copper complex dose-dependently raised collagen synthesis at the cell level.Read the study ↗
In vitroStimulation of sulfated glycosaminoglycan synthesis by the tripeptide-copper complex glycyl-L-histidyl-L-lysine-Cu2+In cultured fibroblasts, the copper complex dose-dependently increased sulfated glycosaminoglycan synthesis measured by 35S-sulfate incorporation.Read the study ↗
Animal modelMuscle type-specific responses to NAD+ salvage biosynthesis promote muscle function in Caenorhabditis elegansIn C. elegans, perturbing the nicotinamide-NAD+ salvage pathway produced tissue-specific effects, implicating salvage-pathway flux as a determinant of tissue NAD+ supply.Read the study ↗
Animal modelAn NAD(+) biosynthetic pathway enzyme functions cell non-autonomously in C. elegans developmentIn C. elegans, loss of the NAD+ salvage enzyme PNC-1 drove developmental phenotypes cell non-autonomously, indicating the enzyme regulates NAD+ metabolite levels across tissues.Read the study ↗
Full documentation, on the record. A Certificate of Analysis and a Safety Data Sheet are available on request for every batch.
Links open the original study on PubMed. For research and educational purposes, descriptive of the published preclinical literature, not therapeutic claims about any ai-peptides product.
