Epithalon (10mg)

Epithalon Research Background

Epithalon (also written Epitalon or Epithalone) is a short synthetic tetrapeptide with the sequence Ala-Glu-Asp-Gly (alanyl-glutamyl-aspartyl-glycine). Assigned CAS number 307297-39-8 and the molecular formula C14H22N4O9, it is a four-residue peptide of roughly 390 g/mol supplied here at 10 mg per research vial. The sequence was derived as a synthetic analogue intended to correspond to the active core of a longer pineal-gland polypeptide preparation studied in the gerontology literature, and Epithalon is produced entirely by solid-phase synthesis rather than isolated from tissue. Because it is one of the smallest peptides frequently encountered in aging-related benchwork, it is often used as a compact, sequence-defined model compound in that research area.

Interest in Epithalon as a research material centers on how such a minimal, highly polar tetrapeptide behaves in cell-culture and preclinical systems, and on its reported in-vitro interactions with pathways associated with cellular senescence. It has no established consumer application. The surrounding body of work is preliminary and ongoing, is drawn largely from in-vitro assays and rodent or invertebrate models, and should not be extrapolated to human or animal outcomes.

What Has Been Studied in Preclinical Models

Published investigations of Epithalon are predominantly in-vitro and animal-model in nature. A recurring line of inquiry involves telomere biology: cell-culture studies have examined whether exposure is associated with changes in telomerase activity and telomere length in cultured human somatic cell lines, making the peptide a frequently cited tool compound in senescence and replicative-lifespan assays. Other reported experimental endpoints include gene-expression and chromatin studies, circadian and melatonin-related signaling in pineal-tissue models, and lifespan or biomarker observations in rodent and Drosophila cohorts under controlled laboratory conditions.

• Cell-culture assays examining telomerase activity and telomere length in cultured human fibroblast and somatic cell lines.
• Replicative-senescence and population-doubling studies used to characterize the peptide as a research tool compound.
• Rodent and invertebrate (Drosophila) models reporting lifespan and physiological-biomarker endpoints.
• Mechanistic work on melatonin, circadian, and gene-expression pathways in pineal-tissue and chromatin models.

Analytical Characterization

Each research lot is supplied as a lyophilized white powder and characterized before release. Identity and purity are established using orthogonal analytical methods so that the material on the Certificate of Analysis (COA) matches the sequence and mass expected for the Ala-Glu-Asp-Gly tetrapeptide. This dual approach separates purity (how much of the sample is the target peptide) from identity (confirmation that the target is the correct molecule).

• HPLC (RP-HPLC) purity: quantified by peak-area integration, with lot purity reported on the COA at greater than or equal to 98%. The chromatogram resolves the main peak from process-related impurities, and because Epithalon is small and very hydrophilic it typically elutes early, so ion-pairing methods are commonly used to retain and resolve it.
• Mass-spectrometry identity: ESI-MS or MALDI-TOF confirms the observed monoisotopic/average mass against the theoretical value for C14H22N4O9, verifying molecular identity.
• Supporting data: appearance, net peptide content, and residual-solvent or water-content checks where applicable.

The COA accompanying each product is the definitive analytical record for that specific lot. Because purity and mass can vary slightly between synthesis batches, researchers should reference the COA tied to the lot number received rather than generic specifications when documenting experimental inputs. Retaining the COA alongside experimental records supports reproducibility and traceability.

Laboratory Handling of Lyophilized Material

As a lyophilized peptide, Epithalon is hygroscopic and sensitive to repeated temperature cycling. Standard laboratory practice is to allow sealed vials to equilibrate to room temperature before opening to minimize condensation, and to reconstitute with an appropriate research-grade aqueous solvent under aseptic technique; the tetrapeptide's high polarity and acidic residues make it readily water-soluble. Aliquoting reconstituted stock into single-use portions limits freeze-thaw cycles that can degrade peptide integrity. Detailed temperature and stability windows for lyophilized, reconstituted, and working solutions appear in the storage table on this page.