Ovagen Product Description
Ovagen is a three-residue peptide built from glutamic acid, aspartic acid, and leucine, joined in the sequence Glu-Asp-Leu. Its compact size places it in the class of ultrashort peptides, defined in the literature as sequences of roughly two to seven amino acid residues.
The peptide is catalogued in public chemistry records under PubChem CID 444128 and carries the molecular formula C₁₅H₂₅N₃O₈. Its identity is fixed by the InChIKey JVSBYEDSSRZQGV-GUBZILKMSA-N, which allows laboratories to confirm the exact stereochemistry they are working with.
EDL appears in the research literature alongside related short sequences such as AEDG, EDR, and AEDL. Laboratories working across this series often compare sequences side by side, since small changes in residue order alter how each peptide behaves in cell-free and cultured-cell systems.
Compound Specifications
| Property |
Value |
| PubChem CID |
444128 |
| Molecular Formula |
C₁₅H₂₅N₃O₈ |
| Molecular Weight |
375.37 g/mol |
| Monoisotopic Mass |
375.16416 Da |
| InChIKey |
JVSBYEDSSRZQGV-GUBZILKMSA-N |
| IUPAC Name |
(2S)-2-[[(2S)-2-[[(2S)-2-amino-4-carboxybutanoyl]amino]-3-carboxypropanoyl]amino]-4-methylpentanoic acid |
| ChEBI ID |
CHEBI:137252 |
| Amino Acid Sequence |
Glu-Asp-Leu (EDL), one-letter EDL |
| Sequence Length |
3 residues |
| Source |
Synthetic |
| Purity |
≥99% (HPLC) |
| Appearance |
Lyophilized white powder |
| Solubility |
Soluble in water |
| Storage |
-20°C, protect from light |
Storage and Handling
- Store the lyophilized compound at -20°C, protected from light.
- After reconstitution, store at 2°C to 8°C and use promptly.
- Maintain aseptic handling to preserve compound integrity.
- Avoid repeated freeze-thaw cycles of reconstituted material.
Lyophilized Format
This compound ships in lyophilized (freeze-dried) form. Freeze-drying supports long-term storage stability and preserves compound integrity. No fillers are added.
Ovagen Research
A systematic review of short peptides catalogued how sequences of two to seven residues have been studied in relation to gene expression and protein synthesis across plant, microbial, insect, rodent, and primate models [1]. That review describes short peptides entering cell nuclei and nucleoli and interacting with nucleosomes, histone proteins, and both single-stranded and double-stranded DNA.
Fluorescence work supports that picture at the cellular level. Labelled short peptides were tracked into the cytoplasm, nucleus, and nucleolus of HeLa cells, and fluorescence-quenching constants indicated sequence-selective binding to deoxyribooligonucleotides, including discrimination of cytosine methylation status [2]. Companion work reported binding of short peptides to labelled histones H1, H2B, H3, and H4, with the interaction depending on both the histone and the peptide primary structure [3]. Together these lines describe an epigenetic-level interaction rather than a receptor-mediated one.
How such peptides reach the intracellular compartment has been modelled directly. EDL was included in a docking study of 26 catalogued ultrashort peptides against the LAT1, LAT2, PEPT1, and PEPT2 carrier proteins, where it returned binding scores placing it among the stronger ligands of the LAT1 amino acid transporter [4]. A companion review examined the same carrier families across tissue types and proposed that carrier distribution helps account for the tissue selectivity reported for individual sequences [5].
Beyond the modelling work, EDL itself has been examined in animal tissue models.
Sequence-Specific Research on EDL
EDL was assessed in rodent renal tissue models of gentamicin exposure and ischemia-reperfusion, where the study authors recorded changes in antioxidant enzyme activity, lipid peroxidation markers, and cellular energy parameters [6]. An earlier study in the same research line compared EDL against AED and AEDG in a cisplatin renal model and reported changes in filtration and electrolyte handling parameters [7].
Related Khavinson sequences have also been examined in cultured cells. Five peptides from the series were incubated with the THP-1 monocytic cell line, where researchers recorded changes in tyrosine phosphorylation of mitogen-activated cytoplasmic kinases and in cytokine expression following lipopolysaccharide exposure [8].
| Research Area |
In Vitro Application |
| Gene Expression Research |
Evaluation of peptide interaction with DNA, nucleosomes, and histone proteins in cell-free systems |
| Peptide Transport Research |
Molecular docking and uptake assays involving LAT and PEPT family carrier proteins |
| Epigenetic Research |
Assessment of sequence-selective binding to methylated and unmethylated oligonucleotides |
| Cell Culture Models |
Comparative characterization of ultrashort peptide sequences in cultured cell lines |
| Analytical Method Development |
Reference material for HPLC and LC-MS identity and purity workflows |
References
- Khavinson VK, Popovich IG, Linkova NS, Mironova ES, Ilina AR (2021). Peptide Regulation of Gene Expression: A Systematic Review. Molecules, 26(22), 7053. https://pmc.ncbi.nlm.nih.gov/articles/PMC8619776/
- Fedoreyeva LI, Kireev II, Khavinson VKh, Vanyushin BF (2011). Penetration of short fluorescence-labeled peptides into the nucleus in HeLa cells and in vitro specific interaction of the peptides with deoxyribooligonucleotides and DNA. Biochemistry (Moscow), 76(11), 1210-1219. https://link.springer.com/article/10.1134/S0006297911110022
- Fedoreyeva LI, Smirnova TA, Kolomijtseva GYa, Khavinson VKh, Vanyushin BF (2013). Interaction of short peptides with FITC-labeled wheat histones and their complexes with deoxyribooligonucleotides. Biochemistry (Moscow), 78(2), 166-175. https://link.springer.com/article/10.1134/S0006297913020053
- Khavinson VK, Linkova NS, Rudskoy AI, Petukhov MG (2023). Feasibility of Transport of 26 Biologically Active Ultrashort Peptides via LAT and PEPT Family Transporters. Biomolecules, 13(3), 552. https://pmc.ncbi.nlm.nih.gov/articles/PMC10046148/
- Khavinson V, Linkova N, Kozhevnikova E, Dyatlova A, Petukhov M (2022). Transport of Biologically Active Ultrashort Peptides Using POT and LAT Carriers. International Journal of Molecular Sciences, 23(14), 7733. https://pmc.ncbi.nlm.nih.gov/articles/PMC9323678/
- Zamorskii II, Shchudrova TS, Lin’kova NS, Nichik TE, Khavinson VKh (2017). Nephroprotective Effect of EDL Peptide at Acute Injury of Kidneys of Different Genesis. Bulletin of Experimental Biology and Medicine, 163(3), 389-393. https://link.springer.com/article/10.1007/s10517-017-3811-1
- Zamorskii II, Shchudrova TS, Lin’kova NS, Nichik TE, Khavinson VKh (2015). Peptides Restore Functional State of the Kidneys During Cisplatin-Induced Acute Renal Failure. Bulletin of Experimental Biology and Medicine, 159(6), 736-739. https://link.springer.com/article/10.1007/s10517-015-3062-y
- Avolio F, Martinotti S, Khavinson VKh, Esposito JE, Giambuzzi G, Marino A, Mironova E, Pulcini R, Robuffo I, Bologna G, Simeone P, Lanuti P, Guarnieri S, Trofimova S, Procopio AD, Toniato E (2022). Peptides Regulating Proliferative Activity and Inflammatory Pathways in the Monocyte/Macrophage THP-1 Cell Line. International Journal of Molecular Sciences, 23(7), 3607. https://pmc.ncbi.nlm.nih.gov/articles/PMC8999041/
Certificate of Analysis (COA) for Every Batch
A Certificate of Analysis (COA) is a document that verifies a compound’s identity, purity, and batch quality through independent laboratory testing. Every compound from BioLongevity Labs ships with a COA tied to its specific batch, so researchers can confirm exactly what they received before it enters a protocol.
Each COA reports results from third-party laboratory analysis, including:
- Ultra-high-performance liquid chromatography with mass spectrometry (UHPLC-MS) for purity, typically confirmed at 99% or higher
- Mass identification for molecular confirmation and content quantitation
- Endotoxin quantitation by Limulus amebocyte lysate (LAL) assay where applicable
- Visual and physical characterization of the finished material
How to verify a COA independently
Every certificate can be checked against the issuing laboratory’s own records, not just the copy hosted here. Verification does not depend on BioLongevity Labs.
- MDx BioAnalytical Laboratory certificates carry a QC tracking number and a search code. Newer certificates also carry a QR code. Scan the code, or enter the search code at mdxbiolabs.com, to pull the official record.
- BioRegen reports of analysis carry a Report ID and a Validation Key. Scan the QR code on the certificate to open the official record, or reference both identifiers when contacting the laboratory at the address printed on the report.
- SafeCert Labs certificates, which appear on a number of earlier batches, carry a COA number and the signature of the reporting chemist. Reference that number when requesting confirmation from the laboratory directly.
Batches are frequently tested by both laboratories independently. When two certificates exist for the same lot, each one resolves at its own issuing laboratory, which lets a researcher confirm the same material twice through two unrelated sources.
COAs are sourced from independent certified labs rather than in-house testing alone, giving researchers a verifiable record of molecular integrity for each batch. All compounds are supplied for research use only.
Review the COAs for this batch below, or browse the full COA library.
Endotoxin Ovagen
Ovagen (251522)
Ovagen (251522E)
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