Vilon 20mg

Description

Disclaimer: Vilon is not approved by the U.S. Food and Drug Administration (FDA) for human or veterinary use. It is intended strictly for laboratory and research purposes only.

What is Vilon?

Vilon is a synthetic dipeptide belonging to the peptide bioregulator class, with the amino acid sequence Lys-Glu (KE). It is a tissue-derived short regulatory peptide originally isolated from the thymus gland and is categorized within the cytomechin family of peptide bioregulators, a group of compounds investigated in preclinical models for their proposed capacity to modulate immune cell transcriptional activity, chromatin accessibility, and gene expression dynamics in target tissue-specific cell preparations.

Vilon is among the shortest characterized members of the cytomechin class and has been investigated in preclinical and in vitro settings as a thymus-associated peptide bioregulator. Research interest in Vilon centers on its proposed interactions with chromatin-associated proteins in immune cell preparations, its reported capacity to modulate lymphocyte transcriptional activity in aging research models, and its utility as a laboratory tool for studying the mechanistic basis of dipeptide bioregulator activity in immunological cell systems.

Vilon is not an approved therapeutic compound. It is intended exclusively for qualified researchers operating in controlled laboratory environments. It is not a dietary supplement or consumer product and has no approved indications for human or veterinary use.

PROPERTIES OF VILON

Property	Details
CAS Number	45234-02-4
Molar Mass	257.30 g/mol
Chemical Formula	C₁₁H₂₁N₃O₅
Stability / Shelf Life	24 months when stored lyophilized at −20°C under recommended conditions
Synonyms	KE peptide; Lys-Glu; Lysylglutamic acid; Normophthal; thymus dipeptide bioregulator
Storage Instructions	−20°C (lyophilized); protect from light, heat, and moisture
Amino Acid Sequence	Lys-Glu (KE)
WADA Status	Not listed on the WADA 2026 Prohibited List

WORKING MECHANISM OF VILON

Vilon is proposed to exert its observed regulatory activity in experimental models through interaction with chromatin-associated histone proteins, consistent with the general mechanistic framework described for the cytomechin peptide bioregulator class in published preclinical literature. In cell-free and cell-based laboratory systems, the KE dipeptide sequence has been proposed to associate with histone fractions involved in chromatin condensation, modulating the structural accessibility of heterochromatin-associated gene sequences in thymus-relevant and immune cell preparations.

Mechanistically, Vilon is thought to influence:

• Deheterochromatinization of facultative heterochromatin in lymphocyte preparations from aged subjects, documented in cell culture studies using cytological and molecular detection methods
• Activation of ribosomal gene transcription in lymphocyte preparations, observed as increased nucleolus organizer region activity following Vilon exposure in experimental cell culture systems
• Release of genes repressed due to condensation of euchromatic regions forming facultative heterochromatin, observed in lymphocyte chromosome preparations under controlled in vitro conditions
• Tissue-preferential activity in thymus and lymphoid cell models, with proposed effects on chromatin accessibility that differ from related cytomechin class peptides in the pattern of heterochromatin modification

The precise molecular receptor or binding partner for Vilon has not been definitively identified in the published literature. As the shortest characterized member of the cytomechin class, the mechanistic basis for Vilon’s proposed activity is subject to ongoing investigation. The compound is proposed to act at the chromatin level through histone-associated protein interactions rather than through classical membrane receptor-ligand kinetics. All mechanistic findings relevant to Vilon are derived from the cytomechin class literature and direct compound-specific preclinical cell culture studies. Findings are not consistent across all experimental systems examined.

What are the Potential Research Observations of Vilon?

The following research findings are based on articles retrieved from PubMed and are reported from preclinical and in vitro studies only. These findings do not constitute clinical evidence.

Thymus-Associated Peptide Bioregulator Activity in Immune Cell Models:

Vilon has been investigated in preclinical models as a thymus-derived peptide bioregulator with proposed activity in lymphoid and immune cell preparations. In cell-based laboratory systems, the KE dipeptide was studied for its effects on structural and facultative heterochromatin of cultured lymphocytes from aged subjects. Vilon was observed to induce deheterochromatinization of facultative heterochromatin, activate ribosomal gene transcription as indicated by nucleolus organizer region staining, and release genes repressed due to condensation of euchromatic regions in chromosome preparations. Notably, Vilon did not induce decondensation of pericentromeric structural heterochromatin, distinguishing its activity profile from related compounds such as Epithalon and Livagen. Findings are from controlled in vitro cell culture systems and have not been validated in clinical contexts. [Lezhava et al., 2004]

Lymphocyte Transcriptional Activity and Aging Research Models:

Vilon has been studied in preclinical models examining transcriptional activity in lymphocyte preparations in the context of aging research. In a comparative in vitro study examining multiple short peptide bioregulators, including Epithalon, Livagen, and Vilon in lymphocyte cultures from elderly donors, all three compounds were associated with activation of chromatin through deheterochromatinization of nucleolus organizer regions. Vilon’s chromatin activation profile was characterized as operating primarily through facultative heterochromatin reactivation, contributing to the understanding of the mechanistic differences among short peptide bioregulators. Observations require compound-specific validation and have not been replicated in clinical settings. [Lezhava et al., 2006]

Chromatin Remodeling in Comparative Cytomechin Class Research:

Vilon has been studied comparatively alongside related tissue-derived peptide bioregulators, including Livagen (KEDA, liver-derived), Vesilute (ED, bladder), and Epithalon (AEDG, pineal), in research frameworks examining structural determinants of short peptide bioregulator activity. Comparative studies have used the KE sequence to probe the minimum structural requirements for cytomechin class transcriptional regulatory activity in target tissue cell preparations, and have documented differential effects on pericentromeric versus facultative heterochromatin across the compound series. Observations are from controlled preclinical systems, and findings are not consistent across all experimental models examined. [Lezhava et al., 2004]

Immune Cell Biology and Thymic Function Research Models:

Vilon has been employed as a research tool in preclinical investigations examining the role of thymus-derived short peptides in immune cell biology. In vitro preparations examining lymphocyte chromatin dynamics have incorporated Vilon as a reference compound for investigating the mechanistic contribution of short thymic peptide sequences to immune cell transcriptional regulatory activity. These observations are limited to cell-based experimental systems and require independent replication. [Lezhava et al., 2004]

Note: Vilon is not approved by the U.S. Food and Drug Administration (FDA) for human or veterinary use. It has no approved therapeutic indications. This compound is intended strictly for scientific research purposes only.

Safety Profile and Toxicological Considerations

Researchers have noted the following observations in experimental settings. Long-term safety data remain absent, and a complete toxicity profile has not been established in any biological system.

• Published in vitro data do not report significant cytotoxicity in cell preparations exposed to Vilon at research-relevant concentrations, consistent with the general tolerability profile reported for related short peptide bioregulators in the cytomechin class
• No LD50 or chronic toxicity data are available in the peer-reviewed literature specifically for Vilon
• No human pharmacokinetic, pharmacodynamic, or clinical safety profile has been established for this compound
• Inadvertent laboratory exposure risks are not characterized; no human safety data exists
• Immunogenicity, organ-level toxicity, and off-target transcriptional effects remain uncharacterized at the preclinical level
• As a synthetic dipeptide, Vilon is expected to be highly susceptible to rapid proteolytic degradation in biological matrices due to its minimal chain length, which must be carefully accounted for in experimental design, dosing strategy, and result interpretation
• Repeated freeze-thaw cycles are associated with reduced peptide integrity and should be avoided in research preparations

WHY CHOOSE RCDBIO FOR VILON?

Each batch of Vilon supplied by RCDbio undergoes independent third-party laboratory testing, with a batch-specific Certificate of Analysis (COA) available for researcher verification before experimental use.

• Independent third-party laboratory testing per batch
• COA confirming compound identity and purity per lot
• Molecular identity confirmed against CAS 45234-02-4
• RCDbio does not self-certify; all quality verification is conducted by accredited independent laboratories

Disclosure: Sponsored by RCDbio. This content is for informational purposes only and does not constitute an endorsement of any product for human use.

FREQUENTLY ASKED QUESTIONS

Is Vilon approved for human use?

No. Vilon is not approved by the FDA for any human or medical application. It is classified as a research-use peptide only and has no approved therapeutic indications in the United States or any other regulatory jurisdiction. It is intended exclusively for qualified researchers in controlled laboratory settings.

What is Vilon, and what tissue is it derived from?

Vilon is a synthetic dipeptide with the sequence Lys-Glu (KE), originally isolated from thymus gland tissue. It is among the shortest characterized members of the cytomechin class of tissue-derived short peptide bioregulators, a group of compounds studied in preclinical models for their proposed tissue-specific transcriptional regulatory activity. Related compounds in this research class include Vesilute (ED, bladder), Livagen (KEDA, liver-derived), and Epithalon (AEDG, pineal), all of which share the general cytomechin class mechanistic framework while exhibiting distinct sequence-dependent activity profiles.

What molecular target is Vilon proposed to interact with in research models?

Based on published in vitro research, Vilon is proposed to interact with chromatin-associated histone proteins involved in the condensation of facultative heterochromatin, modulating the accessibility of previously silenced gene regions in thymus-relevant immune cell preparations. As a dipeptide, Vilon represents the minimal structural unit investigated for cytomechin-class activity. Notably, published data indicate that Vilon does not induce decondensation of pericentromeric structural heterochromatin, distinguishing it from related compounds such as Epithalon and Livagen in its chromatin interaction profile.

How should Vilon be stored in a laboratory setting?

Lyophilized Vilon should be stored at −20°C in a sealed, desiccated container protected from light, heat, and moisture. Reconstituted solutions should be stored at 4°C and used within 7 to 14 days. Due to its minimal chain length as a dipeptide, Vilon may be particularly susceptible to degradation in aqueous solution; single-use aliquots are strongly recommended before freezing to avoid repeated freeze-thaw cycles. Shelf life under recommended lyophilized storage conditions is reported at up to 24 months.

What experimental systems have been used in Vilon research?

Published laboratory studies have employed lymphocyte preparations from aged subjects in cell culture systems, with cytological methods including nucleolus organizer region staining, differential scanning calorimetry, and chromosome structural analysis used to assess chromatin activity. Comparative in vitro models have also examined Vilon alongside Epithalon, Livagen, and Cortagen across matched cell preparations. All findings are from preclinical or cell-based experimental systems and do not represent validated clinical data.

REFERENCES

Lezhava, T., Khavison, V., Monaselidze, J., Jokhadze, T., Dvalishvili, N., Bablishvili, N., & Barbakadze, S. (2004). Bioregulator Vilon-induced reactivation of chromatin in cultured lymphocytes from old people. Biogerontology, 5(2), 73–79. https://pubmed.ncbi.nlm.nih.gov/15105581/ 

Lezhava, T., Monaselidze, J., Kadotani, T., Dvalishvili, N., & Buadze, T. (2006). Anti-aging peptide bioregulators induce chromatin reactivation. Georgian Medical News, (133), 111–115. https://pubmed.ncbi.nlm.nih.gov/16705247/ 

Disclaimer

Vilon is exclusively for laboratory research purposes. RCDbio products are not intended to diagnose, prevent, treat, or cure any disease or medical condition. The Food and Drug Administration has not evaluated the statements on this page. Researchers must comply with all applicable local laws and regulations governing the use of research compounds. By purchasing, you agree to RCDbio Terms and Conditions. RCDbio reserves the right to refuse sales to unauthorized individuals.