Vilon

Vilon (dipeptide Lys-Glu, H-Lys-Glu-OH, KE; CAS 45234-02-4; C11H21N3O5, 275.30 Da) is an ultra-short bioregulator peptide from Khavinson classified as a thymic immunomodulator for research (RUO).

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Vilon

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Research Peptides Only

What is Vilon 20MG

Vilon 20MG is a synthetic dipeptide bioregulator studied in research for its profound immunomodulatory effects and ability to regulate chromatin structure in aging cells. It is intended exclusively for research use.

Regarding its chemical identity, Vilon has a molecular formula of C11H21N5O4 and a molecular weight of 287.3 g/mol. Its reported canonical sequence is Lys-Glu. A confirmed CAS number is not available in open primary reference sources and is therefore omitted.

Its synonyms include Vilon.

Product for research use.

Mechanism of action of Vilon

Vilon is an extremely short peptide (just two amino acids) that penetrates deep into the cellular nucleus. It binds to histones to cause chromatin decondensation, un-silencing genes related to immune function and cellular repair, particularly in T-lymphocytes.

Pharmacokinetics and pharmacodynamics of Vilon

As a dipeptide, it is practically immune to further rapid cleavage until it reaches its target. Its half-life is minimal, but its ability to physically alter the structure of DNA packaging results in a cascade of epigenetic changes that persist long-term.

Scientific evidence on Vilon

The available evidence on Vilon is preliminary and largely inconclusive, and should be interpreted with caution. The literature describes it as having been investigated for multiple indications in preclinical models.

Investigated heavily in models of immunosenescence, severe stress, and cellular aging. Preclinical evidence shows it is highly effective at restoring the proliferative capacity of aged immune cells and down-regulating chronic, low-grade inflammation.

Vilon applications in research

Ideal for (research context):
– In vitro and preclinical studies of its specific receptor pathways.
– Investigation of tissue repair, cell proliferation, and functional restoration in laboratory models.
– Comparative work with related peptides.

Not applicable for:
– clinical, diagnostic or therapeutic use.
– Any administration to humans or animals outside of an authorized research protocol.

Product for research use.

Vilon protocols in preclinical studies

The literature consulted does not include numerical doses from studies that can be cited for Vilon, so no trial schemes or quantities are specified.

The presentations of this product (20MG) refer only to the amount of lyophilized peptide per vial (or volume for liquids) and do not constitute a dosage recommendation. The design of any protocol, including concentrations and working volumes, is the responsibility of the researcher, based on their experimental objectives and the relevant primary literature.

Information provided exclusively for research purposes.

Reconstitution and manipulation of Vilon

As a general guideline for laboratory handling, lyophilized peptides such as Vilon are usually reconstituted with bacteriostatic water (sterile water with approximately 0.9% benzyl alcohol).

Add the solvent slowly down the side of the vial, letting it run over the lyophilized powder; avoid injecting the stream directly onto the powder.
Do not shake: gently rotate the vial until completely dissolved.
Adjust the solvent volume according to the desired working concentration, considering the 20MG contents of the vial.

These guidelines are for general technique and do not replace the internal procedures of each laboratory.

Vilon Stability and Storage

As a standard laboratory handling procedure for peptides:

Freeze-dried (unreconstituted): This is the most stable form. It is best preserved by freezing and protecting it from moisture and light for long-term storage.
Reconstituted: once in solution, the peptide is less stable and must be kept refrigerated, being used within a short period; for extended storage, freezing in aliquots is usually preferred.
Avoid repeated freeze-thaw cycles, as they can degrade the peptide.

Given that the molecule is characterized by rapid enzymatic degradation in biological media, careful cold chain management is especially relevant.

Documented Vilon security profile

The documented safety information in open sources for Vilon is limited and should be interpreted with caution, also considering that it is research material and not for clinical use.

Given its action as a fundamental epigenetic modifier, its theoretical safety in animal models is considered high, acting as a normalizer of cellular age. However, widespread chromatin alteration in vivo requires careful study regarding unforeseen genetic expressions.

Formal contraindications and adverse event rates are not available in the consulted literature, so no figures are reported.

Vilon in a comparative context

Vilon is one of the shortest active peptides known (a dipeptide). Compared to Crystagen (a tripeptide) and Thymalin (an extract), Vilon operates at the most fundamental level of DNA un-packaging, making it incredibly potent for reversing cellular senescence in immune models.

History and development of Vilon

Developed by the Khavinson group as one of the first and simplest “epigenetic switches.” It proved the theory that incredibly short amino acid sequences could act directly on DNA packaging to reverse the aging process in specific cell lines.