Vilon is a synthetic dipeptide (Lys-Glu) investigated in preclinical models for its role in chromatin structure modulation and gene expression regulation. PX1 Research supplies high-purity, laboratory-grade Vilon featuring lot-specific third-party COAs, HPLC purity verification, and mass spectrometry analysis for qualified institutional research.
Vilon is a synthetic dipeptide (Lys-Glu) investigated in preclinical models for its role in chromatin structure modulation and gene expression regulation. PX1 Research supplies high-purity, laboratory-grade Vilon featuring lot-specific third-party COAs, HPLC purity verification, and mass spectrometry analysis for qualified institutional research.
When laboratories seek to buy Vilon biological activity for sale, they require analytical-grade Lys-Glu dipeptide formulated specifically for in vitro assays and controlled animal models. Vilon (L-lysyl-L-glutamic acid) is a short regulatory peptide derived from thymic peptide research, recognized for its capacity to interact directly with nuclear chromatin and modulate specific transcriptional pathways without cell cytotoxicity.
To ensure reproducible assay results, researchers must source Vilon with confirmed purity exceeding 98%, verified sequence identity via electrospray ionization mass spectrometry (ESI-MS), and strict endotoxin control below 0.5 EU/mg. PX1 Research provides USA-manufactured Vilon with complete analytical transparency to support rigorous gene expression, cellular senescence, and immunomodulatory studies.
Vilon is one of the smallest bioactive peptide sequences synthesized, consisting of a simple dipeptide backbone: L-lysine bonded to L-glutamic acid ($C_{11}H_{21}N_{3}O_{5}$, exact molecular weight approximately 275.31 g/mol). Despite its minimal molecular footprint, the hydrophilic properties and specific charge distribution of the lysine amine group and glutamic acid carboxyl side chains allow Vilon to form stable electrostatic interactions with nucleic acid structures.
In physical form, high-purity Vilon presents as a lyophilized white powder that exhibits exceptional solubility in aqueous buffer systems, including phosphate-buffered saline (PBS) and sterile water for injection. Research protocols examining the basic chemical profile of Vilon dipeptide frequently utilize high-performance liquid chromatography (RP-HPLC) to assess chemical purity and verify the absence of truncated peptide impurities or residual processing reagents.
The primary focus of biological activity studies involving Vilon centers on its direct interaction with nuclear material. Preclinical chromatin decondensation assays demonstrate that Vilon binds directly to specific sequences within major and minor DNA grooves as well as histone proteins. This interaction induces structural alterations in heterochromatin, converting dense, transcriptionally inactive chromatin regions into accessible euchromatin.
Through this structural remodeling, Vilon has been observed in vitro to reactivate silenced genes within aging or senescent cell lineages. In human lymphocyte cell cultures and fibroblast models, exposure to Vilon promotes the expression of ribosomal RNA (rRNA) genes and activates marker genes associated with cell repair. Researchers utilizing our peptides research portal frequently investigate these epigenetic mechanisms to determine how short peptide bioregulators influence gene expression profiles without altering the primary DNA sequence.
Extensive rodent and cell culture studies document the immunomodulatory potential of Vilon. Derived conceptually from crude thymic extracts, Vilon exhibits specific activity on T-lymphocyte subpopulations. Preclinical models indicate that application of Vilon stimulates the differentiation of immature thymocytes into functional CD4+ helper and CD8+ cytotoxic T-cell populations, restoring baseline immune parameters in immunodeficient or senescent test animals.
Furthermore, in vitro inflammatory assays show that Vilon modulates cytokine profiles, reducing the overproduction of pro-inflammatory signals such as interleukin-6 (IL-6) and tumor necrosis factor-alpha (TNF-alpha) while maintaining normal interferon production. These findings position Vilon as a key candidate for investigating homeostatic immune signaling, inflammatory resolution, and age-related immunosenescence across diverse non-human biological systems.
Within the category of short peptide bioregulators, Vilon is frequently evaluated alongside related synthetic regulatory peptides such as Epitalon and Thymogen. While all three compounds share a short amino acid sequence designed to influence gene expression and cellular longevity, their target pathways and operational mechanisms differ significantly.
While Vilon (Lys-Glu) focuses heavily on chromatin structural remodeling and general T-cell differentiation, Epitalon (Ala-Glu-Asp-Gly) is predominantly investigated for its capacity to induce telomerase activity and extend telomere length in somatic cells. Thymogen (Glu-Trp), another thymic-derived dipeptide, exhibits a narrower target profile centered primarily on acute immune response activation and macrophage function. Investigating these compounds side-by-side in comparative assays allows researchers to delineate the specific gene-regulatory pathways governed by dipeptide versus tetrapeptide signaling molecules. Explore our full catalog of all research peptides for complementary bioregulatory compounds.
Achieving consistent results when evaluating Vilon biological activity requires strict adherence to analytical reconstitution standards. Vilon is supplied as a lyophilized solid sealed under inert argon gas. Prior to reconstitution, vials should be brought to room temperature inside a laminar flow hood to prevent atmospheric moisture condensation on the cake.
Reconstitution should be performed using sterile, laboratory-grade solvents such as 0.9% sterile bacteriostatic sodium chloride solution or phosphate-buffered saline (PBS, pH 7.4). Solvents should be injected gently against the glass vial wall, followed by soft swirling. Avoid vigorous vortexing or rapid agitation, as mechanical shear stress can disrupt peptide integrity. Stock solutions intended for immediate assaying can be maintained at 2°C to 8°C for short durations, whereas long-term working aliquots must be frozen to prevent hydrolytic degradation.
Lyophilized Vilon maintains chemical stability for up to 24 months when stored at -20°C in a desiccated environment protected from direct light exposure. For long-term archival storage, maintaining temperatures at -80°C is recommended to eliminate hydrolytic micro-reactions.
Once reconstituted into aqueous solution, Vilon exhibits moderate stability; however, repeated freeze-thaw cycles must be strictly avoided. Laboratories should sub-aliquot reconstituted Vilon into single-use micro-centrifuge tubes using low-binding polypropylene plasticware. Working aliquots stored at -20°C should be used within 30 to 60 days to guarantee full bioactivity in delicate gene expression assays. Detailed storage parameters are provided in our wholesale research portal for bulk procurement management.
Research reproducibility hinges entirely on compound purity and batch consistency. When laboratories evaluate vendors to buy Vilon biological activity for sale, verification of analytical documentation is paramount. Low-purity peptide batches containing truncated sequences or unreacted coupling reagents can alter cell viability and yield false-positive or irreproducible data in gene expression assays.
PX1 Research enforces strict quality control standards for every production lot. Every batch undergoes rigorous testing including reverse-phase HPLC (RP-HPLC) to confirm peptide purity ≥98%, electrospray mass spectrometry (ESI-MS) to confirm exact molecular mass (275.31 Da), and Chromogenic Reagent Endotoxin Testing to ensure levels remain below 0.5 EU/mg. Every order includes a lot-specific Certificate of Analysis (COA) issued by an independent ISO 17025 accredited analytical facility.
PX1 Research is a dedicated USA-based supplier committed to advancing scientific discovery by providing verified, research-grade compounds. We recognize that academic institutions, biotechnology firms, and independent laboratories require total supply chain transparency, reliable lot-to-lot consistency, and rapid delivery.
All PX1 Research products are manufactured in state-of-the-art GMP-compliant facilities located in the United States. Orders are dispatched directly from our domestic distribution centers in California and Arizona, offering same-day shipping for weekday orders. By eliminating international transit delays and custom hold times, PX1 Research ensures your laboratory receives pristine, temperature-stable compounds ready for immediate experimental deployment.
What primary biological activity is Vilon researched for?
Vilon (Lys-Glu) is primarily researched for its ability to bind nuclear chromatin, induce heterochromatin decondensation, activate silenced genes in senescent cells, and modulate T-lymphocyte differentiation and cytokine expression in preclinical models.
What is the molecular weight and sequence of Vilon?
Vilon is a synthetic dipeptide composed of L-lysine and L-glutamic acid (Lys-Glu / H-Lys-Glu-OH). Its molecular formula is C11H21N3O5 with a molecular mass of approximately 275.31 g/mol.
How is Vilon quality verified at PX1 Research?
Every lot of Vilon undergoes independent third-party testing in ISO 17025 accredited laboratories. Purity is verified via RP-HPLC (≥98%), identity is confirmed using ESI-MS mass spectrometry, and safety for cell models is validated via endotoxin testing (<0.5 EU/mg).
What solvent is recommended for reconstituting Vilon in lab assays?
Vilon is highly water-soluble. For in vitro and cell culture applications, it is typically reconstituted in sterile phosphate-buffered saline (PBS, pH 7.4) or sterile 0.9% sodium chloride under aseptic laboratory conditions.
How should reconstituted Vilon stock solutions be stored?
Reconstituted Vilon solutions should be divided into single-use sub-aliquots in low-binding plastic tubes and stored at -20°C or -80°C. Repeated freeze-thaw cycles should be strictly avoided to prevent peptide degradation.
Is Vilon suitable for human administration or clinical use?
No. Vilon supplied by PX1 Research is strictly designated for laboratory research use only. It is not intended for human consumption, therapeutic use, veterinary care, or clinical administration.
How does Vilon differ from other short bioregulatory peptides like Epitalon?
While both are gene-regulatory peptides, Vilon is a dipeptide (Lys-Glu) focusing mainly on chromatin structural accessibility and immunomodulation, whereas Epitalon is a tetrapeptide (Ala-Glu-Asp-Gly) known primarily for telomerase activation research.
Where does PX1 Research ship Vilon from?
PX1 Research dispatches all orders directly from fully stocked distribution facilities in California and Arizona, offering same-day shipping for orders placed Monday through Friday.
All products are sold strictly for laboratory and research use only. Not for human or veterinary use, diagnosis, treatment or consumption. Statements have not been evaluated by the FDA.