PX1 Research supplies high-purity, laboratory-grade Vilon (Lys-Glu) engineered specifically for in vitro chromatin remodeling, ribosomal RNA (rRNA) gene transcription, and protein synthesis assays. Available as an analytical research compound, every lot undergoes rigorous third-party verification to guarantee exact sequence identity and exceptional purity.
PX1 Research supplies high-purity, laboratory-grade Vilon (Lys-Glu) engineered specifically for in vitro chromatin remodeling, ribosomal RNA (rRNA) gene transcription, and protein synthesis assays. Available as an analytical research compound, every lot undergoes rigorous third-party verification to guarantee exact sequence identity and exceptional purity.
If your laboratory is looking to buy Vilon ribosome synthesis research compounds, PX1 Research provides analytical-grade L-lysyl-L-glutamic acid (Lys-Glu) manufactured in US-based GMP-compliant facilities. Vilon is a short bioregulatory dipeptide investigated in preclinical research for its capacity to induce chromatin decondensation, activate nucleolar organizer regions (NORs), and stimulate ribosomal RNA gene transcription in cellular models.
Researchers seeking to evaluate the epigenetic effects of short peptides on protein synthesis machinery require reference-grade compounds with fully verified sequence integrity, low endotoxin levels, and zero residual impurities. PX1 Research fulfills these requirements by providing comprehensive third-party Certificates of Analysis (COAs) featuring RP-HPLC purity profiles and ESI-MS mass spectrometry verification for every manufactured lot.
Vilon is a synthetic short bioregulatory dipeptide composed of L-lysine and L-glutamic acid (Lys-Glu). Despite its ultra-low molecular weight (275.3 g/mol), this simple peptide structural motif plays a disproportionately significant role in nuclear target recognition and epigenetic modulation. In preclinical models, the physical structure of Vilon allows it to interact directly with nuclear chromatin structures without requiring complex transport systems.
The molecular design of Vilon relies on the complementary ionic charges of its constituent amino acids. The basic amine group on the lysine side chain and the acidic carboxylic group on the glutamic acid residue allow the dipeptide to engage in selective electrostatic interactions with histone proteins and DNA double-strands. When investigating epigenetic bioregulatory peptides, researchers frequently utilize Vilon as a model compound due to its high stability, minimal steric hindrance, and rapid nuclear permeability during in vitro culture studies.
The primary locus of Vilon activity in cellular research centers upon the nucleolus—the subnuclear organelle responsible for ribosome biogenesis. Ribosomes are the primary cellular machinery required for translating messenger RNA into functional protein chains. In senescent, quiescent, or stressed cell cultures, nucleolar organizer regions (NORs) frequently undergo heterochromatinization, silencing the transcription of 45S pre-ribosomal RNA (pre-rRNA) genes.
Preclinical studies indicate that Vilon interacts directly with condensed heterochromatin structures within the cell nucleus. The dipeptide facilitates the decondensation of pericentromeric heterochromatin, driving an uncoiling event that exposes previously silenced rRNA promoter sequences. This structural opening permits the recruitment of RNA Polymerase I and essential transcription factors (such as UBF and SL1) to the rDNA promoter.
Through this mechanism, Vilon has been observed in vitro to stimulate nucleolar organizer region activation (measured via silver-staining AgNOR methods) and upregulate rRNA transcription. By accelerating pre-rRNA synthesis, the compound provides structural resources necessary for ribosome assembly, supporting baseline cellular protein synthesis capacity in experimental models.
Beyond direct rDNA transcription, Vilon participates in broader epigenetic remodeling. Nuclear magnetic resonance (NMR) spectroscopy and molecular modeling studies suggest that short peptide sequences like Lys-Glu bind to specific grooves in DNA double-strands, particularly in regions rich in AT pairs.
Upon binding, Vilon destabilizes histone-DNA ionic complexes within nucleosomes. This interaction promotes local histone acetylation and alters the structural state of chromatin from densely packed heterochromatin to transcriptionally active euchromatin. In laboratory experiments utilizing human fibroblast and lymphocyte cultures, application of Vilon resulted in a measurable increase in the activation mark histone H3/H4 acetylation, corresponding with reactivated gene expression across multiple metabolic pathways.
A substantial body of international preclinical literature has evaluated Vilon across diverse experimental platforms. Researchers investigating cellular aging mechanisms focus heavily on Vilon's capacity to restore protein synthesis rates in senescent cell strains.
In published rodent models, long-term administration of bioregulatory dipeptides demonstrated alterations in biomarker profiles associated with cellular decline. Specifically, researchers observed enhanced mitotic activity in tissue samples, stabilized chromosomal integrity, and reduced frequency of structural chromosome aberrations. In vitro assays evaluating lymphocytes harvested from elderly animal donors showed that exposure to Vilon restored nucleolar silver-stained region parameters (AgNOR count and area) to levels comparable with young control samples.
Furthermore, transcriptomic profiling of cultured cells exposed to Vilon revealed differential expression of genes involved in cell cycle regulation, DNA repair, and anti-oxidative defense pathways. These findings suggest that Vilon's impact on ribosome synthesis serves as a foundational step in broader cellular homeostasis.
Vilon belongs to a distinct class of short-chain peptide bioregulators developed to target nuclear gene transcription. To select the correct molecule for specific assays, researchers often compare Vilon against other well-studied bioregulatory compounds available in our catalog.
When evaluating chromatin remodeling compounds, researchers frequently compare Vilon to Epitalon, a synthetic tetrapeptide (Ala-Glu-Asp-Gly) known for its investigation in telomerase activity and circadian rhythm gene regulation. While Epitalon primarily targets telomere maintenance and pineal gland gene expression, Vilon demonstrates a more concentrated effect on nucleolar rRNA transcription and rapid ribosomal biogenesis.
Similarly, Vilon is often analyzed alongside Livagen, another short peptide (Lys-Glu-Asp-Ala) implicated in chromatin decondensation, as well as Thymogen (Glu-Trp), which focuses predominantly on immune cell signaling cascades. Among these, Vilon (Lys-Glu) represents the minimal active dipeptide sequence capable of directly inducing nucleolar organizer region reactivation.
Researchers conducting comprehensive comparative studies across peptide classes can review our full spectrum of offerings in the all peptides directory or browse our curated collection of epigenetic research compounds.
When procurement officers and principal investigators search to buy Vilon ribosome synthesis compounds for sensitive molecular biology assays, product purity and verification standards are paramount. Trace contaminants, synthesis side-products, or endotoxin contamination can confound experimental data, alter gene expression profiles, or cause cytotoxicity in cell culture assays.
PX1 Research enforces strict quality assurance protocols for all research compounds:
1. Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC): Ensures chemical purity exceeds 98.0%. RP-HPLC analysis confirms the absence of truncated peptide fragments or organic impurities.
2. Electrospray Ionization Mass Spectrometry (ESI-MS): Verifies exact molecular weight (275.3 g/mol) and confirms correct amino acid sequencing without isomer displacement.
3. Quantitative Endotoxin Testing: Uses Chromogenic Limulus Amebocyte Lysate (LAL) assays to verify that endotoxin levels remain strictly under <0.05 EU/mg, making the material suitable for sensitive in vitro tissue cultures.
4. Batch-Specific Lot Traceability: Every vial is assigned a unique lot number linked directly to an independent third-party Certificate of Analysis available for download by verified research institutions.
Vilon is supplied as a lyophilized (freeze-dried) white powder engineered for long-term chemical stability. To ensure precise concentration control during in vitro experiments, laboratories must follow standard sterile reconstitution procedures.
Reconstitution Procedures:
- Reconstitution Solvent: Use sterile laboratory-grade Water for Injection (WFI), sterile phosphate-buffered saline (PBS, pH 7.4), or low-endotoxin bacteriostatic water depending on experimental downstream applications.
- Solubilization Technique: Allow the vial to equilibrate to room temperature before reconstitution. Inject the desired volume of solvent along the inner glass wall of the vial. Gently swirl or invert the vial until complete dissolution occurs. Avoid aggressive vortexing or high-shear agitation, which may degrade peptide bonds.
- Concentration Target: Common working stock concentrations for in vitro assays range from 1 mg/mL to 10 mg/mL.
Storage & Stability:
- Lyophilized Powder: Store at -20°C for up to 24 months, or -80°C for extended storage. Keep protected from light and moisture.
- Reconstituted Solution: Store reconstituted aliquots at -20°C or -80°C to prevent freeze-thaw degradation. Avoid repeated freeze-thaw cycles. Aliquots stored at 4°C should be utilized within 48 to 72 hours under sterile conditions.
In experimental settings evaluating ribosome synthesis, researchers utilize Vilon across several primary assay architectures:
1. AgNOR Staining Assays: Quantitative silver-staining of nucleolar organizer regions to measure changes in nucleolar area and NOR protein count in cell cultures exposed to varying concentrations of Vilon (typically 1 ng/mL to 100 ng/mL).
2. Quantitative Real-Time PCR (qPCR): Assessment of 45S pre-rRNA transcript levels to quantify changes in RNA Polymerase I transcription rates over specific time courses (e.g., 6, 12, 24, and 48 hours post-treatment).
3. Microarray and RNA-Seq Profiling: Genome-wide transcriptomic analyses to map differential gene expression downstream of chromatin decondensation.
4. Protein Synthesis Rates: Incorporating labeled amino acids (e.g., [3H]-leucine or puromycin-based SUNTOP assays) to measure overall cellular protein translation rates following incubation with Vilon.
Acquiring reliable research peptides requires a trusted domestic supply partner. PX1 Research operates centralized synthesis and distribution facilities located in California and Arizona, providing rapid dispatch and short transit times across North America.
All orders placed Monday through Friday before our daily shipping cutoff ship the same day. Institutional buyers requiring larger quantities for multi-phase study designs can access streamlined order processing and custom batch sizes through our dedicated wholesale laboratory portal. PX1 Research maintains absolute commitment to scientific integrity, providing pure, verifiable, and fully documented compounds for cutting-edge laboratory research.
What is Vilon and what is its chemical structure?
Vilon is a synthetic short bioregulatory dipeptide consisting of L-lysine and L-glutamic acid (Lys-Glu). It has a molecular weight of 275.3 g/mol and is studied in preclinical research for its interactions with nuclear chromatin and ribosomal RNA gene promoters.
How does Vilon influence ribosome synthesis in laboratory models?
Preclinical in vitro studies suggest Vilon induces chromatin decondensation and activates nucleolar organizer regions (NORs). This uncoiling event exposes ribosomal RNA (rRNA) gene promoters, allowing RNA Polymerase I to bind and accelerate 45S pre-rRNA transcription.
How is Vilon quality and purity verified at PX1 Research?
PX1 Research verifies every lot of Vilon using independent third-party laboratories. Quality testing includes Reverse-Phase HPLC to confirm >98% purity, ESI-Mass Spectrometry to confirm identity, and Chromogenic LAL testing to ensure endotoxin levels remain below <0.05 EU/mg.
What reconstituting liquids should be used for Vilon in vitro research?
Vilon can be reconstituted using sterile laboratory-grade water, phosphate-buffered saline (PBS, pH 7.4), or sterile bacteriostatic water, depending on the requirements of your specific cell culture or analytical assay.
How should reconstituted Vilon solutions be stored in the lab?
Reconstituted Vilon solutions should be aliquoted into single-use microcentrifuge tubes to prevent repeated freeze-thaw cycles and stored at -20°C or -80°C. Short-term storage at 4°C is acceptable for up to 72 hours under sterile conditions.
How does Vilon compare to Epitalon or Livagen in epigenetic studies?
While Epitalon (tetra-peptide) focuses primarily on telomerase regulation and Livagen (tetra-peptide) targets chromatin decondensation across broader metabolic pathways, Vilon (dipeptide Lys-Glu) represents the minimal sequence specifically evaluated for rapid nucleolar reactivation and direct rRNA transcription activation.
Is Vilon intended for human consumption or therapeutic use?
No. Vilon supplied by PX1 Research is strictly designated for laboratory research use only (RUO). It is not for human or animal consumption, therapeutic administration, or diagnostic procedures.
Where does PX1 Research ship Vilon orders from?
All PX1 Research compounds are manufactured in US facilities and dispatched from our primary distribution hubs in California and Arizona, with same-day shipping available 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.