Principal investigators seeking to buy Vilon receptor binding reagents for controlled laboratory studies can acquire analytical-grade material through PX1 Research. Vilon (L-lysyl-L-glutamic acid) is supplied strictly as a research compound for in vitro assays and preclinical evaluation. Every lot is manufactured in US-based facilities and accompanied by independent third-party certificate of analysis (COA) documentation verifying chemical identity, RP-HPLC purity, and endotoxin thresholds.
Principal investigators seeking to buy Vilon receptor binding reagents for controlled laboratory studies can acquire analytical-grade material through PX1 Research. Vilon (L-lysyl-L-glutamic acid) is supplied strictly as a research compound for in vitro assays and preclinical evaluation. Every lot is manufactured in US-based facilities and accompanied by independent third-party certificate of analysis (COA) documentation verifying chemical identity, RP-HPLC purity, and endotoxin thresholds.
Vilon is a synthetic short-chain peptide bioregulator consisting of two amino acid residues: L-lysine and L-glutamic acid (H-Lys-Glu-OH). With a molecular formula of C11H21N3O5 and a nominal molecular weight of approximately 275.31 g/mol, Vilon represents one of the smallest bioactive peptide sequences derived from functional thymic extract investigations. Researchers interested in purchasing high-purity material can browse our catalog of all peptides or navigate directly to order Vilon peptide for experimental use.
Unlike complex, long-chain polypeptide hormones that rely on folded tertiary conformations to achieve receptor occupancy, Vilon operates through direct molecular interactions driven by its distinct ionic charge distribution. The basic N-terminal lysine residue and the acidic C-terminal glutamic acid residue confer a zwitterionic character at physiological pH, allowing the dipeptide to participate in specialized hydrogen bonding, electrostatic surface interactions, and targeted chromatin binding. In preclinical research setups, Vilon is analyzed as a model molecule for peptide-driven epigenetic modulation and nuclear transport assays.
A central focus of contemporary peptide biochemistry is determining whether short peptides interact primarily with classical G-protein coupled receptors (GPCRs) on the cell membrane or penetrate intracellular compartments to bind directly with nuclear structures. Preclinical research indicates that Vilon receptor binding characteristics involve a dual-phase mechanism: transient interactions with cell-surface transport proteins followed by rapid intracellular uptake and nuclear translocation.
In vitro cellular models demonstrate that labeled Vilon sequences cross cytoplasmic boundaries through passive diffusion and peptide transporter-mediated pathways. Once inside the nucleus, Vilon does not bind exclusively to traditional transmembrane receptors; rather, it exhibits selective binding affinities for histone proteins and specific nucleotide sequences within the major and minor grooves of double-stranded DNA. Biophysical assays utilizing surface plasmon resonance (SPR) and fluorescence polarization show that the dipeptide binds selectively to promoter regions of genes associated with cell cycle regulation, protein synthesis, and immunomodulatory pathways.
Beyond classical membrane-bound receptor pathways, Vilon functions as a direct chromatin-modulating agent. Molecular dynamics simulations and nuclear magnetic resonance (NMR) spectroscopy suggest that Lys-Glu intercalates into histone-DNA complexes, altering the electrostatic charge density surrounding condensed heterochromatin. This interaction destabilizes condensed heterochromatin structures, promoting local chromatin decondensation and unmasking transcriptionally silenced gene regions.
Investigating these nuclear mechanisms provides critical insight into the broader class of short bioregulatory molecules. Researchers exploring these gene-regulatory cascades often consult our overview on Khavinson peptides bioregulators to compare how di-, tri-, and tetrapeptides influence histone acetylation and DNA methylation patterns in cell culture systems. Preclinical data confirm that Vilon-induced chromatin remodeling enhances the accessibility of RNA polymerase II to specific promoter sequences, thereby upregulating target mRNA transcription without altering the underlying genomic sequence.
In vitro and animal models have evaluated Vilon across various experimental paradigms focused on cellular senescence, immunomodulation, and thymic tissue maintenance. In cultured human lymphocyte assays, exposure to low nanomolar concentrations of Vilon was observed to stimulate ribosomal RNA synthesis and activate total protein translation markers in senescent cell populations.
Rodent models exploring thymic involution demonstrate that administration of Lys-Glu supports the structural preservation of thymic epithelial cells and regulates the expression of key cytokines, including interleukin-2 (IL-2) and interferon-gamma (IFN-γ). For detailed scientific literature on these immunological pathways, explore our analytical repository on thymic peptide mechanisms. Furthermore, in vitro models examining vascular endothelial cells indicate that Vilon exposure correlates with altered expression of heat shock proteins (HSP70) and antioxidant enzymes, protecting cells against chemically induced oxidative stress.
To contextualize Vilon within the broader landscape of synthetic peptide bioregulators, laboratory researchers frequently compare its structure, binding targets, and biological profiles against other short-chain research peptides. Below is a comparative overview of three widely studied compounds in this class:
While Epitalon (Ala-Glu-Asp-Gly) is predominantly investigated for its influence on telomerase activity and pineal gland gene expression, Vilon (Lys-Glu) focuses more narrowly on thymic chromatin unwinding and immune-related gene transcription. Similarly, Thymogen (Glu-Trp) shares an immunological research focus with Vilon, yet exhibits distinct hydrophobic binding interactions due to its tryptophan residue compared to the basic, polar lysine residue found in Vilon. Researchers conducting side-by-side screening assays can review our PX1 Research library for comparative experimental protocols.
When purchasing compounds for sensitive receptor binding assays, chromatin immunoprecipitation (ChIP), or cell culture experiments, analytical purity is paramount. Uncharacterized impurities, trifluoroacetate (TFA) salts, or residual bacterial endotoxins can invalidate assay data, alter binding kinetics, or cause non-specific cytotoxicity in vitro.
PX1 Research enforces rigid quality control standards for every production lot. Every batch undergoes comprehensive testing, including high-performance liquid chromatography (HPLC) to confirm peptide purity exceeds 98.0%, mass spectrometry (MS) to verify precise molecular weight (275.3 g/mol), and chromogenic Limulus Amebocyte Lysate (LAL) testing to ensure endotoxin levels remain strictly under 0.01 EU/mg. For a complete technical breakdown of analytical methodologies, review our guide on peptide purity testing HPLC MS.
Vilon is supplied as a lyophilized (freeze-dried) powder in sealed glass vials to ensure long-term chemical stability. To preserve structural integrity and prevent degradation prior to experimental use, laboratory personnel should observe standardized handling protocols:
1. Storage of Lyophilized Powder: Store sealed vials at -20°C in a dry environment protected from light. Lyophilized Vilon remains stable under these conditions for up to 24 months. 2. Reconstitution Solvent: Reconstitute using sterile, endotoxin-free water or phosphate-buffered saline (PBS, pH 7.4). Gentle manual swirling is recommended; avoid vigorous mechanical vortexing to prevent peptide shearing. 3. Aliquoting and Storage: Reconstituted solutions should be divided into single-use experimental aliquots and stored at -80°C to eliminate repeated freeze-thaw cycles. 4. Concentration Verification: Calculate final assay concentrations using liquid chromatography or ultraviolet-visible (UV-Vis) spectrophotometry prior to dosing cell cultures.
Procuring research-grade peptides requires a reliable supplier that guarantees chemical fidelity, batch-to-batch consistency, and transparent analytical documentation. PX1 Research manufactures all compounds within GMP-compliant, US-based facilities, ensuring strict oversight throughout the synthesis, purification, and packaging stages.
Principal investigators and laboratory procurement managers seeking volume quantities for long-term studies can establish institutional access through our wholesale lab account portal. Every order shipped from our California and Arizona distribution centers includes a lot-specific Certificate of Analysis detailing HPLC chromatograms, mass spectra, and endotoxin assay results, ensuring complete traceability for academic and industrial research applications.
What is the primary target of Vilon in receptor binding studies?
Preclinical studies indicate Vilon (Lys-Glu) targets nuclear chromatin and histone proteins rather than acting exclusively through classical transmembrane GPCR receptors, leading to local DNA decondensation and altered gene expression.
How is Vilon's identity and purity verified at PX1 Research?
PX1 Research verifies every lot using Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC) for purity (≥98%) and Electrospray Ionization Mass Spectrometry (ESI-MS) for molecular weight verification, backed by an independent ISO 17025 accredited COA.
What are the endotoxin limits for PX1 Research Vilon?
All Vilon lots supplied by PX1 Research are tested via chromogenic LAL assays to ensure endotoxin levels remain below 0.01 EU/mg, preventing endotoxin-induced cytotoxicity in cell culture experiments.
How does Vilon differ structurally from Epitalon and Thymogen?
Vilon is a dipeptide (Lys-Glu), Thymogen is a dipeptide with a different sequence (Glu-Trp), and Epitalon is a tetrapeptide (Ala-Glu-Asp-Gly). Each possesses distinct molecular weights, charge profiles, and specific nuclear binding targets.
What solvents are recommended for reconstituting Vilon in laboratory settings?
Vilon readily dissolves in sterile endotoxin-free water, normal saline, or standard laboratory buffers such as Phosphate-Buffered Saline (PBS, pH 7.4) for in vitro cell culture work.
How should reconstituted Vilon solutions be stored?
Once reconstituted, Vilon solutions should be partitioned into single-use laboratory aliquots and stored at -80°C to avoid degradation from repeated freeze-thaw cycles.
Is Vilon approved for human clinical use or therapeutic treatment?
No. Vilon is provided strictly as a research compound for in vitro laboratory assays, preclinical binding studies, and molecular evaluation. It is not for human or veterinary use.
Where are PX1 Research compounds manufactured and shipped from?
PX1 Research compounds are manufactured in US-based GMP-compliant facilities and shipped directly from our fulfillment hubs in California and Arizona.
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.