Vilon is a synthetic bioregulatory dipeptide extensively evaluated in cell culture models for its role in chromatin remodeling, gene reactivation, and cellular proliferation. Principal investigators and laboratory managers can source high-purity, analytically verified [Vilon 10mg](/product/vilon-10mg) directly from PX1 Research for rigorous in vitro and ex vivo experimental applications.
Vilon is a synthetic bioregulatory dipeptide extensively evaluated in cell culture models for its role in chromatin remodeling, gene reactivation, and cellular proliferation. Principal investigators and laboratory managers can source high-purity, analytically verified [Vilon 10mg](/product/vilon-10mg) directly from PX1 Research for rigorous in vitro and ex vivo experimental applications.
Researchers seeking to buy Vilon cell proliferation peptides for sale must prioritize analytical purity, sequence integrity, and verified endotoxin limits prior to experimental deployment. Vilon (Lysyl-Glutamic acid, Lys-Glu) is a synthetic short bioregulatory peptide investigated in preclinical models for its ability to decondense heterochromatin, stimulate protein synthesis, and accelerate cellular proliferation across aging fibroblast and immunocompetent cell lines.
When purchasing reference material, selecting fully validated compounds with lot-specific documentation is essential to ensure reproducible assay conditions. PX1 Research supplies high-purity research peptides manufactured under strict quality standards to support advanced cell culture, epigenetic, and tissue regeneration research.
Vilon is an ultra-short bioregulatory dipeptide composed of L-lysine and L-glutamic acid joined by a peptide bond (H-Lys-Glu-OH). With a molecular formula of C11H21N3O5 and a molecular weight of approximately 275.3 g/mol, Vilon belongs to the class of short peptide regulators originally developed during foundational studies on thymic peptide extracts.
Due to its minimal molecular size, Vilon exhibits unique biochemical properties compared to larger polypeptide structures. The basic side chain of lysine combined with the acidic side chain of glutamic acid enables specific electrostatic interactions with double-stranded DNA and nuclear histone complexes. In cell-free and in vitro assay systems, this hydrophilic dipeptide demonstrates high stability in aqueous buffering systems, making it an ideal candidate for precise dose-response profiling in cellular models.
The primary biochemical mechanism attributed to Vilon in literature centers on its interaction with the cell nucleus and epigenetic regulatory structures. In vitro studies demonstrate that Lys-Glu selectively binds to major and minor grooves of DNA, as well as histone proteins, promoting heterochromatin decondensation. By relaxing tightly wound chromatin architecture, Vilon facilitates RNA polymerase access to previously silenced or suppressed promoter regions.
Preclinical investigations utilizing fluorescence microscopy and micrococcal nuclease digestion assays reveal that exposure to Vilon leads to structural reorganization of nuclear chromatin in senescent cells. This structural relaxation correlates with increased transcriptional activity, restored synthesis of ribosomal RNA (rRNA), and upregulated expression of markers associated with metabolic activation and cellular proliferation. Detailed analyses of these genomic pathways are archived in the PX1 peptide research library.
Multiple in vitro models have evaluated the impact of Vilon on cell proliferation kinetics, particularly in primary fibroblast cultures, epithelial models, and immune cell populations. In rodent and human cell line studies, incubation with microgram concentrations of Vilon produced a statistically significant increase in the proportion of cells entering the S and G2/M phases of the cell cycle.
Researchers investigating epigenetic bioregulatory peptides have observed that Vilon enhances the proliferative capacity of embryonic and adult dermal fibroblasts without inducing atypical karyotypic alterations or uncontrolled transformation. In senescent cell populations exhibiting replicative arrest, application of Lys-Glu was shown to reactivate DNA synthesis, upregulate Ki-67 nuclear marker expression, and improve total cell yield over multi-passage culture protocols.
To contextualize Vilon within the broader landscape of bioregulatory and cytoprotective research compounds, laboratory evaluators frequently compare its structural and functional metrics against related synthetic short peptides. The table below outlines key comparative parameters across prominent short-chain research peptides:
As detailed above, while tetrapeptides like Epithalon exert primary effects via telomerase activation and pineal gene regulation, Vilon operates as an immediate dipeptide chromatin modifier focused heavily on immune cell and fibroblast proliferation. In contrast, organ-derived complexes like Thymalin contain multi-peptide fractions, whereas Vilon offers a highly defined, single-entity dipeptide sequence. For cellular repair and tissue organization assays, researchers often contrast Vilon's nuclear mechanisms with the membrane and extracellular signaling pathways of BPC-157 or TB-500.
Beyond structural fibroblast proliferation, Vilon is widely studied in immunobiology for its capacity to restore functional responses in compromised splenocyte and lymphocyte cultures. In vitro assays using thymocytes and peripheral blood mononuclear cells (PBMCs) demonstrate that Lys-Glu treatment upregulates key interleukin receptors and enhances endogenous cytokine expression, including IL-2 and interferon-gamma.
These immunomodulatory properties make Vilon a critical reference standard for investigating age-related immune dysfunction (immunosenescence). In cell culture models exposed to oxidative stress or ionising radiation, pre-incubation with Vilon reduced apoptotic cell markers, preserved mitochondrial membrane potential, and maintained cell proliferation rates, underscoring its dual role as a proliferative driver and cytoprotective agent.
Proper laboratory handling is imperative to preserve the structural stability and bioactivity of lyophilized Vilon. Upon receipt, the peptide powder should be stored unopened in a desiccated environment at -20°C for short-term projects or -80°C for long-term storage.
For reconstitution in experimental workflows, utilize sterile, endotoxin-free water or phosphate-buffered saline (PBS, pH 7.4). Vilon exhibits excellent aqueous solubility due to its charged amino acid side chains. Gently swirl or vortex the vial until complete dissolution is achieved; avoid violent agitation to prevent shearing. Reconstituted stock solutions should be aliquoted into single-use polypropylene tubes to minimize freeze-thaw cycles and stored at -20°C. For institutional procurement requirements, lab administrators can explore bulk terms through the PX1 Wholesale program.
When designing cell proliferation assays utilizing Vilon, researchers typically employ multi-parametric detection systems to quantify metabolic activity, DNA synthesis, and cell cycle distribution. Standard experimental frameworks include:
1. **Colorimetric Metabolic Assays**: Utilizing CCK-8 or MTT reagents to measure mitochondrial dehydrogenase activity following 24 to 72 hours of Vilon exposure.
2. **Thymidine Analog Incorporation**: Incorporating BrdU or EdU into newly synthesized DNA to measure direct cell division rates via fluorescence microscopy or flow cytometry.
3. **Flow Cytometry Cell Cycle Analysis**: Propidium iodide (PI) staining to map G0/G1, S, and G2/M phase transitions across control vs. treated cell populations.
4. **Transcriptomic Profiling**: Quantitative Real-Time PCR (qPCR) targeting cyclin-dependent kinases (CDKs), proliferating cell nuclear antigen (PCNA), and chromatin remodeling complexes.
To ensure valid, publication-grade experimental results, principal investigators must rigorously vet peptide suppliers. Research-grade Vilon must be accompanied by comprehensive batch verification rather than generic theoretical certificates. Essential quality metrics include:
- **Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC)**: Confirms chemical purity by verifying that the primary dipeptide peak constitutes ≥98% of total integrated peak area.
- **Electrospray Ionization Mass Spectrometry (ESI-MS)**: Verifies molecular weight and monoisotopic mass to rule out truncated sequences, residual protecting groups, or synthesis artifacts.
- **Limulus Amebocyte Lysate (LAL) Endotoxin Testing**: Ensures endotoxin levels remain below strictly controlled limits (<0.01 EU/mg) to prevent false-positive inflammatory responses in cell cultures.
- **USA Manufacturing & ISO 17025 Testing**: Guarantees production compliance within state-of-the-art facilities and third-party laboratory verification.
PX1 Research is dedicated to supplying the scientific community with ultra-pure, reliably batch-tested peptides for non-clinical research applications. Every lot of Vilon 10mg undergoes rigorous analytical validation in ISO 17025 accredited testing facilities within the United States.
We provide transparent, lot-specific Certificates of Analysis (COAs) featuring full HPLC chromatograms and Mass Spectrometry reports with every shipment. Operating from distribution hubs in California and Arizona, PX1 Research offers same-day shipping on orders placed Monday through Friday before 3:00 PM PST, ensuring your laboratory maintains uninterrupted workflow efficiency.
What is the amino acid sequence of Vilon?
Vilon is a synthetic dipeptide with the chemical sequence Lysyl-Glutamic acid (Lys-Glu / KE).
How does Vilon influence cell proliferation in laboratory models?
Preclinical studies indicate Vilon binds directly to chromatin structures, inducing heterochromatin decondensation. This structural modification unmasks DNA promoter regions, enhancing gene expression, protein synthesis, and cellular entry into the S and G2/M cell cycle phases.
What purity level does PX1 Research guarantee for Vilon?
PX1 Research provides Vilon at a verified purity standard of ≥98%, confirmed via lot-specific RP-HPLC peak area integration and Mass Spectrometry molecular weight verification.
How should reconstituted Vilon be stored in the lab?
Once reconstituted with sterile PBS or bacteriostatic water, Vilon should be divided into single-use aliquots and stored at -20°C or -80°C to preserve peptide stability and prevent degradation from repeated freeze-thaw cycles.
Are PX1 Research peptides tested for endotoxins?
Yes. Every production batch undergoes LAL endotoxin testing to ensure levels remain under strict threshold limits (<0.01 EU/mg), eliminating confounding inflammatory variables in cell culture assays.
Can Vilon be used in human clinical trials or consumer products?
No. Vilon supplied by PX1 Research is strictly designated for in vitro, ex vivo, and non-clinical laboratory research use only. It is not for human or animal consumption, medical diagnosis, or therapeutic applications.
How does Vilon differ structurally from Epithalon?
Vilon is a dipeptide composed of two amino acids (Lys-Glu), primarily targeting chromatin structure and rapid cell proliferation. Epithalon is a tetrapeptide (Ala-Glu-Asp-Gly) designed around pineal gland regulation and telomerase expression.
Does PX1 Research offer institutional account pricing for bulk peptide orders?
Yes. Academic institutions, biotechnology firms, and contract research organizations (CROs) can request tiered pricing and bulk supply agreements through the PX1 Research wholesale program.
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.