Vesilute 10mg

Description

Disclaimer: Vesilute is not approved by the U.S. Food and Drug Administration (FDA) for human or veterinary use. It is intended strictly for laboratory and research purposes only.

What is Vesilute?

Vesilute is a synthetic dipeptide belonging to the peptide bioregulator class, with the amino acid sequence Glu-Asp (ED). It is a tissue-derived short regulatory peptide originally isolated from urinary bladder tissue and is categorized within the cytomechin family of peptide bioregulators, a group of compounds investigated in preclinical models for their proposed capacity to modulate gene transcription and cellular regulatory activity in target tissue-specific cell preparations.

Vesilute has been investigated in preclinical and in vitro settings for its proposed interactions with chromatin-associated proteins and its capacity to modulate transcriptional activity in urogenital epithelial and smooth muscle cell preparations. Research interest in Vesilute centers on its utility as a laboratory tool for studying tissue-specific dipeptide bioregulator activity, the mechanistic basis of short peptide regulatory activity in urothelial cell models, and the relationship between the Glu-Asp sequence and chromatin accessibility in bladder tissue-relevant cell systems.

Vesilute is not an approved therapeutic compound. It is intended exclusively for qualified researchers operating in controlled laboratory environments. It is not a dietary supplement or consumer product and has no approved indications for human or veterinary use. Research interest in Vesilute extends to the broader genitourinary system, including prostate gland preparations, where related cytomechin ED-sequence compounds have been investigated in preclinical smooth muscle cell regulation models 

PROPERTIES OF VESILUTE

Property	Details
CAS Number	3918-84-1
Molar Mass	262.2 Da
Chemical Formula	C₉H₁₄N₂O₇
Stability / Shelf Life	24 months when stored lyophilized at −20°C under recommended conditions
Synonyms	ED peptide; Glu-Asp; alpha-glutamylaspartic acid; bladder cytomedine
Storage Instructions	−20°C (lyophilized); protect from light, heat, and moisture
Amino Acid Sequence	Glu-Asp (ED)
WADA Status	Not listed on the WADA 2026 Prohibited List

WORKING MECHANISM OF VESILUTE

Vesilute is proposed to exert its observed regulatory activity in experimental models through interaction with chromatin-associated histone proteins, consistent with the mechanistic profile reported for related short-chain peptide bioregulators within the cytomechin class. In cell-free and cell-based laboratory systems, short ED-sequence dipeptides have been proposed to associate with histone fractions involved in chromatin condensation, modulating the structural accessibility of heterochromatin-associated gene sequences in target tissue-relevant cell preparations.

Mechanistically, Vesilute is thought to influence:

• Histone protein interaction in cell-free chromatin preparations, proposed based on mechanistic studies conducted with structurally related cytomechin peptides in the peer-reviewed literature
• Transcriptional activity modulation in urothelial and smooth muscle cell preparations, investigated in preclinical models using bladder tissue-derived cell systems
• Chromatin condensation state alterations in target tissue cell preparations, consistent with the epigenetic regulatory mechanism proposed for the broader cytomechin peptide bioregulator class
• Tissue-specific regulatory activity in urogenital epithelial cell models, investigated in the context of understanding the functional specificity of short peptide bioregulators across different tissue-derived cell preparations

The precise molecular receptor or binding partner for Vesilute has not been definitively identified in the published literature. The compound is proposed to act at the chromatin level through histone-associated interactions rather than through classical membrane receptor-ligand kinetics. All mechanistic findings relevant to Vesilute are extrapolated from the broader cytomechin class literature and from limited compound-specific preclinical studies. Findings are not consistent across all experimental systems examined.

What are the Potential Research Observations of Vesilute?

The following research findings are based on articles retrieved from PubMed and are reported from preclinical and in vitro studies only. These findings do not constitute clinical evidence.

Tissue-Specific Peptide Bioregulator Activity in Urogenital Cell Models:
Vesilute has been investigated in preclinical models as a tissue-specific peptide bioregulator derived from bladder tissue. In cell-based laboratory preparations using urothelial and smooth muscle cell systems, short ED-sequence peptides have been studied for their proposed capacity to modulate transcriptional activity in target tissue-relevant preparations. These observations contribute to understanding the tissue-specificity of short peptide regulatory activity within the cytomechin class and the mechanistic basis for organ-specific peptide bioregulator function. Findings are from controlled in vitro systems and have not been validated in clinical contexts. [Khavinson et al., 2012]

Chromatin Remodeling and Epigenetic Regulatory Research Models:

Vesilute has been studied within the broader framework of cytomechin class peptide bioregulator research, examining short peptide-mediated chromatin remodeling. Preclinical investigations employing structurally related peptides from the same class have documented associations between short regulatory peptide exposure and modulation of heterochromatin condensation state in target cell preparations. These findings provide a mechanistic research framework for understanding Vesilute’s proposed activity in analogous experimental systems. Data are from cell-based in vitro models and require compound-specific validation. [Khavinson et al., 2012]

Comparative Cytomechin Class Research:

Vesilute has been studied comparatively alongside related tissue-derived peptide bioregulators within the cytomechin class in research frameworks examining the structural and functional determinants of tissue-specific short peptide regulatory activity. Comparative studies have used the ED dipeptide sequence to investigate differential transcriptional regulatory profiles across target and non-target tissue cell preparations, contributing to foundational research on organ-specific peptide bioregulator mechanisms. Observations are from controlled preclinical systems, and findings are not consistent across all experimental models examined. [Khavinson and Morozov, 2003]

Note: Vesilute is not approved by the U.S. Food and Drug Administration (FDA) for human or veterinary use. It has no approved therapeutic indications. This compound is intended strictly for scientific research purposes only.

Safety Profile and Toxicological Considerations

Researchers have noted the following observations in experimental settings. Long-term safety data remain absent, and a complete toxicity profile has not been established in any biological system.

• Published in vitro data do not report significant cytotoxicity in cell preparations exposed to Vesilute at research-relevant concentrations, consistent with the general tolerability profile observed for related short peptide bioregulators in the cytomechin class
• No LD50 or chronic toxicity data are available in the peer-reviewed literature specifically for Vesilute
• No human pharmacokinetic, pharmacodynamic, or clinical safety profile has been established for this compound
• Inadvertent laboratory exposure risks are not characterized; no human safety data exists
• Immunogenicity, organ-level toxicity, and off-target transcriptional effects remain uncharacterized at the preclinical level
• As a short synthetic dipeptide, Vesilute is expected to be highly susceptible to rapid proteolytic degradation in biological matrices, which must be carefully accounted for in experimental design and result interpretation

WHY CHOOSE RCDBIO FOR VESILUTE?

Each batch of Vesilute supplied by RCDbio undergoes independent third-party laboratory testing, with a batch-specific Certificate of Analysis (COA) available for researcher verification before experimental use.

• Independent third-party laboratory testing per batch
• COA confirming compound identity and purity per lot
• Molecular identity confirmed against CAS 3918-84-1
• RCDbio does not self-certify; all quality verification is conducted by accredited independent laboratories

Disclosure: Sponsored by RCDbio. This content is for informational purposes only and does not constitute an endorsement of any product for human use.

FREQUENTLY ASKED QUESTIONS

Is Vesilute approved for human use?

No. Vesilute is not approved by the FDA for any human or medical application. It is classified as a research-use peptide only and has no approved therapeutic indications in the United States or any other regulatory jurisdiction. It is intended exclusively for qualified researchers in controlled laboratory settings.

What is Vesilute, and what tissue is it derived from?

Vesilute is a synthetic dipeptide with the sequence Glu-Asp (ED), originally isolated from urinary bladder tissue. It belongs to the cytomechin class of tissue-derived short peptide bioregulators, a group of compounds studied in preclinical models for their proposed tissue-specific transcriptional regulatory activity. The ED dipeptide sequence is distinct from related bioregulators such as Vilon (KE, thymus-derived), Livagen (KEDA, liver-derived), and Epithalon (AEDG, pineal-derived), each characterized by unique amino acid sequences and proposed tissue-specific regulatory profiles.

What molecular target is Vesilute proposed to interact with in research models?

Based on the mechanistic literature available for the cytomechin peptide bioregulator class, Vesilute is proposed to interact with histone proteins involved in chromatin condensation, modulating the structural accessibility of heterochromatin regions in target tissue-relevant cell preparations. A specific high-affinity receptor has not been definitively characterized for Vesilute specifically. Mechanistic extrapolations are based on class-level research conducted with structurally related short peptide bioregulators in cell-free and cell-based laboratory systems.

How should Vesilute be stored in a laboratory setting?

Lyophilized Vesilute should be stored at −20°C in a sealed, desiccated container protected from light, heat, and moisture. Reconstituted solutions should be stored at 4°C and used within 7 to 14 days. Single-use aliquots are recommended before freezing to avoid repeated freeze-thaw cycles, which are associated with reduced peptide integrity. Shelf life under recommended lyophilized storage conditions is reported at up to 24 months.

What experimental systems have been used in Vesilute and related cytomechin research?

Published laboratory studies relevant to the cytomechin class and to Vesilute specifically have employed urothelial cell preparations, bladder tissue-derived cell systems, and cell-free chromatin preparations in histone binding assays. Comparative research has also used in vivo rodent models examining tissue-specific peptide bioregulator activity. All findings are from preclinical or cell-based experimental systems and do not represent validated clinical data.

REFERENCES

Khavinson, V. K., Linkova, N. S., Polyakova, V. O., Kheifets, O. V., Tarnovskaya, S. I., & Kvetnoy, I. M. (2012). Peptides tissue-specifically stimulate cell differentiation during aging. Bulletin of Experimental Biology and Medicine, 153(1), 148–151. https://pubmed.ncbi.nlm.nih.gov/22808515/ 

Khavinson, V. Kh., & Morozov, V. G. (2003). Peptides of the pineal gland and thymus prolong human life. Neuro Endocrinology Letters, 24(3-4), 233–240. https://pubmed.ncbi.nlm.nih.gov/14523363/ 

Research transparency note: As of June 2026, peer-reviewed publications indexed on PubMed specifically examining the Glu-Asp (Vesilute) dipeptide sequence in isolation are limited. The above references relate to the cytomechin peptide bioregulator research context established by V. Kh. Khavinson and colleagues, whose laboratory originally characterized Vesilute alongside related tissue-derived short peptide bioregulators. Researchers are encouraged to consult primary literature for additional compound-specific data.

Disclaimer

Vesilute is exclusively for laboratory research purposes. RCDbio products are not intended to diagnose, prevent, treat, or cure any disease or medical condition. The Food and Drug Administration has not evaluated the statements on this page. Researchers must comply with all applicable local laws and regulations governing the use of research compounds. By purchasing, you agree to RCDbio Terms and Conditions. RCDbio reserves the right to refuse sales to unauthorized individuals.