Peptide Registry

Thymogen

Price range: $29.00 through $49.00

  • Contents: Thymogen (Glu-Trp; EW dipeptide; glutamyl-tryptophan)
  • Form: Lyophilized powder
  • Purity: >99%
Quantity Discount Price
1 - 3 - -
4 - 7 10% -
8 + 18% -
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Description

Thymogen is the defined synthetic form of the EW dipeptide, glutamyl-tryptophan. It is isolated from Thymalin via reversed-phase HPLC and subsequently synthesized as a precisely characterized molecular entity. However, where Thymalin is a complex extract, Thymogen is a single sequence. Its DNA-binding sequence has been identified through molecular docking as GGAG, a specific interaction that positions it in specialty research peptide immune gene regulation research as a tool for probing how minimal peptide sequences encode tissue-specific regulatory information.

Chemical Information

  • Chemical Name: Thymogen (L-glutamyl-L-tryptophan)
  • Also Known As: Glu-Trp; L-glutamyl-L-tryptophan
  • Compound Class: Synthetic dipeptide; immunomodulatory bioregulator (Khavinson series)
  • Sequence: Glu-Trp
  • Molecular Formula: C16H19N3O5
  • Molecular Weight: 333.3 g/mol
  • CAS Number: Not independently confirmed against a public chemical registry

Applications

  • Immune signaling and T-cell regulation research. Thymogen is a synthetic dipeptide studied for its role in modulating immune cell differentiation and cytokine signaling. This positions it alongside Thymalin as a research tool for thymus-related immune regulation, but as a single defined molecular entity rather than a polypeptide extract
  • Monocyte/macrophage inflammatory signaling research. Published in vitro work using the human THP-1 monocytic cell line found that Thymogen, alongside Epithalon, Vilon, Thymalin, and Chonluten, modulated LPS-stimulated cytokine output and proliferative signaling. Researchers use this shared dataset to compare relative anti-inflammatory and immunomodulatory effects across the Khavinson peptide family
  • Comparative dipeptide bioregulator research. As one of the simplest Khavinson-series compounds (a single dipeptide with a defined structure), Thymogen is used as a reference point in structure-activity research comparing di-, tri-, and tetrapeptide bioregulators (e.g., Vilon, Chonluten, Epithalon) for immunomodulatory potency
  • Note on evidence base: Published data on Thymogen is mostly in Russian-language pharmacological literature, where it has been studied as a registered immunomodulatory agent; independent Western replication is more limited

Storage and Handling

Store lyophilized powder under refrigeration (2-8C), protected from heat, light, and moisture. Thymogen dissolves readily in aqueous buffer; store reconstituted solution at 2-8C and use promptly, avoiding repeated freeze-thaw cycles.

Compliance Notice

Thymogen is for laboratory research use only. They are not for human or veterinary use and carry no therapeutic, diagnostic, or clinical indication. FDA has not evaluated this product. By purchasing this product, the buyer confirms that they will follow appropriate institutional safety procedures and use it exclusively for controlled research.

Frequently Asked Questions

What is Thymogen?

Thymogen (EW) is the synthetic dipeptide glutamyl-tryptophan, isolated from the Thymalin polypeptide complex and synthesized as a defined molecular entity. It is studied for immune gene regulation through direct DNA binding at the GGAG sequence, T-cell maturation in thymic cell models, and cAMP/cGMP balance modulation. Its precise chemical identity makes it the appropriate tool when mechanistic thymic research requires a single defined sequence rather than a complex extract.

How does Thymogen relate to Thymalin?

Thymogen is the defined synthetic form of Thymalin's primary active component. Thymalin is a polypeptide complex containing multiple bioactive sequences, including EW and KE. Thymogen isolates the EW sequence as a single compound, providing chemical homogeneity and allowing researchers to attribute observed effects specifically to the EW sequence rather than to the full complement of bioactive peptides present in Thymalin.

What makes the GGAG DNA binding specificity significant?

GGAG is the specific double-stranded DNA sequence that molecular docking studies identify as the preferential binding site for the EW dipeptide. This sequence specificity supports the Khavinson hypothesis that short bioregulatory peptides achieve tissue-specific gene regulation through direct promoter region binding rather than through non-specific charge-based interactions. For researchers studying the molecular basis of peptide-DNA interaction, this defined binding sequence makes Thymogen a tractable model compound.