Thymosin Alpha-1 vial 10 mg

Thymosin Alpha-1 is a synthetic polypeptide of the class of thymic peptides, chemically a linear, N-terminally acetylated peptide of 28 amino acids. In scientific research, it is studied as a model compound for receptor-mediated signal transduction and as a reference standard in analytical work. This compound is offered as a freeze-dried powder of 10 mg per vial, exclusively for laboratory and research purposes.

What is Thymosin Alpha-1?

Thymosin Alpha-1 (Thymalfasine, Tα1) is a polypeptide with the sequence Ac-Ser-Asp-Ala-Ala-Val-Asp-Thr-Ser-Ser-Glu-Ile-Thr-Thr-Lys-Asp-Leu-Lys-Glu-Lys-Lys-Glu-Val-Val-Glu-Glu-Ala-Glu-Asn, which structurally corresponds to the N-terminal fragment of the precursor protein prothymosin alpha (113 amino acids). The molecule is strongly acidic in character due to the high proportion of glutamic acid and aspartic acid residues and contains no cysteine ​​and therefore no disulfide bridges. This structure—a short, unbound chain without a tertiary fold structure, with a defined chemical modification—makes the compound a reproducible model in peptide chemistry and structure-activity research.

In research models, Thymosin Alpha-1 is primarily studied for its interaction with Toll-like receptors, particularly TLR2 and TLR9, on isolated myeloid cells. In vitro, it has been described that this receptor binding modulates downstream signaling pathways, including NF-κB, p38 MAPK, and IRF3, and that in cell models, tryptophan catabolism is influenced via the enzyme indoleamine-2,3-dioxygenase (IDO). N-terminal acetylation appears to be the determining factor for the degree of receptor interaction in cell models, enabling comparative research with non-acetylated analogues. Consequently, Thymosin Alpha-1 is used as a model compound and reference substance within scientific research.

Research areas

In a laboratory context, Thymosin Alpha-1 occurs in the following research areas, among others:

• Receptor research into Toll-like receptors (TLR2 and TLR9) and the associated ligand-receptor affinity in isolated cell models in vitro.
• Enzymological research into the modulation of indoleamine-2,3-dioxygenase and tryptophan catabolism in cell culture systems.
• Research into intracellular signal transduction, with NF-κB-, p38-MAPK-, and IRF3-mediated cascades as readout parameters.
• Structure-activity research into the role of N-terminal acetylation and acidic amino acid residues in short peptide chains.
• Analytical method development and validation (HPLC, LC-MS, amino acid analysis) using Thymosin Alpha-1 as the reference standard.
• Stability and solubility studies of freeze-dried polypeptides under controlled temperature and pH conditions.

Each of these applications involves controlled laboratory or preclinical model research.

Thymosin Alpha-1 in our research assortment

Thymosin Alpha-1 falls under the category of freeze-dried peptides in vial form within our product range. While this compound targets receptor-mediated signal transduction via Toll-like receptors, other components within the same product line have been specifically chosen to cover enzymatic, growth factor-linked, or membrane-linked targets. These compounds share the freeze-dried vial form and associated handling requirements, but differ fundamentally in amino acid sequence, molecular size, and investigated mechanism.

Specifications

Shape, handling and storage

Thymosin Alpha-1 is supplied as a freeze-dried powder with a standardized 10 mg per vial. Unlike solid tablet forms, this is a lyophilisate: the material is placed in a suitable solvent prior to analytical work. The powder may lie as a thin layer or loose cake at the bottom or against the wall of the vial; this is inherent to the freeze-drying process.

Store the closed vial in a cool, dry place, protected from direct light, in the original packaging; for long-term storage, −20 °C is customary. Handle the compound with standard laboratory precautions: work in a clean environment, use appropriate protective equipment, avoid repeated temperature changes, and prevent cross-contamination. Keep the packaging out of reach of unauthorized persons.

Composition and lab results

This lyophilisate has a controlled purity of ≥ 99% (HPLC). The vial contains the freeze-dried polypeptide without added active ingredients; buffer salt residues from the manufacturing process may be present, as is common with synthetically prepared peptides.

You can find an overview of the available analytical documentation on our lab results pageThe reports are centrally collected there for your own research records.

Frequently Asked Questions

To which substance class does Thymosin Alpha-1 belong?
It is a synthetic polypeptide of 28 amino acids from the class of thymic peptides: not a small organic molecule, but a linear amino acid chain with an acetyl group at the N-terminus.

What role does prothymosin alpha play in research?
Thymosin Alpha-1 is sequence-matched to the N-terminal region of prothymosin alpha, an 113-amino acid precursor protein. In research models, this relationship is used to determine which part of the chain is responsible for the observed receptor interaction in vitro.

In what form is the connection supplied?
As freeze-dried powder (lyophilisate) of 10 mg in a sealed vial, with a purity of ≥ 99% (HPLC).

How do I store the vial?
Cool, dry, and protected from light, preferably in the original packaging. For long-term storage, a temperature of -20°C is generally maintained.