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Thymosin α1 (Tα1), also known as thymalfasin, is a 28-amino-acid N-terminally acetylated peptide derived from the thymosin family. Its sequence is Ac-SDAAVDTSSEITTKDLKEKKEVVEEAEN.
Tα1 has been extensively studied as an immunomodulatory peptide in dendritic cells, T lymphocytes and other immune-cell systems. Its effects are context-dependent and involve multiple innate and adaptive immune pathways rather than a single receptor mechanism.
Product Information
| Property | Specification |
|---|---|
| Product Name | Thymosin α1 (Thymalfasin) |
| CAS No. | 62304-98-7 |
| 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 |
| One-Letter Sequence | Ac-SDAAVDTSSEITTKDLKEKKEVVEEAEN |
| Peptide Length | 28 amino-acid residues |
| Molecular Formula | C129H215N33O55 |
| Molecular Weight | Approximately 3108.3 Da |
| N-Terminus | Acetylated Ser |
| C-Terminus | Free carboxyl terminus |
| Research Areas | Dendritic cells, T-cell biology, innate immunity, immune regulation |
N-Terminal Acetylation Is Part of the Molecule
Thymosin α1 begins with N-acetyl-Ser. The acetyl group is covalently attached to the peptide backbone and forms part of the defined molecular structure.
We recommend distinguishing N-terminal acetylation from an acetate counterion when comparing product specifications, molecular weight or analytical data between suppliers.
Immune-Cell Research
Tα1 has been studied across multiple immune-cell populations, including dendritic cells and CD4+ and CD8+ T cells. Its biological effects vary with activation state, cellular background and experimental stimulus.
Recent cell-subset profiling found comparatively strong transcriptional effects in activated CD8+ T cells, while effects on tumor-cell transcription were much more limited under the study conditions.
This reinforces the importance of defining the target cell population when Tα1 is used in mechanistic immunology experiments.
Recent TLR7 and Dendritic-Cell Mechanism
A 2026 study identified an additional mechanistic role for Tα1 in dendritic cells. In that system, Tα1 associated with apoptotic-body-derived microRNAs and protected selected RNA species from lysosomal degradation, supporting TLR7-dependent dendritic-cell activation and downstream CD8+ T-cell responses.
These findings expand the experimental framework for Tα1 beyond a generalized description as an “immune stimulant” and illustrate its potential role in nucleic-acid-associated innate immune signaling.
Synthetic and Quality Considerations
Thymosin α1 is a relatively acidic 28-residue peptide containing multiple Asp and Glu residues. Identity, N-terminal acetylation, molecular mass and chromatographic purity should be evaluated together for quantitative studies.
For sensitive immune-cell experiments, contamination and counterion specifications may also be relevant. Our Peptide Quality Control capabilities support analytical HPLC and mass spectrometry according to the selected specification.
Frequently Asked Questions
How many amino acids are in Thymosin α1?
Thymosin α1 contains 28 amino-acid residues.
Is the “Ac” in the sequence an acetate salt?
No. In Ac-SDAAVDTSSEITTKDLKEKKEVVEEAEN, Ac represents covalent N-terminal acetylation of the first serine residue.
Does Thymosin α1 act through only one immune receptor?
Current research supports context-dependent effects across several immune pathways and cell populations rather than a single universal receptor mechanism.
Can Thymosin α1 analogs be synthesized?
Sequence variants, terminal modifications and labeled constructs can be evaluated through Chemical Peptide Synthesis.