Thymosin Alpha-1

A 28-amino-acid acetylated thymic peptide studied in cell-based receptor-signaling and structural-biology research models.

Molecular Profile

Type
Linear N-terminally acetylated polypeptide (28 residues; thymic peptide)
Molecular formula
C129H215N33O55
Molecular weight
~3,108.3 Da
CAS number
62304-98-7
Amino acids
28
Sequence
Ac-SDAAVDTSSEITTKDLKEKKEVVEEAEN
Modification
N-terminal acetylation at Ser1; highly acidic (pI 4.2); no cysteine residues or disulfide bonds; linear peptide.

Mechanism & Target Class

An N-terminally acetylated 28-residue thymic peptide derived from prothymosin alpha. Research characterizes it as a pleiotropic signaling peptide engaging a family of cell-surface pattern-recognition receptors studied across several receptor subtypes and cell populations, with reports spanning multiple receptor-subtype engagements. Downstream signal transduction proceeds through the adaptor protein MyD88 and nodes including TRAF6, IRAK4, IKK, NF-κB, p38 MAPK, and IRF3/IRF7, with measured outputs including cell-maturation markers, interleukin-12 production, type I interferon induction, IDO-mediated tryptophan catabolism, NK-cell activity markers, and T-cell differentiation markers. Structurally, the peptide is disordered in aqueous solution and adopts helical conformations in membrane-mimetic environments; biophysical studies have characterized N-terminal insertion into phospholipid vesicles, serum-albumin carriage, and interactions with galectin-1. No single high-affinity receptor has been definitively established across the literature.

Storage & Handling

Lyophilized
−20 °C (±5 °C); white to off-white powder; protect from heat, light, and moisture.
Handling
Linear peptide; no cysteine residues or disulfide bonds; N-terminal acetylation reported to confer resistance to aminopeptidase degradation. Aliquot to minimize freeze–thaw exposure.

Primary Database

PubChem CID 16130571 ↗

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