Thymosin Alpha-1
A 28-amino-acid acetylated thymic peptide studied in cell-based receptor-signaling and structural-biology research models.
Quick answers
What is Thymosin Alpha-1?
Thymosin Alpha-1 is a 28-amino-acid acetylated thymic peptide studied in cell-based receptor-signaling and structural-biology research models. It is a linear N-terminally acetylated polypeptide (28 residues; thymic peptide) with a molecular weight of ~3,108.3 Da and the formula C129H215N33O55.
How much published research cites Thymosin Alpha-1?
The Luvaminos Thymosin Alpha-1 record cites 26 published references, dated 1977 to 2024. Each is listed on this page with a link to its source.
Does Luvaminos test Thymosin Alpha-1, and where is the certificate?
Luvaminos does not currently stock Thymosin Alpha-1. Every peptide lot Luvaminos sells is tested by Freedom Diagnostics Testing, PLLC, an independent laboratory, and its certificate is published at luvaminos.com/coa under the lot number printed on the vial.
What modifications does Thymosin Alpha-1 carry?
Thymosin Alpha-1: N-terminal acetylation at Ser1; highly acidic (pI 4.2); no cysteine residues or disulfide bonds; linear peptide.
How is Thymosin Alpha-1 powder stored?
Sealed Thymosin Alpha-1 powder: −20 °C (±5 °C); white to off-white powder; protect from heat, light, and moisture. Linear peptide; no cysteine residues or disulfide bonds; N-terminal acetylation reported to confer resistance to aminopeptidase degradation.
How is Thymosin Alpha-1 different from Thymalin?
Thymosin Alpha-1 and Thymalin are different compounds: Thymosin Alpha-1 has 28 amino acids, a molecular weight of ~3,108.3 Da and formula C129H215N33O55; Thymalin is a thymic peptide preparation (polypeptide complex). Thymosin Alpha-1: N-terminal acetylation at Ser1.
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.
Primary Database
References (26)
Reviews
1Garaci E, Paci M, Matteucci C, Costantini C, Puccetti P, Romani L. (2024). Frontiers in Medicine
- 2
Tao N, Xu X, Ying Y, Hu S, Sun Q, Lv G, Gao J. (2023). Molecules
- 3
Soeroto AY, Suryadinata H, Yanto TA, Hariyanto TI. (2023). Inflammopharmacology
- 4
Dominari A, Hathaway D, Pandav K, et al. (2020). World Journal of Virology
- 5
Costantini C, Bellet MM, Pariano M, Renga G, Stincardini C, Goldstein AL, Garaci E, Romani L. (2019). Frontiers in Oncology
- 6
Li C, et al. (2016). BMC Infectious Diseases
- 7
Camerini R, Garaci E. (2015). Expert Opinion on Biological Therapy
- 8
Zhang YY, Chen EQ, Yang J, Duan YR, Tang H. (2009). Virology Journal
Clinical
9Wang Z, Chen J, Zhu C, et al. (2021). Frontiers in Immunology
- 10
Liu Y, Pang Y, Hu Z, et al. (2020). Clinical Infectious Diseases
- 11
Wu J, Zhou L, Liu J, et al. (2013). Critical Care
- 12
Ciancio A, Andreone P, Kaiser S, et al. (2012). Journal of Viral Hepatitis
DOI: 10.1111/j.1365-2893.2011.01524.xPubMed 22233415NCT01178996
- 13
Maio M, Mackiewicz A, Testori A, et al. (2010). Journal of Clinical Oncology
- 14
Poo JL, Sánchez-Ávila F, Kershenobich D, et al. (2004). Journal of Gastroenterology and Hepatology
- 15
Chien RN, Liaw YF, et al. (1998). Hepatology
- 16
Gravenstein S, Duthie EH, Miller BA, et al. (1989). Journal of the American Geriatrics Society
Primary research
17Matteucci C, Nepravishta R, Argaw-Denboba A, et al. (2023). International Immunopharmacology
- 18
Romani L, Oikonomou V, Moretti S, et al. (2017). Nature Medicine
- 19
Nepravishta R, Mandaliti W, Eliseo T, et al. (2015). Expert Opinion on Biological Therapy
- 20
Elizondo-Riojas MA, Chamow SM, Tuthill CW, Gorenstein DG, Volk DE. (2011). Biochemical and Biophysical Research Communications
- 21
Bozza S, Gaziano R, Bonifazi P, et al. (2007). International Immunology
- 22
Romani L, Bistoni F, Montagnoli C, et al. (2006). Blood
- 23
Zhang P, Chan J, Dragoi AM, et al. (2005). EMBO Reports
- 24
Romani L, Bistoni F, Gaziano R, et al. (2004). Blood
- 25
Grottesi A, Sette M, Palamara T, et al. (1998). Peptides
- 26
Goldstein AL, et al. (1977). Proc Natl Acad Sci USA
Related compounds