Thymosin Alpha-1 is a natural regulator of immune function. Since its discovery in 1972—isolated from thymus gland tissue—it has been studied for its potential therapeutic role in a wide range of conditions, including:
Cystic fibrosis
Infectious diseases (e.g., tuberculosis, cytomegalovirus)
Respiratory disorders
Chronic hepatitis
Cancer
Thymosin Alpha-1 is recognized as a potent immune modulator, making it of high interest in both clinical and research settings.
$50 USD
Out of stock
Expiry date | 3/12/27 |
Date Produced | 3/12/25 |
CAS # | 62304-98-7 |
Formula | C₁₂₉H₂₁₅N₃₃O₅₅ |
M.W. | 3108.315 g/mol |
REF | 16130571 |
Purity | 99% HPLC |
RUO | Research Use Only |
Not for human or veterinary use. Made in USA
This product is intended as a research chemical only. Not for human use. Peptides will arrive in a lyophilized (powder) form for maximum stability.
Thymosin Alpha-1 is a naturally occurring peptide fragment first discovered in 1972. It has since been studied in clinical trials for a variety of conditions, including cystic fibrosis, infections (such as tuberculosis and cytomegalovirus), respiratory disorders, chronic hepatitis, and cancer. It is currently approved for use in treating chronic hepatitis B and C in 35 under-developed nations.
Sequence: 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
Molecular Formula: C₁₂₉H₂₁₅N₃₃O₅₅
Molecular Weight: 3108.315 g/mol
PubChem CID: 16130571
CAS Number: 62304-98-7
Synonyms: Thymalfasin
Thymosin alpha-1, originally isolated from thymus tissue, is a potent immune regulator. The thymus plays a critical role in producing and maturing T-cells, which are essential for adaptive immunity. Research in thymus-deficient mice shows that thymosin alpha-1 alone can restore immune function and prevent widespread infection. It does this by activating signaling pathways and stimulating cytokine production [¹].
In vaccine development, thymosin alpha-1 may improve the immune response to inactivated vaccines, potentially resulting in stronger and longer-lasting immunity [²]. It may also be valuable in sepsis, helping to reduce mortality and long-term complications by regulating overactive immune responses [³].
Thymosin alpha-1 supports neurodevelopment, particularly in developing brains. Studies in mice show it enhances cognitive function, promotes neuron growth, and suppresses inflammation-related neural damage [⁴]. This makes it a potential candidate for treating neurodevelopmental conditions like cerebral palsy.
Image: 4-week-old mice given thymosin alpha-1 learned to escape mazes faster.
Source: PubMed
Thymosin alpha-1 matures dendritic cells, boosting the immune system’s ability to recognize and fight fungal infections such as aspergillosis [⁵]. By improving antigen presentation, it enhances immune responses at their foundational level [⁶].
Approved in 35+ countries, thymosin alpha-1 is used to treat chronic hepatitis B and C. It also enhances vaccine responses for both viruses and is considered a highly cost-effective therapy [⁷].
Thymosin alpha-1 may restore immune function in HIV patients undergoing antiretroviral therapy (HAART), helping to correct immune imbalances and improve overall quality of life [⁸][⁹]. It may also inhibit latent HIV reactivation by stimulating CD8+ T-cell responses.
New studies show thymosin alpha-1 can inhibit angiotensin-converting enzyme (ACE), leading to reduced blood pressure and potential cardiovascular benefits [¹⁰]. It may offer a safer alternative to traditional ACE inhibitors.
Research shows thymosin alpha-1 inhibits cancer cell growth and migration in lung cancer models [¹¹]. In combination with chemotherapy (e.g., dacarbazine), it has increased progression-free survival without added toxicity [¹²][¹³]. Modified long-acting versions are also showing enhanced anticancer effects in breast cancer models [¹⁴][¹⁵].
Cancers being studied in connection with thymosin alpha-1:
Breast cancer
Melanoma
Liver cancer
Lung cancer
Colon cancer
Thymosin alpha-1 reduces inflammatory pain by inhibiting cytokine production (e.g., TNF-α, IL-1β) at the site of inflammation. This mechanism differs from traditional NSAIDs and may offer fewer side effects [¹⁶].
In cystic fibrosis (CF), thymosin alpha-1 reduces inflammation and may restore function to the defective CFTR protein. It is under investigation as a promising single-molecule therapy for CF [¹⁷].
In cases of avulsed (knocked-out) front teeth, thymosin alpha-1 improves gum healing and increases the survival of replanted teeth. This makes it a promising adjunct in traumatic dental injury treatment [¹⁸].
The potential applications of Thymosin Alpha-1 are too numerous to list in a single summary. What stands out, however, is that the peptide is already in medical use in several countries. Researchers are actively exploring ways to enhance its efficacy and improve production methods to make it faster and more cost-effective [¹⁹]. Given its promising immune-modulating effects and low side effect profile, clinical trials for new Thymosin Alpha-1 variants are expected to expand in the coming years across indications ranging from cancer to infectious disease.
Thymosin Alpha-1 exhibits minimal side effects, low oral, and excellent subcutaneous bioavailability in mice.
Note: Per kg dosages in mice do not translate to humans.
Thymosin Alpha-1 sold at Ai-Peptides is strictly for educational and scientific research purposes only. It is not for human consumption.
Only licensed researchers are authorized to purchase this compound.
The above literature was researched, edited, and organized by Dr. Logan, M.D.
Dr. Logan holds a doctorate from Case Western Reserve University School of Medicine and a B.S. in Molecular Biology.
Allan L. Goldstein, MD is the Professor and Catharine B. & William McCormick Chair of the Department of Biochemistry and Molecular Biology at The George Washington University School of Medicine and Health Sciences, where he has served since 1978.
Thymosins were first discovered in the mid-1960s when Dr. Goldstein, working in the laboratory of Abraham White at the Albert Einstein College of Medicine in New York, studied the role of the thymus in the development of the vertebrate immune system. He is widely regarded as a leading expert on the thymus gland and the immune system and is one of the co-discoverers of the thymosins.
Dr. Goldstein has authored over 400 scientific publications, holds more than 15 U.S. patents, and has edited multiple books in the fields of biochemistry, immunology, neurobiology, and biomedicine. He serves on editorial boards for numerous scientific and medical journals and has consulted for various research organizations in both the private and public sectors. He is also the co-founder of the Institute for Advanced Studies in Aging and Geriatric Medicine, a member of the Board of Trustees for the Albert Sabin Vaccine Institute, and Chairman of the Board of RegeneRx Biopharmaceuticals.
Dr. Goldstein earned his B.S. from Wagner College (1959), and his M.S. and Ph.D. from Rutgers University (1964). He was on the faculty of the Albert Einstein College of Medicine from 1964 to 1972, and later joined the University of Texas Medical Branch in Galveston as Professor and Director of the Division of Biochemistry.
R. King and C. Tuthill, “Immune Modulation with Thymosin Alpha 1 Treatment,” Vitam. Horm., vol. 102, pp. 151–178, 2016.
PubMed
C. Zhang et al., “Gene cloning, expression and immune adjuvant properties of the recombinant fusion peptide Tα1-BLP on avian influenza inactivate virus vaccine,” Microb. Pathog., vol. 120, pp. 147–154, Jul. 2018.
PubMed
F. Pei et al., “Thymosin alpha 1 treatment for patients with sepsis,” Expert Opin. Biol. Ther., vol. 18, no. sup1, pp. 71–76, 2018.
PubMed
G. Wang et al., “Immunopotentiator Thymosin Alpha-1 Promotes Neurogenesis and Cognition in the Developing Mouse via a Systemic Th1 Bias,” Neurosci. Bull., vol. 33, no. 6, pp. 675–684, Dec. 2017.
PubMed
L. Romani et al., “Thymosin α 1 activates dendritic cells for antifungal Th1 resistance through Toll-like receptor signaling,” Blood, vol. 103, no. 11, pp. 4232–4239, Jun. 2004.
PubMed
L. Romani et al., “Thymosin alpha1: an endogenous regulator of inflammation, immunity, and tolerance,” Ann. N. Y. Acad. Sci., vol. 1112, pp. 326–338, Sep. 2007.
PubMed
A. L. Goldstein and A. L. Goldstein, “From lab to bedside: emerging clinical applications of thymosin alpha 1,” Expert Opin. Biol. Ther., vol. 9, no. 5, pp. 593–608, May 2009.
PubMed
C. Matteucci et al., “Thymosin alpha 1 and HIV-1: recent advances and future perspectives,” Future Microbiol., vol. 12, pp. 141–155, 2017.
PubMed
C. Matteucci et al., “Thymosin α 1 potentiates the release by CD8(+) cells of soluble factors able to inhibit HIV-1 and human T lymphotropic virus 1 infection in vitro,” Expert Opin. Biol. Ther., vol. 15 Suppl 1, pp. S83–100, 2015.
PubMed
J. Kharazmi-Khorassani et al., “Antioxidant and angiotensin-converting enzyme (ACE) inhibitory activity of thymosin alpha-1 (Thα1) peptide,” Bioorganic Chem., vol. 87, pp. 743–752, Jun. 2019.
PubMed
J. Kharazmi-Khorassani and A. Asoodeh, “Thymosin alpha-1; a natural peptide inhibits cellular proliferation, cell migration, the level of reactive oxygen species and promotes the activity of antioxidant enzymes in human lung epithelial adenocarcinoma cell line (A549),” Environ. Toxicol., May 2019.
PubMed
M. Maio et al., “Large randomized study of thymosin alpha 1, interferon alfa, or both in combination with dacarbazine in patients with metastatic melanoma,” J. Clin. Oncol., vol. 28, no. 10, pp. 1780–1787, Apr. 2010.
PubMed
R. Danielli et al., “Thymosin α1 in melanoma: from the clinical trial setting to the daily practice and beyond,” Ann. N. Y. Acad. Sci., vol. 1270, pp. 8–12, Oct. 2012.
PubMed
X. Shen et al., “Generation of a novel long-acting thymosin alpha1-Fc fusion protein and its efficacy for the inhibition of breast cancer in vivo,” Biomed. Pharmacother., vol. 108, pp. 610–617, Dec. 2018.
PubMed
F. Wang et al., “Thymosin Alpha1-Fc Modulates the Immune System and Down-regulates the Progression of Melanoma and Breast Cancer with a Prolonged Half-life,” Sci. Rep., vol. 8, no. 1, p. 12351, Aug. 2018.
Nature
Y. Xu et al., “Thymosin Alpha-1 Inhibits Complete Freund’s Adjuvant-Induced Pain and Production of Microglia-Mediated Pro-inflammatory Cytokines in Spinal Cord,” Neurosci. Bull., Feb. 2019.
PubMed
L. Romani et al., “Thymosin α1 represents a potential potent single-molecule-based therapy for cystic fibrosis,” Nat. Med., vol. 23, no. 5, pp. 590–600, May 2017.
PubMed
P. F. Day et al., “Interventions for treating traumatised permanent front teeth: avulsed (knocked out) and replanted,” Cochrane Database Syst. Rev., vol. 2, p. CD006542, May 2019.
PubMed
M. Schmidt et al., “Design of a substrate-tailored peptiligase variant for the efficient synthesis of thymosin-α1,” Org. Biomol. Chem., vol. 16, no. 4, pp. 609–618, Jan. 2018.
PubMed
All of our products are manufactured using the Lyophilization (Freeze Drying) process, which ensures that our products remain 100% stable for shipping for up to 3-4 months.
Once the peptides are reconstituted (mixed with bacteriostatic water), they must be stored in the fridge to maintain stability. After reconstitution, the peptides will remain stable for up to 30 days.
Lyophilization is a unique dehydration process, also known as cryodesiccation, where the peptides are frozen and then subjected to low pressure. This causes the water in the peptide vial to sublimate directly from solid to gas, leaving behind a stable, crystalline white structure known as lyophilized peptide. The puffy white powder can be stored at room temperature until you’re ready to reconstitute it with bacteriostatic water.
Once peptides have been received, it is imperative that they are kept cold and away from light. If the peptides will be used immediately, or in the next several days, weeks or months, short-term refrigeration under 4C (39F) is generally acceptable. Lyophilized peptides are usually stable at room temperatures for several weeks or more, so if they will be utilized within weeks or months such storage is typically adequate.
However, for longer term storage (several months to years) it is more preferable to store peptides in a freezer at -80C (-112F). When storing peptides for months or even years, freezing is optimal in order to preserve the peptide’s stability.
For further information on proper storage techniques, click the link below:
Peptide Storage Information
This product is intended as a research chemical only. Not for human use. Peptides will arrive in a lyophilized (powder) form for maximum stability.
Thymosin Alpha-1 is a naturally occurring peptide fragment first discovered in 1972. It has since been studied in clinical trials for a variety of conditions, including cystic fibrosis, infections (such as tuberculosis and cytomegalovirus), respiratory disorders, chronic hepatitis, and cancer. It is currently approved for use in treating chronic hepatitis B and C in 35 under-developed nations.
Sequence: 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
Molecular Formula: C₁₂₉H₂₁₅N₃₃O₅₅
Molecular Weight: 3108.315 g/mol
PubChem CID: 16130571
CAS Number: 62304-98-7
Synonyms: Thymalfasin
Thymosin alpha-1, originally isolated from thymus tissue, is a potent immune regulator. The thymus plays a critical role in producing and maturing T-cells, which are essential for adaptive immunity. Research in thymus-deficient mice shows that thymosin alpha-1 alone can restore immune function and prevent widespread infection. It does this by activating signaling pathways and stimulating cytokine production [¹].
In vaccine development, thymosin alpha-1 may improve the immune response to inactivated vaccines, potentially resulting in stronger and longer-lasting immunity [²]. It may also be valuable in sepsis, helping to reduce mortality and long-term complications by regulating overactive immune responses [³].
Thymosin alpha-1 supports neurodevelopment, particularly in developing brains. Studies in mice show it enhances cognitive function, promotes neuron growth, and suppresses inflammation-related neural damage [⁴]. This makes it a potential candidate for treating neurodevelopmental conditions like cerebral palsy.
Image: 4-week-old mice given thymosin alpha-1 learned to escape mazes faster.
Source: PubMed
Thymosin alpha-1 matures dendritic cells, boosting the immune system’s ability to recognize and fight fungal infections such as aspergillosis [⁵]. By improving antigen presentation, it enhances immune responses at their foundational level [⁶].
Approved in 35+ countries, thymosin alpha-1 is used to treat chronic hepatitis B and C. It also enhances vaccine responses for both viruses and is considered a highly cost-effective therapy [⁷].
Thymosin alpha-1 may restore immune function in HIV patients undergoing antiretroviral therapy (HAART), helping to correct immune imbalances and improve overall quality of life [⁸][⁹]. It may also inhibit latent HIV reactivation by stimulating CD8+ T-cell responses.
New studies show thymosin alpha-1 can inhibit angiotensin-converting enzyme (ACE), leading to reduced blood pressure and potential cardiovascular benefits [¹⁰]. It may offer a safer alternative to traditional ACE inhibitors.
Research shows thymosin alpha-1 inhibits cancer cell growth and migration in lung cancer models [¹¹]. In combination with chemotherapy (e.g., dacarbazine), it has increased progression-free survival without added toxicity [¹²][¹³]. Modified long-acting versions are also showing enhanced anticancer effects in breast cancer models [¹⁴][¹⁵].
Cancers being studied in connection with thymosin alpha-1:
Breast cancer
Melanoma
Liver cancer
Lung cancer
Colon cancer
Thymosin alpha-1 reduces inflammatory pain by inhibiting cytokine production (e.g., TNF-α, IL-1β) at the site of inflammation. This mechanism differs from traditional NSAIDs and may offer fewer side effects [¹⁶].
In cystic fibrosis (CF), thymosin alpha-1 reduces inflammation and may restore function to the defective CFTR protein. It is under investigation as a promising single-molecule therapy for CF [¹⁷].
In cases of avulsed (knocked-out) front teeth, thymosin alpha-1 improves gum healing and increases the survival of replanted teeth. This makes it a promising adjunct in traumatic dental injury treatment [¹⁸].
The potential applications of Thymosin Alpha-1 are too numerous to list in a single summary. What stands out, however, is that the peptide is already in medical use in several countries. Researchers are actively exploring ways to enhance its efficacy and improve production methods to make it faster and more cost-effective [¹⁹]. Given its promising immune-modulating effects and low side effect profile, clinical trials for new Thymosin Alpha-1 variants are expected to expand in the coming years across indications ranging from cancer to infectious disease.
Thymosin Alpha-1 exhibits minimal side effects, low oral, and excellent subcutaneous bioavailability in mice.
Note: Per kg dosages in mice do not translate to humans.
Thymosin Alpha-1 sold at Ai-Peptides is strictly for educational and scientific research purposes only. It is not for human consumption.
Only licensed researchers are authorized to purchase this compound.
The above literature was researched, edited, and organized by Dr. Logan, M.D.
Dr. Logan holds a doctorate from Case Western Reserve University School of Medicine and a B.S. in Molecular Biology.
Allan L. Goldstein, MD is the Professor and Catharine B. & William McCormick Chair of the Department of Biochemistry and Molecular Biology at The George Washington University School of Medicine and Health Sciences, where he has served since 1978.
Thymosins were first discovered in the mid-1960s when Dr. Goldstein, working in the laboratory of Abraham White at the Albert Einstein College of Medicine in New York, studied the role of the thymus in the development of the vertebrate immune system. He is widely regarded as a leading expert on the thymus gland and the immune system and is one of the co-discoverers of the thymosins.
Dr. Goldstein has authored over 400 scientific publications, holds more than 15 U.S. patents, and has edited multiple books in the fields of biochemistry, immunology, neurobiology, and biomedicine. He serves on editorial boards for numerous scientific and medical journals and has consulted for various research organizations in both the private and public sectors. He is also the co-founder of the Institute for Advanced Studies in Aging and Geriatric Medicine, a member of the Board of Trustees for the Albert Sabin Vaccine Institute, and Chairman of the Board of RegeneRx Biopharmaceuticals.
Dr. Goldstein earned his B.S. from Wagner College (1959), and his M.S. and Ph.D. from Rutgers University (1964). He was on the faculty of the Albert Einstein College of Medicine from 1964 to 1972, and later joined the University of Texas Medical Branch in Galveston as Professor and Director of the Division of Biochemistry.
R. King and C. Tuthill, “Immune Modulation with Thymosin Alpha 1 Treatment,” Vitam. Horm., vol. 102, pp. 151–178, 2016.
PubMed
C. Zhang et al., “Gene cloning, expression and immune adjuvant properties of the recombinant fusion peptide Tα1-BLP on avian influenza inactivate virus vaccine,” Microb. Pathog., vol. 120, pp. 147–154, Jul. 2018.
PubMed
F. Pei et al., “Thymosin alpha 1 treatment for patients with sepsis,” Expert Opin. Biol. Ther., vol. 18, no. sup1, pp. 71–76, 2018.
PubMed
G. Wang et al., “Immunopotentiator Thymosin Alpha-1 Promotes Neurogenesis and Cognition in the Developing Mouse via a Systemic Th1 Bias,” Neurosci. Bull., vol. 33, no. 6, pp. 675–684, Dec. 2017.
PubMed
L. Romani et al., “Thymosin α 1 activates dendritic cells for antifungal Th1 resistance through Toll-like receptor signaling,” Blood, vol. 103, no. 11, pp. 4232–4239, Jun. 2004.
PubMed
L. Romani et al., “Thymosin alpha1: an endogenous regulator of inflammation, immunity, and tolerance,” Ann. N. Y. Acad. Sci., vol. 1112, pp. 326–338, Sep. 2007.
PubMed
A. L. Goldstein and A. L. Goldstein, “From lab to bedside: emerging clinical applications of thymosin alpha 1,” Expert Opin. Biol. Ther., vol. 9, no. 5, pp. 593–608, May 2009.
PubMed
C. Matteucci et al., “Thymosin alpha 1 and HIV-1: recent advances and future perspectives,” Future Microbiol., vol. 12, pp. 141–155, 2017.
PubMed
C. Matteucci et al., “Thymosin α 1 potentiates the release by CD8(+) cells of soluble factors able to inhibit HIV-1 and human T lymphotropic virus 1 infection in vitro,” Expert Opin. Biol. Ther., vol. 15 Suppl 1, pp. S83–100, 2015.
PubMed
J. Kharazmi-Khorassani et al., “Antioxidant and angiotensin-converting enzyme (ACE) inhibitory activity of thymosin alpha-1 (Thα1) peptide,” Bioorganic Chem., vol. 87, pp. 743–752, Jun. 2019.
PubMed
J. Kharazmi-Khorassani and A. Asoodeh, “Thymosin alpha-1; a natural peptide inhibits cellular proliferation, cell migration, the level of reactive oxygen species and promotes the activity of antioxidant enzymes in human lung epithelial adenocarcinoma cell line (A549),” Environ. Toxicol., May 2019.
PubMed
M. Maio et al., “Large randomized study of thymosin alpha 1, interferon alfa, or both in combination with dacarbazine in patients with metastatic melanoma,” J. Clin. Oncol., vol. 28, no. 10, pp. 1780–1787, Apr. 2010.
PubMed
R. Danielli et al., “Thymosin α1 in melanoma: from the clinical trial setting to the daily practice and beyond,” Ann. N. Y. Acad. Sci., vol. 1270, pp. 8–12, Oct. 2012.
PubMed
X. Shen et al., “Generation of a novel long-acting thymosin alpha1-Fc fusion protein and its efficacy for the inhibition of breast cancer in vivo,” Biomed. Pharmacother., vol. 108, pp. 610–617, Dec. 2018.
PubMed
F. Wang et al., “Thymosin Alpha1-Fc Modulates the Immune System and Down-regulates the Progression of Melanoma and Breast Cancer with a Prolonged Half-life,” Sci. Rep., vol. 8, no. 1, p. 12351, Aug. 2018.
Nature
Y. Xu et al., “Thymosin Alpha-1 Inhibits Complete Freund’s Adjuvant-Induced Pain and Production of Microglia-Mediated Pro-inflammatory Cytokines in Spinal Cord,” Neurosci. Bull., Feb. 2019.
PubMed
L. Romani et al., “Thymosin α1 represents a potential potent single-molecule-based therapy for cystic fibrosis,” Nat. Med., vol. 23, no. 5, pp. 590–600, May 2017.
PubMed
P. F. Day et al., “Interventions for treating traumatised permanent front teeth: avulsed (knocked out) and replanted,” Cochrane Database Syst. Rev., vol. 2, p. CD006542, May 2019.
PubMed
M. Schmidt et al., “Design of a substrate-tailored peptiligase variant for the efficient synthesis of thymosin-α1,” Org. Biomol. Chem., vol. 16, no. 4, pp. 609–618, Jan. 2018.
PubMed
All of our products are manufactured using the Lyophilization (Freeze Drying) process, which ensures that our products remain 100% stable for shipping for up to 3-4 months.
Once the peptides are reconstituted (mixed with bacteriostatic water), they must be stored in the fridge to maintain stability. After reconstitution, the peptides will remain stable for up to 30 days.
Lyophilization is a unique dehydration process, also known as cryodesiccation, where the peptides are frozen and then subjected to low pressure. This causes the water in the peptide vial to sublimate directly from solid to gas, leaving behind a stable, crystalline white structure known as lyophilized peptide. The puffy white powder can be stored at room temperature until you’re ready to reconstitute it with bacteriostatic water.
Once peptides have been received, it is imperative that they are kept cold and away from light. If the peptides will be used immediately, or in the next several days, weeks or months, short-term refrigeration under 4C (39F) is generally acceptable. Lyophilized peptides are usually stable at room temperatures for several weeks or more, so if they will be utilized within weeks or months such storage is typically adequate.
However, for longer term storage (several months to years) it is more preferable to store peptides in a freezer at -80C (-112F). When storing peptides for months or even years, freezing is optimal in order to preserve the peptide’s stability.
For further information on proper storage techniques, click the link below:
Peptide Storage Information
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