Disclaimer: Information provided is for research and educational purposes only. TB-500 is not approved by the FDA or any regulatory agency for human or veterinary use.

Introduction: What Is TB-500?

TB-500 (sometimes written as TB500) is a synthetic peptide modeled after a key segment of thymosin beta-4 (Tβ4), a naturally occurring protein found in almost all animal tissues. It has been studied for its role in tissue repair and regeneration, especially in muscle, tendon, ligament, and wound-healing models.¹ ²

Preclinical research demonstrates that TB-500 promotes cell migration, angiogenesis, and tissue repair—making it a unique compound among regenerative peptides².

TB-500 At-a-Glance

• Type: Synthetic peptide fragment (N-terminal region of thymosin beta-4)
  
• Sequence: Ac-SDKP or longer fragments (e.g., LKKTETQ)
  
• Discovered: Late 1990s–early 2000s, building on Tβ4 research from the 1960s–1990s
  
• Key Features: Binds actin, stimulates angiogenesis and cell migration
  
• Primary Research: Animal models of muscle, tendon, ligament, cardiac, and wound healing
  

Chemical Structure & Origin

TB-500’s peptide sequence—typically Ac-SDKP or longer N-terminal fragments—confers its strong actin-binding and cell migration effects. As a synthetic analog, TB-500 is not found naturally but is based on a conserved active region within the Tβ4 peptide.

TB-500 peptide structure and amino acid sequence

How TB-500 Works (in Brief)

TB-500 exerts its effects through pathways shared with thymosin β-4, its parent peptide. It binds to actin, a major cellular structural protein, promoting cell migration, angiogenesis, and tissue remodeling in response to injury.³⁴ By facilitating the movement of repair cells and supporting new blood-vessel growth, TB-500 contributes to accelerated healing in preclinical models.²

Discovery and Key Research Milestones

The history of TB-500 is rooted in the discovery of thymosin beta-4, a 43-amino-acid peptide isolated in the 1960s–1970s from the thymus gland. Scientists later identified a specific sequence—responsible for most of Tβ4’s actin-binding and healing properties—and synthesized it as TB-500 for research use³. Unlike full-length Tβ4, TB-500 is optimized for laboratory synthesis, stability, and cost-effectiveness.

Year	Study & Source	Key Finding
1977	Goldstein AL et al., PNAS (PMID 265536)⁴	Thymosin fractions isolated from thymus
1997	Malinda KM et al., FASEB J (PMID 9194528)²	Tβ4 (and by analogy TB-500) promotes cell migration, angiogenesis
1996/ 1999	Van Troys et al., EMBO J (PMID 8617195)⁵; Safer et al., Biochemistry (PMID 9153421)⁶	Tβ4 actin-binding site mapped; actin-sequestration mechanism clarified
2002	Huff T et al., FEBS Lett (PMID 11978733)⁷	Tβ4 released from platelets and cross-linked to fibrin/collagen; relevance to wound healing
2005	Goldstein AL et al., Trends Mol Med (PMID 16099219)³	Tβ4 “moonlights” as both actin-sequestering and tissue repair peptide.

Conclusion & Key Takeaways

TB-500 is a synthetic peptide fragment designed to harness the regenerative properties of thymosin beta-4. Its ability to stimulate cell migration and new blood vessel formation has made it a popular research tool for studies of muscle, tendon, ligament, and wound healing—especially in animal and veterinary contexts.

FAQs About TB-500

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References

1. Huff T, Müller CS, Otto AM, Netzker R, Hannappel E. β-Thymosins, small acidic peptides with actin-binding properties. FEBS Letters. 2001;528(1-3):27–33. https://www.sciencedirect.com/science/article/abs/pii/S135727250000087X
   
2. Malinda KM, Goldstein AL, Kleinman HK. Thymosin β4 stimulates directional migration of human umbilical vein endothelial cells. FASEB J. 1997;11(7):474–481.https://pubmed.ncbi.nlm.nih.gov/9194528/
   
3. Goldstein AL, Hannappel E, Kleinman HK. Thymosin beta 4: actin-sequestering protein moonlights to repair injured tissues. Trends Mol Med. 2005;11(9):421-429. https://pubmed.ncbi.nlm.nih.gov/16099219/
   
4. Goldstein AL, Guha A, Zatz MM, Hardy MA, White A. Purification and biological activity of thymosin, a hormone of the thymus gland. Proc Natl Acad Sci USA. 1972;69(7):1800–1803. [PMID: 4505666]
   https://pubmed.ncbi.nlm.nih.gov/4505657/
   
5. Safer D, Elzinga M, Nachmias VT. Thymosin β4 and Fx, an actin-sequestering peptide, are indistinguishable. J Biol Chem. 1991;266(7):4029–4032. [PMID: 1995622] https://pubmed.ncbi.nlm.nih.gov/1999398/
   
6. Van Troys M, Vandekerckhove J, Ampe C. Structural modules in actin-binding proteins: towards a new classification. FEBS Lett. 1999;399(1-2):1–7. [PMID: 8617195] https://pubmed.ncbi.nlm.nih.gov/9990286/
   
7. Huff T, Müller CS, Otto AM, Netzker R, Hannappel E. Thymosin β4 is released from human blood platelets and attached to fibrin and collagen. FASEB J. 2002;16(6):691–696. [PMID: 11978733] https://pubmed.ncbi.nlm.nih.gov/11978733/