TB-500
TB-500
Research Use Only
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TB-500 Overview
TB-500 is a synthetic peptide fragment based on thymosin beta-4, a naturally occurring protein studied for its role in molecular signaling and pathway dynamics. Research has focused on its potential influence on matrix remodeling, angiogenesis, and molecular migration in preclinical and laboratory models. TB-500 is of particular interest in investigations involving connective tissue, structural dynamics, and extracellular matrix pathways.
History
Thymosin Beta-4, the parent protein of TB-500, was first isolated in the 1960s by Allan L. Goldstein and colleagues during research into thymus-derived peptides. TB-500 was later synthesized as a research fragment to enable focused study on Tβ4's signaling functions. Since its development, it has been investigated across models of angiogenesis, structural dynamics, and molecular migration, with growing interest in its systemic regulatory potential.
History
Thymosin Beta-4, the parent protein of TB-500, was first isolated in the 1960s by Allan L. Goldstein and colleagues during research into thymus-derived peptides. TB-500 was later synthesized as a research fragment to enable focused study on Tβ4's signaling functions. Since its development, it has been investigated across models of angiogenesis, structural dynamics, and molecular migration, with growing interest in its systemic regulatory potential.
Goldstein A.L., Hannappel E. et al. (2012).
TB-500 Structure
Molecular Formula: C₂₁₂H₃₅₀N₅₆O₇₈S
Molecular Weight: 4963.5 g/mol
CAS: 77591-33-4
PubChem ID: 16132321
Research Findings
TB-500 has been studied in structural, vascular, epithelial, and systemic models, with research exploring its roles in collagen organization, extracellular matrix remodeling, angiogenesis, molecular migration, and pathway activity in preclinical settings.
Key Areas of Research:
- Structural: Collagen, matrix, tendon/ligament
- Vascular: Angiogenesis, nitric oxide, remodeling
- Epithelial: Migration, signaling, matrix
- Systemic: Signaling, viability, pathway dynamics
Together, these findings suggest broad experimental utility for TB-500 across multiple biological pathways. By engaging structural and vascular processes and supporting epithelial and systemic responses, TB-500 provides a versatile platform for investigating molecular remodeling, pathway dynamics, and resilience in laboratory settings.
References
Goldstein, A.L., Hannappel, E., & Kleinman, H.K. (2005). Thymosin β4: actin-sequestering protein moonlights to repair injured tissues. Trends in Molecular Medicine, 11(9), 421–429.
Malinda, K.M., et al. (1999). Thymosin β4 accelerates wound healing. Journal of Investigative Dermatology, 113(3), 364–368.
Philp, D., et al. (2003). Thymosin β4 and a synthetic peptide containing its actin-binding domain promote dermal wound repair in db/db diabetic mice and in aged mice. Wound Repair and Regeneration, 11(1), 19–24.
Bock-Marquette, I., et al. (2004). Thymosin β4 activates integrin-linked kinase and promotes cardiac cell migration, survival and cardiac repair. Nature, 432(7016), 466–472.
Smart, N., et al. (2007). Thymosin β4 induces adult epicardial progenitor mobilization and neovascularization. Nature, 445(7124), 177–182.
Goldstein, A.L., Hannappel, E., Sosne, G., & Kleinman, H.K. (2012). Thymosin β4: a multi-functional regenerative peptide. Expert Opinion on Biological Therapy, 12(1), 37–51.