TB-500
Thymosin Beta-4 Fragment
Research Use Only
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TB-500 Overview
TB-500 is a synthetic peptide fragment derived from 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.
TB-500 Structure
CAS #: 77591-33-4
Molecular Formula: C₂₁₂H₃₅₀N₅₆O₇₈S
Molecular Weight: 4963.5 g/mol
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:
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Structural: Collagen, matrix, tendon/ligament
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Vascular: Angiogenesis, nitric oxide, remodeling
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Epithelial: Migration, signaling, matrix
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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.