TB-500
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TB-500 is a synthetic peptide that corresponds to the sequence of Thymosin Beta-4, a naturally occurring actin-sequestering protein found in high concentrations in eukaryotic cells. It consists of 43 amino acids. Research focuses on its ability to uphold the cellular cytoskeleton through the regulation of actin polymerization, a process critical for cell motility and migration.
For Research Use Only. Not for human consumption.
$84.00
In stock
In stock
TB-500 possesses the molecular formula C₂₁₂H₃₅₀N₅₆O₇₈S. It is chemically identical to the active region of Thymosin Beta-4 (Tβ4), a major actin-sequestering molecule. The peptide’s primary function in biological systems involves binding to G-actin (monomeric actin) and preventing its polymerization into F-actin filaments. This regulation is essential for maintaining cytoskeletal structure and facilitating cellular changes required for motility.
Scientific studies investigate the role of TB-500 in angiogenesis and tissue differentiation. In laboratory models, the peptide is observed to influence the migration of endothelial cells and keratinocytes. Researchers postulate that this activity is mediated not only by actin interaction but also through the upregulation of specific enzymes such as matrix metalloproteinases (MMPs), which degrade the extracellular matrix to allow for cell movement.
In murine models of cardiac and skeletal muscle injury, TB-500 is utilized to examine mechanisms of inflammation control and fibrosis reduction. Data suggests that the peptide may downregulate inflammatory cytokines and promote the survival of cardiomyocytes under stress conditions. It serves as a vital tool for understanding the molecular pathways of tissue regeneration and cellular defense.
This product is strictly for laboratory and research purposes only. TB-500 is not intended for human use, diagnostic, or therapeutic procedures. It serves as a reagent for scientific study and method development.
References
- Goldstein, A. L., et al. (2005). “Thymosin beta4: actin-sequestering protein moonlights to repair injured tissues.” Trends in Molecular Medicine, 11(9), 421-429.
- Philp, D., et al. (2004). “Thymosin beta4 promotes angiogenesis, wound healing, and hair follicle development.” Mechanisms of Ageing and Development, 125(2), 113-115.
- Sosne, G., et al. (2010). “Thymosin beta 4: a novel corneal wound healing and anti-inflammatory agent.” Clinical Ophthalmology, 4, 597-604.
