TB-500

TB-500 is a synthetic 43-amino acid peptide representing the active region of Thymosin Beta-4 (Tβ4), a naturally occurring 43-amino acid protein involved in actin polymerization, cell migration, and tissue repair signaling. It is studied in research for its effects on wound healing mechanisms and inflammatory modulation.

TB-500 is a synthetic peptide corresponding to the active region of Thymosin Beta-4, a naturally occurring actin-sequestering protein. It is studied in research for its effects on actin dynamics, cell migration, and tissue repair signaling pathways. Supplied as a lyophilized research peptide.

Thymosin Beta-4 was first isolated from the thymus gland in 1981 by Allan Goldstein's research group. It was subsequently identified as a major actin-sequestering protein in eukaryotic cells. TB-500 represents a synthetic form studied for the same actin-binding and cell migration properties characterized in the native protein.

Published studies demonstrate that TB-500/Tβ4 sequesters G-actin monomers, modulating actin polymerization dynamics and promoting cell migration in wound healing assays. Research has shown upregulation of matrix metalloproteinases, enhanced endothelial cell migration, and modulation of inflammatory cytokine profiles. Animal studies have examined its activity in dermal, cardiac, and neurological tissue repair models.