TB-500
TB-500 (5mg / 10mg)
Vial Size
Third-Party Tested
Independent lab verified
Batch-Specific CoA
Publicly accessible
YPB.215
Reference number
10mg
Lyophilized vial
Thymosin Beta-4 fragment. Naturally occurring peptide present in virtually all human and animal cells. Studied for tissue repair since the 1990s.
Origin
Thymosin Beta-4 (TB-4) was first isolated from calf thymus by Allan Goldstein and colleagues at the National Institutes of Health in the 1960s. TB-500 refers to a synthetic version of the full 43-amino-acid TB-4 sequence, produced for research applications. The peptide is found in all nucleated cells and is particularly concentrated in blood platelets and wound fluid.
Research Lineage
Research on Thymosin Beta-4 spans over five decades, with early characterization by Goldstein et al. at George Washington University. Subsequent work by Huff, Hannappel, and Sosne has explored its role in cell migration, angiogenesis, and extracellular matrix remodeling. Over 1,000 papers reference Thymosin Beta-4 in the PubMed database.
Mechanism of Action
TB-4 is the principal actin-sequestering molecule in eukaryotic cells, binding to G-actin and regulating cytoskeletal dynamics. In preclinical models, it has been observed to promote endothelial cell migration, hair follicle stem cell activation, and matrix metalloproteinase activity. Research has investigated its involvement in the Wnt signaling pathway and VEGF-mediated angiogenesis.
Structural Notes
43-amino-acid polypeptide. Molecular weight: 4921 Da. N-terminally acetylated. Active domain identified as the central actin-binding motif LKKTET (residues 17-22).
Key References
Goldstein AL et al. Proc Natl Acad Sci USA. 1977;74(2):725-9.
Sosne G et al. Expert Opin Biol Ther. 2007;7(11):1811-8.
Philp D et al. FASEB J. 2004;18(9):1016-8.
Research Use Only. This product is intended for laboratory research purposes only. Not for human or veterinary use. Not for sale to minors.