BPC-157/TB-500 (Wolverine)

This research blend contains two separately characterized peptides. BPC-157 is a synthetic linear pentadecapeptide (GEPPPGKPADDAGLV, about 1,419.5 g/mol) corresponding to a partial sequence of a protein fraction isolated from gastric juice. TB-500 corresponds to thymosin beta-4, a 43-residue polypeptide of about 5 kDa and the most abundant member of the beta-thymosin family in mammalian tissue, where it acts as the main G-actin sequestering peptide. The two components are structurally unrelated: one is a short proline-rich peptide without disulfide bridges, the other a larger actin-binding polypeptide.

BPC-157/TB-500 (Wolverine) in the research literature

Most published studies examine each component on its own. BPC-157 has been examined in rat tendon fibroblast explant and culture systems, where it increased outgrowth, migration and spreading together with FAK and paxillin phosphorylation, and in isolated rat aorta and endothelial cells, where it was linked to nitric oxide generation through Src, caveolin-1 and eNOS. Thymosin beta-4 has been examined in endothelial migration and aortic-ring sprouting assays, in which a seven-residue actin-binding motif reproduced the activity of the full peptide.

A 2026 exploratory study in a rat Achilles tendon transection model included BPC-157, TB-500 and dual-peptide groups; the authors reported no additional histologic or biomechanical effect in the dual-peptide group relative to either peptide alone.