BPC-157 / TB-500 20mg

Combination research blend of BPC-157 and TB-500. Studied in tissue-repair research applications. Lyophilized powder. Reconstitute with bacteriostatic water for in-vitro research. Store at -20°C. Certificate of Analysis attached to this listing.

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The stack rationale is mechanistic complementarity. BPC-157 and TB-500 both promote tissue repair, but through largely non-overlapping pathways. Pairing them is hypothesized — not proven — to give broader coverage than either alone.

BPC-157 is a 15-amino-acid synthetic peptide derived from a sequence found in human gastric juice. Animal-model evidence consistently shows local effects: angiogenesis at the injury site (VEGF upregulation), growth-factor signaling (EGF, FGF), nitric oxide pathway modulation, and accelerated tendon-to-bone interface healing in rat Achilles transection studies.

TB-500 is a synthetic fragment of Thymosin Beta-4, a 43-amino-acid actin-binding protein. The parent molecule has Phase 2 human data in cardiac and ocular contexts. Mechanistically, it acts systemically: it sequesters G-actin, promotes endothelial cell migration in scratch-wound assays, and has shown progenitor-cell mobilization signals in preclinical cardiac models.

Complementary Mechanism Targets include: - BPC-157: Local tissue repair signaling, VEGF upregulation, nitric oxide pathway modulation, and indirect cell migration via growth factors. - TB-500: Systemic cell migration and mobilization, endothelial migration, and direct cell migration through G-actin sequestering.

Half-life figures are pharmacokinetic estimates from animal studies; no published human PK data exists for either fragment. Synergy is theoretical, as no controlled study has tested whether the BPC-157 + TB-500 combination outperforms either compound alone. The rationale is mechanistic, not empirical. [Source: Peptide Dosing Protocols — wolverine-stack]

COA: View certificate →

Teton Labs product catalog · research-use compound data.