BPC-157 + TB 500

BPC-157 (Body Protection Compound-157) is a 15-amino acid peptide fragment derived from a naturally occurring gastric protein. Extensively researched for its cytoprotective properties, BPC-157 plays a role in modulating inflammatory cascades, enhancing fibroblast migration, and stimulating angiogenic repair in soft tissue, tendon, and gastrointestinal models. TB-500’s primary research focus stems from its ability to upregulate actin-binding proteins, facilitating cell migration, angiogenesis, and tissue remodeling in experimental settings. It has shown promise in modulating inflammatory cytokines, reducing fibrosis, and accelerating wound healing in non-human models. Together, these peptides are researched for their potential additive effects on muscle, tendon, and ligament recovery, as well as their ability to support endothelial cell differentiation and reduce oxidative or mechanical stress in non-clinical models.

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Description

BPC-157 + TB-500 Blend is strictly investigational. It is not approved for human or veterinary use and is not classified as a dietary supplement, drug, or therapeutic agent by any regulatory body.For research use only. Not for human or veterinary use.

Sequence BPC-157: H-Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val-OH
TB-500: Ac-Ser-Asp-Lys-Pro-Asp-Met-Ala-Glu-Ile-Glu-Lys-Phe-Asp-Lys-Ser-Lys-Leu-Lys-Lys-Thr-Glu-Thr-Glu-Lys-Asp-Lys-OH
Molecular Formula (combined range) C₂₁₁H₃₅₈N₆₆O₁₁₉S₁
Molecular Weight ~5650 Da
PubChem CID  BPC-157: 9941957
TB-500: 16132393
CAS #  BPC-157: 137525-51-0
TB-500: 77591-33-4

The BPC-157 + TB-500 blend represents a synergistic pairing of two extensively studied research peptides known for their distinct yet complementary mechanisms in tissue repair, angiogenesis, and cellular recovery pathways.

BPC-157, a synthetic pentadecapeptide derived from a naturally occurring gastric protein, has been widely investigated for its roles in fibroblast activity, nitric-oxide–mediated vascular support, and modulation of inflammatory cytokines. Its influence on endothelial protection and microvascular stability continues to make it a focus of experimental regenerative biology.

TB-500 (Thymosin β-4 fragment), a naturally occurring actin-binding peptide, is recognized for its ability to promote cell migration, angiogenic signaling, and cytoskeletal stabilization. Research has shown that TB-500’s activity in enhancing cellular motility and differentiation may complement BPC-157’s role in soft tissue healing and repair.

When studied in combination, these peptides have demonstrated synergistic outcomes in experimental wound-healing and tissue-regeneration models, supporting hypotheses of enhanced actin polymerization, fibroblast recruitment, and reduced fibrotic response. Researchers also evaluate this pairing for its potential influence on endothelial cell differentiation, oxidative stress resistance, and recovery from mechanical or ischemic injury.

Laboratory interest continues to grow around the BPC-157 + TB-500 interaction, particularly within models of musculoskeletal injury, epithelial repair, and angiogenic modulation — offering valuable insight into the interconnected pathways of cellular repair and inflammation control.

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