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Every Batch Third-Party Tested
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Research Grade Purity
Research Use Only
Janoshik-Certified
Every Batch Third-Party Tested
Latest COAs Available
Research Grade Purity
Research Use Only
BPC-157 / TB-500 20MG
RM280.00
Two-peptide blend · BPC-157 + TB-500
A synergistic regenerative peptide blend combining BPC-157 and TB-500 for tissue repair research.
In stock — ships from Malaysia
Description
Description
Key Research Findings
- BPC-157 — a large preclinical literature on wound healing, tendon and ligament repair, and gastrointestinal cytoprotection, reviewed in Frontiers in Pharmacology (2021).
- TB-500 / thymosin β4 — cardiac cell migration and repair reported in Nature (2004); accelerated wound healing reported in the Journal of Investigative Dermatology (1999).
- No published study has examined the two peptides administered together. The case for combining them is mechanistic — see below.
Research described here was conducted on the individual peptides, not on this blend. Provided as scientific background only.
Overview
- A single lyophilised vial containing two peptides: BPC-157 (10 mg) and TB-500 (10 mg).
- BPC-157 is a 15-amino-acid sequence derived from a protein found in gastric juice.
- TB-500 is a synthetic fragment of thymosin β4, a naturally occurring protein involved in cell movement and repair.
- Both are studied for tissue repair, but they act through different mechanisms, which is why they are supplied together.
- Supplied for laboratory research only.
How It Works
- BPC-157 — promotes the growth of new blood vessels (via VEGFR-2), influences the nitric oxide system, and activates the FAK–paxillin pathway that helps fibroblasts migrate into damaged tissue.
- TB-500 — binds and sequesters actin, the protein that forms a cell’s internal scaffolding. This makes cells more mobile and helps them travel to a site of injury.
- In short: BPC-157 is associated with building blood supply and connective tissue, TB-500 with moving cells to where they are needed.
- The parent molecule of TB-500, full-length thymosin β4, has been evaluated in human trials (for example ClinicalTrials.gov NCT01311518). TB-500 is a fragment of that molecule, not the same compound.
Mechanistic Hypothesis — Untested
BPC-157 and TB-500 are combined because their mechanisms address different stages of tissue repair. One is associated with establishing blood supply and connective tissue; the other with mobilising cells toward the site of injury. On paper the two do not overlap, which is the basis for supplying them together. The blend is commonly referred to as the “Wolverine Stack”.
This remains a hypothesis. It has not been tested in a published study, and complementary mechanisms do not by themselves demonstrate a combined effect. Commentary discussing the rationale and its limits: The Synergistic Potential of a BPC-157 and TB-500 Peptide Blend: Speculative Roles (commentary, not peer-reviewed).
Research Effects
Lab & Animal Studies
Tissue Repair
Tendon, ligament, muscle and skin repair reported for BPC-157 in animal models.
Lab & Animal Studies
Angiogenesis
Formation of new blood vessels reported for both peptides in preclinical work.
Lab & Animal Studies
Cell Migration
Actin-mediated cell migration and progenitor cell recruitment reported for thymosin β4.
Lab & Animal Studies
Gastrointestinal Protection
Reported for the BPC-157 component in rodent models of gastric and intestinal injury.
Lab & Animal Studies
Wound Closure
Wound contraction and re-epithelialisation reported for thymosin β4.
Mechanistic Hypothesis
Combined Effect
The proposal that the two peptides reinforce one another rests on their pathways being complementary. No study has tested the combination.
Lab & Animal Studies — laboratory or animal studies onlyMechanistic Hypothesis — proposed on mechanism, not tested
Amino Acid Sequences
BPC-157 — Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val15-amino-acid pentadecapeptide derived from a sequence in human gastric juice.TB-500 — synthetic fragment of thymosin β4 (43 amino acids)Includes the actin-binding domain of the parent protein.
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Research use only. Sold strictly for research and laboratory use only. Not for human or animal consumption. Not for diagnostic, therapeutic or clinical use. Citations describe research contexts and do not imply approval for human use.
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