
A synergistic blend of BPC-157 and TB-500 — the two most studied repair peptides — combined in a single vial for regenerative research protocols.
| Purity | ≥99% (LC-MS verified) |
| Form | Lyophilized powder, preservative free |
| Storage | Cool and dry; refrigerate after reconstitution |
| Batch | COA available on request |
A synergistic blend of BPC-157 and TB-500 — the two most studied repair peptides — combined in a single vial for regenerative research protocols.
This vial contains BPC-157 and TB-500 combined in a single lyophilized preparation. The two peptides are unrelated in origin and act through different described mechanisms, but are studied together often enough in tissue-repair research that a combined vial removes the need to reconstitute and handle two separate preparations.
BPC-157 is a synthetic fragment of a gastric protein associated in the literature with angiogenic and nitric-oxide signalling. TB-500 reproduces the actin-binding region of thymosin beta-4 and is associated with cell migration. The stated milligram figure is the combined peptide content.
Supplied for laboratory research use only. Not for human consumption.
The rationale for studying the two together is that the mechanisms reported for each are distinct rather than overlapping — vascular signalling in one case, cytoskeletal regulation in the other. Research using both is generally designed to observe whether the combination behaves differently from either alone.
Associated in published work with VEGFR2 upregulation, nitric-oxide synthase modulation, and fibroblast activity in tendon models.
Associated with G-actin sequestration and with migration of endothelial cells, keratinocytes and fibroblasts in culture.
Studies of the individual peptides are far more numerous than studies of the combination. Both components are preclinical-stage research compounds and neither is an approved drug.
Concentration is set by the volume of diluent added. For a 10mg vial, 2mL of bacteriostatic water yields 5mg/mL. Calculate the working concentration your protocol requires rather than following a generic figure.
| State | Temperature | Practical shelf life |
|---|---|---|
| Lyophilized, sealed | −20 °C | 24+ months |
| Lyophilized, sealed | 2–8 °C | ~12 months |
| Lyophilized, sealed | Room temperature | Weeks — transit only |
| Reconstituted, bacteriostatic water | 2–8 °C | ~3–4 weeks |
| Reconstituted, sterile water | 2–8 °C | Same session |
Lyophilized peptide is stable enough to survive shipping at ambient temperature, which is why cold-chain courier service is not required for transit. Long-term storage is a different matter — material intended to be held for months belongs in a freezer.
Protect from light, and avoid repeated freeze-thaw cycles. Each cycle causes measurable degradation, so dividing a reconstituted stock into single-use aliquots before freezing is preferable to thawing and refreezing one vial repeatedly.
Every lot is tested by an independent laboratory using two orthogonal methods. HPLC (high-performance liquid chromatography) establishes purity as a percentage of total peptide content, separating the target compound from truncated sequences and synthesis by-products. LC-MS (liquid chromatography–mass spectrometry) confirms molecular identity by mass.
Both matter. Purity alone is insufficient — a 99% pure sample of the wrong compound is still the wrong compound. Together the two tests establish identity and quality, which is why This blend is released only after both pass.
The certificate of analysis references the lot number printed on your vial label. Request the COA for your lot at [email protected].
Peer-reviewed studies indexed in PubMed. Each links to the abstract and, where a free copy exists, to the full text. We link primary sources rather than summarising them second-hand.
Compounds studied alongside this one, or acting through related pathways.
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