BPC-157 + TB-500, sold as the Wolverine blend, is a single lyophilized vial containing two structurally unrelated repair-model peptides co-lyophilized at a 1:1 mass ratio: the 15-residue gastric pentadecapeptide BPC-157 and the 7-residue acetylated actin-binding fragment of thymosin beta-4 known as TB-500. A 10 mg vial supplies 5 mg of each; a 20 mg vial supplies 10 mg of each. The blend exists because a number of published repair protocols call for both sequences together, and combining them in one vial removes a reconstitution step, a septum puncture and a source of pipetting error.
It also introduces a problem that a single-peptide vial does not have: a 1:1 mass ratio is not a 1:1 molar ratio. This page covers what each component is, how they differ mechanistically, why the ratio arithmetic matters, and how to read a certificate for a two-component product. The Wolverine blend is supplied for laboratory research only.
Wolverine blend at a glance
| Property | BPC-157 | TB-500 |
|---|---|---|
| Sequence | Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val | Ac-Leu-Lys-Lys-Thr-Glu-Thr-Gln |
| Length | 15 residues | 7 residues, N-acetylated |
| Parent molecule | Body protection compound, gastric juice protein | Thymosin beta-4 (43 residues), actin-binding domain |
| CAS number | 137525-51-0 | 885340-08-9 |
| Molecular weight | 1419.55 g/mol | 889.02 g/mol |
| Reported mechanism | Angiogenic and growth-factor signalling; nitric oxide pathway | G-actin sequestration; cell migration and cytoskeletal dynamics |
| Amount in 10 mg vial | 5 mg (approx. 3.52 micromoles) | 5 mg (approx. 5.62 micromoles) |
| Amount in 20 mg vial | 10 mg | 10 mg |
| Purity specification | Each component independently purified to ≥99% by RP-HPLC before blending; COA reports each separately | |
What is in the vial, and why these two
BPC-157 is a 15-residue fragment of a protein isolated from human gastric juice, sometimes called body protection compound. It has no close structural relatives in the peptide catalogue, and its literature is dominated by gastrointestinal, tendon and vascular models in rodents, with reported effects on angiogenesis, growth-factor receptor expression and nitric oxide signalling.
TB-500 is a different animal entirely: a seven-residue, N-terminally acetylated fragment corresponding to the actin-binding motif of thymosin beta-4, the 43-residue protein that is the principal G-actin sequestering molecule in mammalian cells. Its literature centres on cytoskeletal dynamics, cell migration and corneal and cardiac repair models. It is a fragment, not the whole protein, and the distinction is substantive — the full-length 43-residue protein is a separate product with a separate literature.
The two are grouped by convention, not by biology. What they share is the class of model they appear in, not a pathway. That is precisely why researchers combine them: the reasoning in the published repair literature is that vascular and growth-factor endpoints on one side, and cell-migration and cytoskeletal endpoints on the other, address different parts of the same process. Whether the combination produces effects beyond either component alone has not been resolved in published work, and any experiment using the blend should be designed with single-peptide arms if that question is the one being asked.
The ratio arithmetic that matters
The blend is 1:1 by mass. Because BPC-157 weighs 1419.55 g/mol and TB-500 weighs 889.02 g/mol, equal masses are not equal molar quantities. In a 10 mg vial, the 5 mg of BPC-157 is approximately 3.52 micromoles and the 5 mg of TB-500 is approximately 5.62 micromoles — about 60% more TB-500 in molar terms. For work read out in mass units this is irrelevant; for receptor-level or molar-equivalence comparisons it is a material difference that should be stated explicitly in the method rather than assumed away.
This is a general property of blends, not a defect of this one, and it is one of the main reasons researchers sometimes prefer separate vials. Our guide to peptide blends versus single vials works through the trade-off in detail.
How each component is thought to work
BPC-157
Reported mechanisms include upregulation of vascular endothelial growth factor receptor 2 signalling and associated angiogenic responses, interaction with the nitric oxide system, and effects on growth-factor expression in injured tissue. Rodent studies have described accelerated closure and improved tensile properties in tendon and gastrointestinal injury models. The peptide has no established receptor, and much of the mechanistic account is inferred from pathway readouts rather than binding studies.
TB-500
The seven-residue sequence carries the actin-binding motif of thymosin beta-4. G-actin sequestration alters the monomer pool available for filament assembly, which in turn affects cell motility — the mechanism most often cited for migration and repair observations. Whether a short fragment reproduces the behaviour of the intact 43-residue protein is a live question in the literature, discussed in our piece on why a fragment is not the whole protein.
All of this is preclinical. Neither peptide has an approved use, and neither has a substantial controlled human trial record.
Forms and sizes we supply
The Wolverine blend is stocked in 10 mg (5 mg of each component, USD 130) and 20 mg (10 mg of each, USD 230) lyophilized vials. Both components are synthesised and purified independently to at least 99% before being combined and co-lyophilized, so the certificate reports each peptide on its own rather than characterising the mixture as a single entity.
Related preparations include the four-component KLOW blend and the three-component GLOW blend, and the group sits under recovery blends. Single vials of each component remain available for study designs that need independent control of the two concentrations.
Reconstitution and storage in a laboratory context
Reconstitution of a blend is the same calculation as for a single peptide, performed twice. A 10 mg vial reconstituted with 2 mL of bacteriostatic water gives 5 mg/mL total peptide, which is 2.5 mg/mL of BPC-157 and 2.5 mg/mL of TB-500. Drawing 0.1 mL (10 units on a U-100 syringe) removes 500 mcg total — 250 mcg of each. In molar terms that 0.1 mL contains approximately 176 nanomoles of BPC-157 and approximately 281 nanomoles of TB-500. Recording both figures, rather than only the total mass, is what makes a blend experiment reproducible.
Both peptides are readily soluble in aqueous diluent. Add diluent slowly against the vial wall, swirl rather than shake, and inspect for complete dissolution and clarity. Lyophilized vials are stored at −20 °C, protected from light and moisture; reconstituted solution is refrigerated and aliquoted so that a single container is not repeatedly warmed and re-chilled. Method detail is in the reconstitution guide and the storage guide.
Purity, COA and how to read one for a blend
A two-component product needs a certificate that behaves accordingly, and this is where blends are most often misrepresented in the market. The certificate for this blend reports BPC-157 and TB-500 separately: a purity figure, a chromatogram and a mass confirmation for each, matched to the vial lot number. Three checks follow from that.
First, confirm you are reading two sets of data, not one. A single purity figure for a mixture is not a meaningful number, because a chromatogram of a blend legitimately shows two large peaks — a naive purity calculation on such a trace would report roughly 50%. Second, confirm both masses: 1419.55 g/mol for BPC-157 and 889.02 g/mol for TB-500, with the acetyl group on TB-500 accounted for. Third, check that the stated ratio is a specification with a tolerance, not an assumption; the ratio is set at blending, and it is the one attribute a downstream buyer cannot verify by eye. Our COA reading guide covers the underlying methods.
Regulatory status
Neither component is an approved drug in the United States or elsewhere, and the blend is not a dietary supplement or a generally available compounded medication. BPC-157 in particular has been the subject of regulatory attention in the compounding context in recent years. Material supplied here is research use only, for in-vitro and preclinical laboratory investigation by qualified researchers, and is not intended for human or veterinary administration.
Related peptides and further reading
For the mechanistic contrast between the two components, see BPC-157 vs TB-500. For how multi-peptide recovery preparations are composed and where the ratios come from, see our article on how recovery blends are composed.