For research use only. This reference describes BPC-157 strictly as a chemical compound used in cell-culture and animal research. Research-grade BPC-157 is not equivalent to, and is not a substitute for, any FDA-approved pharmaceutical product of a similar name. Nothing here is intended for human or animal consumption. We make no health, performance, or therapeutic claims of any kind. For the full context, see our research-use disclaimer.
BPC-157 — also called Body Protection Compound-157, and referenced in the literature as bepecin or by the development code PL-14736 — is a synthetic 15-amino-acid oligopeptide. The molecule is reported to be derived from a fragment of a larger protein found in human gastric juice, and that 15-residue stretch is widely cited as the activity-essential portion. What follows covers the peptide's primary structure, its unusually stable behavior in proteolytic environments, the in-vitro endpoints most often reported across the literature, the two signaling pathways characterized in endothelial cell models, and where the regulatory record sits today for researchers ordering material for laboratory work.
Primary structure and physicochemical identifiers
For a peptide that has accumulated this much in-vitro literature, BPC-157's structural identity is unusually well-defined. PubChem (CID 9941957) and the encyclopedia entry for the compound both list the primary sequence as Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val. You'll see the same sequence in supplier certificates of analysis and in the methods sections of the cell-culture papers cited later in this article.
Molecular formula and mass
The molecular formula is C62H98N16O22, with a calculated mass of approximately 1,419 Da. PubChem also provides a canonical SMILES string, an InChI, and an InChIKey — the identifiers chemical-supply databases use to disambiguate this pentadecapeptide from unrelated compounds whose acronyms also start with "BPC". When ordering reference material, the InChIKey is the cleanest single identifier to verify on a certificate of analysis.
Origin and naming
The 15-residue fragment is described in the foundational reviews as derived from a larger native protein in human gastric juice. The synthetic version prepared for laboratory work is chemically identical to that fragment as characterized — the same primary sequence, not a structural analog. One thing worth flagging: BPC-157 shares its name with an investigational drug code (PL-14736), so researchers should treat research-grade material sold for in-vitro use as not equivalent to, and not a substitute for, any FDA-approved pharmaceutical product of a similar name.
Stability profile in proteolytic environments
One practical reason BPC-157 has been adopted across so many in-vitro paradigms is its proteolytic stability. The comprehensive review by Sikiric and colleagues aggregates two decades of work and reports no measurable degradation of the 15-amino-acid fragment after 24 hours of incubation in human gastric juice under standard conditions. The same review describes the peptide as resistant to trypsin, chymotrypsin, and a panel of intracellular cathepsin proteases.
Structural rationale
The structural feature most often credited for that stability is the four proline residues distributed across the sequence. Proline imposes conformational constraints that interfere with the substrate binding many serine and cysteine proteases require, and the reviewers position this as the chemical basis for the molecule's behavior as a "stable gastric pentadecapeptide". For researchers planning timecourse assays — receptor expression studies, scratch-wound migration paradigms, Matrigel tube-formation experiments — that stability translates into predictable peptide concentrations across multi-day incubations without re-spiking the medium.
In-vitro endpoints reported across the literature
Published in-vitro work on BPC-157 clusters around two cell types: vascular endothelial cells and connective-tissue fibroblasts. The endpoints in each are well-defined and reproduced across multiple groups. That reproducibility is what makes the compound useful as a reference reagent in angiogenesis and proliferation assays.