What is BPC-157?
BPC-157 is a synthetic peptide belonging to the pentadecapeptide class, meaning it is composed of a single linear chain of 15 amino acid residues. Its documented primary sequence is Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val, and it is catalogued under CAS registry number 137525-51-0. The molecule is a partial sequence corresponding to a fragment of a larger protein originally characterized in gastric juice, and it is produced for research by solid-phase peptide synthesis rather than extraction.
Structurally, BPC-157 carries the molecular formula C62H98N16O22 and an average molecular weight of 1419.55 g/mol. The sequence is notable for its proline-rich core (three consecutive proline residues) and multiple acidic residues (one glutamate and two aspartate residues), features that contribute to the peptide's conformational rigidity and aqueous handling characteristics. It is an unmodified linear peptide with free N- and C-termini as represented by the listed sequence, and contains no cysteine residues and therefore no disulfide bridging.
Within the scientific literature, BPC-157 is a peptide frequently examined in in-vitro and preclinical tissue-repair and gastrointestinal research models. American Peptides supplies this material strictly as a reference standard and research reagent for laboratory investigation. It is not a drug, dietary supplement, or article intended for human or veterinary use, and this monograph is limited to describing the chemistry, physical properties, and analytical profile of the material.
Reconstitution & handling
BPC-157 is provided as a lyophilized (freeze-dried) powder and is soluble in aqueous buffers. For laboratory reconstitution, the peptide is typically dissolved in sterile water or bacteriostatic water; the acidic and proline-rich residues of the sequence make it readily miscible in neutral aqueous media, though a small fraction of research protocols employ dilute acetic acid or an appropriate buffer to aid initial dissolution of the lyophilate. Solvent should be added slowly down the wall of the vial and allowed to solubilize by gentle swirling rather than vigorous vortexing or shaking, which can introduce shear stress and foaming that promote peptide aggregation.
Once diluent contacts the powder, the solution should be permitted to stand until fully clarified before any downstream handling. Reconstitution volume is selected by the researcher to achieve the desired working concentration for their assay. Because reconstituted peptide is far less stable than the dry solid, only the quantity required for near-term experimental use should be brought into solution, and preparation is best performed under clean, aseptic conditions to preserve integrity.
Storage & stability
In its lyophilized form, BPC-157 is stable for extended periods when stored desiccated and protected from light; short-term storage at 2-8 °C is acceptable, while long-term storage at -20 °C or colder is preferred to minimize degradation. After reconstitution, the peptide should be kept refrigerated at 2-8 °C for near-term use or aliquoted and frozen at -20 °C for longer intervals, with repeated freeze-thaw cycles avoided because they accelerate hydrolysis and aggregation. Aliquoting into single-use portions is the recommended practice to maintain sample integrity across a study.
How it's tested
Identity and purity of BPC-157 are established through orthogonal analytical methods. Reversed-phase high-performance liquid chromatography (RP-HPLC) is used to quantify chromatographic purity, which is confirmed at ≥99% for this material, resolving the target peptide from process-related impurities and truncated sequences. Mass spectrometry (typically ESI-MS or MALDI-TOF) verifies molecular identity by confirming the observed mass against the theoretical molecular weight of 1419.55 g/mol for formula C62H98N16O22. Each lot is accompanied by a Certificate of Analysis (COA) documenting these results, providing lot-specific traceability for reference-standard and research applications.