What is BPC-157?
The molecular reference for this catalog records the full sequence H-Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val-OH across 15 residues. Three consecutive prolines near the amino terminus give the chain an unusually rigid local conformation, and the absence of cysteine, methionine, and tryptophan means there is no disulfide to scramble and no residue especially prone to oxidation. Net charge is acidic, with two aspartates and one glutamate against a single lysine.
BPC-157 is a partial sequence of a larger protein found in gastric juice and is not itself a naturally isolated peptide. In rodent studies it has been examined across a wide range of injury models involving tendon, muscle, gut mucosa, and vascular tissue, with published work reporting changes in angiogenic markers such as VEGFR2 signalling and in nitric oxide pathway readouts in the animals studied (Sikiric, 2018).
Several things are not settled. No specific receptor has been identified, most of the published record originates from a small number of collaborating groups, and independent replication is limited. Reported stability in acidic conditions is frequently cited but rests on a narrow experimental base.
Reconstitution & handling
The peptide dissolves quickly and completely in sterile or bacteriostatic water, added slowly down the inner wall of the vial with gentle swirling. No co-solvent is required, and the acidic sequence gives good solubility at neutral pH. Concentration is simple division, so 3 mL added to a 10 mg vial yields approximately 3.33 mg per millilitre.
Storage & stability
Sealed lyophilized vials are stored at -20 °C, protected from light and moisture, and warmed to room temperature before the stopper is pierced. Reconstituted solution is refrigerated at 2 to 8 °C, divided into single use aliquots, and protected from repeated freezing and thawing. Because the sequence contains no methionine or cysteine, oxidation is less of a concern here than with many peptides; the practical limits in solution are hydrolysis at the aspartate residues and microbial growth in unpreserved water.
How it's tested
Each lot is analysed by reversed phase HPLC at 214 and 220 nm, with main peak area reported at 99 percent or greater. Mass spectrometry confirms identity against the theoretical average mass of 1419.53 calculated from C62H98N16O22, which matters for a proline rich sequence where incomplete coupling during synthesis is a recognised risk. Net peptide content is quantified separately, and a lot-matched certificate is available on request.