BPC-157 10 mg

BPC-157 is a synthetic pentadecapeptide of fifteen amino acid residues with the sequence GEPPPGKPADDAGLV. Its composition is dominated by a proline-rich N-terminal region and a pair of adjacent aspartate residues, and it contains no cysteine and therefore no disulfide bridge. It is produced by solid-phase peptide synthesis and supplied as the free-acid, non-acetylated form unless a lot certificate states otherwise.

No high-affinity receptor for BPC-157 has been established in the peer-reviewed literature, and no dissociation constant against a defined binding site has been reported. In-vitro characterisation is consequently framed around measured endpoints rather than a named target: reported systems include VEGFR2 phosphorylation quantified by immunoblot in cultured endothelial cell lines and nitric oxide synthase enzymatic assays in cell lysates. These are analytical readouts of a defined system and are reported as such.

Primary literature on the synthesis, sequence characterisation and in-vitro analytical chemistry of the pentadecapeptide GEPPPGKPADDAGLV is indexed in PubMed and in peptide chemistry journals. Search results and cited literature do not establish the performance of a commercial lot or a use recommendation.