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Compound Profile: BPC-157

BPC-157 is one of the most widely discussed research peptides and one of the least well described. This profile sets out what the molecule is, where it comes from, why it behaves unusually for a peptide of its size, and the areas of preclinical literature in which it appears.

6 min read · Updated 8 October 2026 · Ref. RL-008

Identity

BPC-157 (Body Protection Compound-157) is a synthetic pentadecapeptide with the sequence Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val. Its molecular formula is C62H98N16O22 and its average molecular weight is approximately 1,419.5 g/mol. It is supplied as a white lyophilised powder and is readily soluble in water. The compound is also referred to in the literature as PL 14736 and, in its arginine-salt form, as Pentadecapeptide BPC 157.

Origin

The sequence was identified in the early 1990s by a research group at the University of Zagreb as a fragment of a larger protein present in human gastric juice. Unlike most short peptides it is stable in gastric acid, which was an early point of interest and distinguishes it from the majority of research peptides, which degrade rapidly in acidic or protease-rich environments.

Research classification

BPC-157 is categorised as a cytoprotective or gastroprotective peptide in the literature. It has no known receptor in the classical sense; proposed mechanisms in published work involve the nitric-oxide system, growth-factor receptor expression, and the organisation of the actin cytoskeleton in migrating cells. These remain areas of active investigation rather than settled pharmacology.

Areas of published research

The preclinical literature is extensive and spans several decades. The largest body of work concerns tissue-repair models: tendon, ligament and muscle injury in rodents, and fibroblast migration and outgrowth in cell culture. A second strand concerns the gastrointestinal tract, reflecting the compound's origin, including models of ulceration and inflammatory bowel conditions. Further work examines angiogenesis in chick chorioallantoic membrane and rodent assays, and interactions with the nitric-oxide pathway. The great majority of these studies are in animal or in-vitro systems; controlled human data is very limited, and the compound is not an approved medicine in any jurisdiction.

Analytical characterisation

BPC-157 runs as a single, well-resolved peak on reversed-phase HPLC. Its acid stability simplifies handling during analysis. Identity is confirmed by mass spectrometry against the theoretical mass; the absence of methionine, cysteine or tryptophan means it is comparatively resistant to oxidation. Regent Peptides supplies BPC-157 in 5 mg and 10 mg vials, UK manufactured, with every batch tested by Janoshik Analytical for purity and identity; the certificate is linked to the batch reference on the vial.

Relationship to TB-500

BPC-157 is frequently studied, and sold, alongside TB-500. The two are structurally unrelated: TB-500 is a seven-residue fragment of thymosin beta-4 with an actin-binding motif, while BPC-157 is a gastric-derived pentadecapeptide. The pairing in the literature reflects an interest in whether their proposed mechanisms are complementary in repair models rather than any chemical similarity. We supply both individually and as a combined 20 mg blend.

Educational reference for laboratory work. Regent Peptides products are supplied for in-vitro research use only and are not for human or veterinary use. Nothing on this page is administration guidance.