What Is BPC-157? Identity, Origin and Analysis

What is BPC-157? It is a synthetic 15-residue peptide, GEPPPGKPADDAGLV, with an average molecular mass of about 1419.5 g/mol and CAS number 137525-51-0. A University of Zagreb group first described it in 1993 as a partial sequence of a larger protein they isolated from gastric juice. Of about 230 PubMed records on BPC-157, roughly three in four list the same Zagreb author, most report rat or mouse experiments, and no controlled human study has been published.

BPC-157 at a glance

Source: PubChem CID 9941957 for formula and mass; sequence as given in references 1 and 4; literature counts from a PubMed search run on 21 October 2026 (see the methods note).

Research materials: Vortex supplies BPC-157 as a lyophilised research reagent: BPC-157. Vortex has not published a standalone BPC-157 lab report. A partner-facility report covering the BPC-157 + TB-500 blend is listed at /coa/.

Where the name BPC-157 comes from

BPC stands for “body protection compound”, the name the Zagreb group gave to the parent protein. The number 157 identifies the 15-residue fragment that the group sequenced and later made synthetically. Papers from the originating group often call it “stable gastric pentadecapeptide BPC 157”. Doping-control papers use “BPC 157” or “BPC-157” [1, 2], and a 2026 review uses “body protection compound 157” as a search synonym [4].

The code PL 14736 comes from PLIVA, a Zagreb pharmaceutical company that developed the peptide in the 2000s. Papers that use the code refer to the same sequence. A 2026 review notes that no phase II trial of the peptide has been completed [4].

The name refers to one sequence only. Salt forms and counter-ions, such as acetate or trifluoroacetate left over from purification, can differ between suppliers. They change the gross mass of powder in a vial without changing the peptide. That is why a certificate of analysis reports net peptide content separately from vial fill.

Discovery history of BPC-157

The research line starts with a 1993 paper by Sikiric and colleagues from the Department of Pharmacology at the University of Zagreb (J Physiol Paris, 1993). They described a protein from gastric juice with a relative molecular mass of about 40,000, named it BPC, and reported that a 15-amino-acid fragment had been fully characterised. A 2026 review summarises the same origin: a synthetic pentadecapeptide derived from a fragment of a gastric protein [4].

The material used in research since then is a synthetic peptide. It is not extracted from gastric juice. It is made by standard solid-phase peptide synthesis, the same chemistry used for most research peptides of this length. Stable-isotope-labelled versions, with carbon-13 and nitrogen-15 built into selected residues, have been synthesised for metabolism work in doping-control laboratories [2].

In 2017, the Sports Medicine Research and Testing Laboratory in Salt Lake City identified BPC-157 in confiscated vials, confirmed the sequence GEPPPGKPADDAGLV and published a detection method [1]. It is among the 54 prohibited compounds covered by a 2026 Ghent screening method for blood samples [3].

The shape of the BPC-157 literature

A PubMed search on 21 October 2026 for BPC-157 and its synonyms in titles and abstracts returned 230 records. The counts below come from that search and describe the literature, not any finding in it.

Source: PubMed, searched 21 October 2026. Counts are of indexed records, including reviews and commentaries, and will drift as new papers are indexed.

Three features stand out. First, concentration: one research group accounts for most of the record, so study design and reporting habits are shared across most of the papers. Second, species: the primary research is overwhelmingly rodent pharmacology, with a smaller body of cell-culture work. Third, pace: about 40% of all records appeared in the last six years, many of them reviews rather than new experiments.

Independent work is a small share. It comes mainly from laboratories in Taiwan and China, from anti-doping laboratories in the United States, China and Belgium [1, 2, 3], and from review authors in several countries. A 2026 review counts three small uncontrolled pilot reports in people, with fewer than 30 participants in total, none with a control group [4]. No controlled human study of BPC-157 has been published, and no cell-surface receptor has been identified. One 2026 cell study reported an intracellular binding partner, described in the next section [6].

What cell and molecular studies of BPC-157 have measured

Most BPC-157 papers report whole-animal experiments, and this article does not summarise them. A much smaller set measured what happens in cultured cells, isolated tissue samples or cell-free systems. Their endpoints are molecular or cellular: signalling proteins, protein levels, binding partners and cell behaviour in a dish. The two papers below come from Chang Gung University in Taiwan and from Xi’an, China. Neither is from the Zagreb group.

Endothelial cells and isolated rat aorta: Src, caveolin-1 and eNOS

In a 2020 study, Hsieh and colleagues worked with cultured vascular endothelial cells and with rings of isolated rat aorta [5]. In the endothelial cells, BPC-157 raised intracellular nitric oxide, measured with a fluorescent probe, and increased phosphorylation of three signalling proteins: Src, caveolin-1 and endothelial nitric oxide synthase (eNOS). A Src inhibitor abolished those phosphorylation changes, which places Src upstream in the pathway. Co-immunoprecipitation showed less caveolin-1 bound to eNOS after BPC-157 exposure, and the authors reported that eNOS activation required that release from caveolin-1. They also reported that the nitric oxide generated in these cells was linked to greater endothelial cell migration in vitro.

In the aorta rings, BPC-157 relaxed the tissue in a concentration-dependent way. The relaxation was weaker when the endothelium was removed, and it was blocked by L-NAME, an inhibitor of nitric oxide synthase, or by haemoglobin, which binds nitric oxide. The authors attributed the relaxation to nitric oxide released from the endothelium [5].

Endothelial cells: an intracellular binding partner, FBXO22

A 2026 study by Zhang and colleagues reported a specific intracellular binding partner for BPC-157 [6]. Using protein-interaction and ubiquitination assays, they reported that BPC-157 inside cells binds FBXO22, an adaptor protein for an E3 ubiquitin ligase, and that the proline at position 3 of the peptide is needed for the interaction. The complex reduced ubiquitination and proteasomal breakdown of the transcription factor BACH1, so BACH1 protein accumulated. In cultured vascular endothelial cells, that BACH1 accumulation was linked to higher proliferation and more tube formation, a standard in vitro assay of endothelial network formation.

The proline at position 3 is the first residue of the Pro-Pro-Pro run described in the chemistry section below. The study ties a measured cellular interaction to a specific residue of the sequence.

How to read the cell-level BPC-157 record

• It is small. A handful of papers report molecular endpoints in cells, against well over a hundred rodent pharmacology papers.
• Each finding comes from one laboratory. Neither result above has been reported by an independent group.
• The pathways are not yet connected. eNOS signalling and FBXO22-BACH1 binding were measured by different groups. No paper links them, and no cell-surface receptor has been identified.
• These are laboratory readouts. A change in phosphorylation, protein level or tube formation in a culture dish describes that culture. It is not a measurement of anything outside it.

Chemistry of the BPC-157 sequence

The sequence explains most of the peptide’s analytical behaviour.

• Composition. Four prolines (including the Pro-Pro-Pro run at positions 3 to 5), three glycines, two alanines, two aspartates, one glutamate, one lysine, one leucine and one valine.
• Charge. Three acidic side chains against one lysine give a net charge of about −2 at neutral pH. BPC-157 is an acidic peptide.
• No aromatic residues. There is no tryptophan, tyrosine or phenylalanine, so the peptide absorbs almost nothing at 280 nm. HPLC purity for BPC-157 is measured at the peptide-bond wavelength, around 210 to 220 nm.
• No sulfur. There is no cysteine or methionine, so there are no disulfide bonds to verify and no methionine oxidation to watch for.
• No asparagine or glutamine. The usual deamidation sites are absent.
• Aspartate pair. The adjacent aspartates at positions 10 and 11 are the most chemically reactive part of the chain. Aspartate residues are a common site of acid-catalysed backbone cleavage and of isomerisation in peptides generally.

Proline-rich stretches restrict backbone flexibility, and the Pro-Pro-Pro run gives the N-terminal half of the peptide a fairly rigid shape. No crystal or solution structure of BPC-157 has been published.

Stability of BPC-157 in analytical studies

The originating group has long described BPC-157 as unusually stable in gastric juice, and a 2026 review repeats that description [4]. That claim comes mainly from the originating group’s own work. Formal forced-degradation studies, the standard way to map a peptide’s breakdown under heat, light, acid, base and oxidation, have not been published.

Doping-control laboratories have produced the most independent stability data, all of it in biological matrices rather than in powder:

• In plasma in vitro, BPC-157 formed a stable metabolite, and the intact peptide was stable in urine for at least four days [1].
• Using the isotope-labelled peptide, a Shanghai laboratory found one metabolite from a previously undescribed pathway and eight from ordinary amide-bond cleavage across two incubation systems [2].
• A 2026 Ghent method found BPC-157 stable for at least two months at −20 °C in dried blood spots, serum and plasma. At 4 °C and 22 °C it degraded completely in serum, while it stayed detectable in dried matrices [3].
• In animal pharmacokinetic work summarised by a 2026 review, the plasma half-life of the intact peptide was under 30 minutes in two species [4].

These are analytical findings about how the peptide behaves in a sample tube. They are not storage guidance for research material. For lyophilised powder, general practice is cold, dry and dark storage in a sealed vial. The Vortex product page lists −20 °C away from light for unopened lyophilised powder. Our post on lyophilised peptide storage and stability covers moisture, light and temperature in more detail.

Analytical verification of BPC-157

BPC-157 is a small, well-defined peptide, which makes analytical identity straightforward in principle. Three separate measurements answer three separate questions.

Identity by mass spectrometry

The monoisotopic mass is 1418.70 Da. In electrospray mass spectrometry, the singly protonated ion appears near m/z 1419.71 and the doubly protonated ion near m/z 710.36. Tandem mass spectrometry breaks the peptide at its amide bonds and confirms the order of residues from the fragment ions. Anti-doping laboratories have published validated LC-MS methods for BPC-157 and its metabolites, with detection limits from 0.01 to about 0.1 ng/mL in urine [1, 2].

Purity by HPLC

HPLC purity shows what fraction of the material absorbing at 210 to 220 nm elutes as the main peak. It does not by itself prove that the main peak is the right sequence. A peak that matches a reference standard’s retention time is evidence of identity only as good as that standard.

Net peptide content

Net content reports how much peptide is in the vial, separate from counter-ions, water and other non-peptide mass. For BPC-157 it is the figure to compare with the label amount. Our guide to reading a peptide COA explains each line.

Checking a lot of BPC-157

A report for a BPC-157 lot should show identity, ideally by mass spectrometry with the observed mass, HPLC purity and net content. Vortex has not published a standalone BPC-157 report. The report currently listed at /coa/ is a partner-facility report for the BPC-157 + TB-500 blend.

Source: vortexresearch.net/coa/, accessed 21 October 2026.

The identity line on this report is by HPLC. The summary page does not list a mass-spectrometry result, and the report covers the blend, not standalone BPC-157. Researchers who need lot-specific mass confirmation for a standalone BPC-157 vial should request it or arrange independent testing. Our post on evaluating a research peptide supplier lists the questions worth asking.

Open questions about BPC-157 as a molecule

• Does the peptide have a cell-surface receptor? None has been identified.
• Will the FBXO22 interaction reported in 2026 replicate in another laboratory, and does it relate to the eNOS signalling findings?
• What is its degradation profile under standard forced-degradation conditions, and does the aspartate pair dominate it?
• Does the gastric-juice stability reported by the originating group replicate in independent hands?
• What solution or crystal structure does the proline-rich chain adopt?
• Will a controlled human study ever be published? None exists as of October 2026.

For a related compound that suppliers sell alongside BPC-157, see TB-500 vs thymosin beta-4. For what has been published on the two together, see BPC-157 and TB-500: what research exists on the pair.

Frequently asked questions

What is BPC-157?

BPC-157 is a synthetic 15-residue peptide with the sequence GEPPPGKPADDAGLV, an average molecular mass of about 1419.5 g/mol and CAS number 137525-51-0. It was described in 1993 by a University of Zagreb group as a partial sequence of a larger protein from gastric juice.

What does BPC stand for?

BPC stands for “body protection compound”, the name the originating Zagreb group gave to the parent gastric protein. The number 157 identifies the 15-residue fragment. The same peptide appears in the literature as BPC 157, BPC157, PL 14736 and “stable gastric pentadecapeptide BPC 157”.

Who has published research on BPC-157?

A PubMed search in October 2026 returned about 230 records, and about 76% of them list the originating Zagreb author. Most report rat or mouse experiments. Independent work comes mainly from laboratories in Taiwan and China and from anti-doping laboratories. No controlled human study has been published.

How is BPC-157 identity verified?

Mass spectrometry should show a monoisotopic mass near 1418.70 Da, and tandem mass spectrometry can confirm the sequence. HPLC gives purity but does not prove identity on its own. Vortex currently lists a partner-facility report for the BPC-157 + TB-500 blend at /coa/, with identity listed by HPLC.

What have cell studies of BPC-157 measured?

In cultured endothelial cells, researchers reported higher intracellular nitric oxide and phosphorylation of Src, caveolin-1 and eNOS (2020), and an intracellular binding partner, FBXO22, that stabilises the transcription factor BACH1 (2026). Each finding comes from a single laboratory, and no cell-surface receptor has been identified.

How this article was prepared

Written by the Vortex Research Editorial Team. Identity data come from PubChem and the cited papers. Literature counts come from a PubMed search run on 21 October 2026 for “BPC 157”, “BPC-157”, “BPC157”, “PL 14736” and “pentadecapeptide BPC” in titles and abstracts, with sub-counts by author (Sikiric P), by species terms (rat, rats, mice, mouse) and by publication date. Statements about where independent work comes from are based on the author affiliations in those search results. Every PMID below was checked against PubMed for title, journal and year, and each citation was matched to the sentence it supports. Cell and molecular studies were found by PubMed searches for BPC-157 with cell, endothelial, fibroblast, in vitro and signalling terms, and only papers whose endpoints are measured in cells, isolated tissue samples or cell-free systems are described. Whole-animal findings are not summarised. Product facts come from the live Vortex product and /coa/ pages.

References

1. Cox HD, Miller GD, Eichner D. Detection and in vitro metabolism of the confiscated peptides BPC 157 and MGF R23H. Drug Test Anal. 2017;9(10):1490-1498. PMID: 28035768. doi:10.1002/dta.2152
2. Tian T, Jing J, Li Y, et al. Stable isotope labeling-based nontargeted strategy for characterization of the in vitro metabolic profile of a novel doping BPC-157 in doping control by UHPLC-HRMS. Molecules. 2023;28(21):7345. PMID: 37959764. doi:10.3390/molecules28217345
3. Mazzarino M, Colpaert T, Deventer K, Van Eenoo P. Rapid and harmonized analytical workflow for the determination of peptidic and non-peptidic doping agents in dried and liquid blood matrices. Analyst. 2026;151(15):4398-4413. PMID: 42328738. doi:10.1039/d6an00455e
4. Mateescu DM, Gavrilescu DM, Constantinescu FE, et al. BPC-157 as an investigational peptide therapeutic: biopharmaceutical challenges, formulation strategies, and translational development barriers. Pharmaceutics. 2026;18(5):625. PMID: 42198317. doi:10.3390/pharmaceutics18050625
5. Hsieh MJ, Lee CH, Chueh HY, et al. Modulatory effects of BPC 157 on vasomotor tone and the activation of Src-Caveolin-1-endothelial nitric oxide synthase pathway. Sci Rep. 2020;10(1):17078. PMID: 33051481. doi:10.1038/s41598-020-74022-y
6. Zhang J, Liu M, Ou H, et al. BPC157 drives angiogenesis through FBXO22-dependent stabilization of BACH1. Cell Commun Signal. 2026;24(1):149. PMID: 41606641. doi:10.1186/s12964-026-02694-6

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