If you have been reading about gastric juice protein and want a single page that covers the useful parts, this is it: definitions, context, how it is studied, and the questions that come up repeatedly.
Last reviewed on 2026-06-04. Where a claim depends on a specific study, the study is described rather than over-claimed.
Standard practice for the solid form is storage at minus twenty degrees Celsius or colder, kept dry and away from light. Containers are usually sealed with a desiccant to limit moisture uptake. Reconstituted solutions are typically held at two to eight degrees Celsius and used within a short window, because potency can decline over days to weeks depending on the buffer and concentration. Freezing an already dissolved sample may help, though repeated thawing is discouraged. Specific shelf-life claims vary between suppliers and are rarely supported by published stability studies.
Identity and purity are usually assessed by reversed-phase high-performance liquid chromatography with ultraviolet detection near 214 nanometers, a wavelength that captures the peptide backbone. The main peak area is reported as a percentage of total peak area, which serves as a conventional purity figure. Mass spectrometry provides an independent check on molecular mass and helps confirm the expected sequence. Additional tests may include amino acid analysis and water content determination. Results are only comparable when the same column, gradient, and detection settings are used.
BPC-157 is a synthetic pentadecapeptide whose sequence is commonly given as Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val. It is described in the literature as a fragment of a larger protein found in human gastric juice, referred to as body protection compound. The peptide was first characterized in the early 1990s by a research group in Zagreb, Croatia. Its molecular formula is C62H98N16O22 and its monoisotopic mass is approximately 1419 daltons.
Supplied material is typically a lyophilized white to off-white powder. The peptide is freely soluble in water and in common aqueous buffers, which allows it to be handled as a stock solution. Because the sequence contains no cysteine, disulfide cross-linking is not a route of degradation. The absence of aromatic residues means ultraviolet absorbance at 280 nm is minimal, so quantification usually relies on peptide bond absorbance near 214 nm or on amino acid analysis.
Common synonyms in catalogs include pentadecapeptide BPC 157, BPC157, and the full sequence name. A CAS registry number in the 137525-51-0 range is frequently listed, though the assignment should be verified against the supplier certificate of analysis. The name itself is not a pharmacopoeial designation, and there is no standardized international nonproprietary name. Distinguishing genuine material from related fragments generally requires mass spectrometry, since several truncated sequences share similar chromatographic behavior.
| Property | Value | Notes |
|---|---|---|
| Lyophilized powder storage | -20 C or colder, desiccated, protected from light | Long-term condition cited in supplier documentation |
| Reconstituted solution storage | 2-8 C for short-term use | Stability decreases after dissolution |
| Appearance | White to off-white lyophilized powder | Used as a visual identity check |
| Solubility | Soluble in water and aqueous buffers | Limited solubility in nonpolar organic solvents |
| Typical analytical method | Reversed-phase HPLC with UV detection at 214 nm | Purity estimate; mass spectrometry confirms molecular mass |
The peptide was first described in the early 1990s by a group studying gastric secretions and tissue repair. Its fifteen-residue chain is usually written as GEPPPGKPADDAGLV in single-letter code. The free peptide has the formula C62H98N16O22 and a theoretical mass near 1419.5 daltons. These identifiers are established chemical facts that can be checked against standard peptide databases. There is no ambiguity about the primary structure.
Most published findings come from rodent experiments using induced injury or surgical models. Human reports remain scarce and are largely observational, which limits how much can be stated with confidence. Questions about absorption, distribution, metabolism, and clearance in people are still open. Dose translation between species is likewise unresolved. Researchers tend to read the animal literature as a starting point rather than a settled account.
BPC-157 is a synthetic peptide composed of fifteen amino acids. Its sequence corresponds to part of a protein found in human gastric juice, which is the origin of the "body protection compound" label. In laboratory work the material is treated as a defined research chemical rather than a finished product. Published research has centered on animal models, and the peptide is not an approved medicine in most countries.
Quality assessment rests on two separate questions: whether the chain is the intended one, and how much of the sample is that chain. Reverse-phase high-performance liquid chromatography with ultraviolet detection is the standard purity measurement, while mass spectrometry confirms identity through the observed molecular mass. Amino acid analysis and sequence verification provide further checks. A reported purity percentage describes the proportion of the sample represented by the main peak, not the amount of peptide by mass, since counter-ions and water make up part of any lyophilized lot.
In its usual supplied form, the peptide is a white to off-white lyophilized powder that dissolves readily in water and in aqueous buffers. Powder keeps far longer than solution, so material is normally shipped and stored dry, then dissolved only when needed. Once in solution, the chain is subject to hydrolysis and the liquid supports microbial growth, and practical guidance generally treats the dissolved form as short-lived. Containers should stay sealed and desiccated, because the powder takes up moisture from air.
Long-term storage of the dry powder is typically described at minus twenty degrees Celsius or colder, while shorter holding periods may use ordinary refrigeration. Repeated warming and cooling cycles are discouraged because they stress the material and can promote aggregation or loss. Light exposure and residual moisture are both treated as avoidable sources of degradation, and working aliquots are often prepared to limit how many times a container is opened. Sealed vials with a desiccant are the usual container.
=== Debatte um Wirtschaftlichkeit === 2016 stellte die Firma Sanofi Pasteur MSD die Produktion ihres hochwirksamen Kombinations-Antivenins Fav-Afrique zur Behandlung von Patienten nach Bissen der zehn wichtigsten Giftschlangen-Arten der Subsahara-Region ein. Zur Begründung hieß es, die afrikanischen Abnehmer kauften seit 2006 billigere Antivenine anderer Hersteller, etwa aus Indien, deshalb sei die Herstellung nicht mehr wirtschaftlich. Die Weltgesundheitsorganisation verwies jedoch darauf, dass keineswegs alle Konkurrenzprodukte dieselbe Wirksamkeit hätten wie Fav-Afrique. Ursache dafür sind regional unterschiedliche Ernährungsgewohnheiten von Schlangen, so dass selbst das Gift einer einzigen Art unterschiedlich zusammengesetzt sein kann und der Forschungsaufwand zur Herstellung von hocheffektiven Antiveninen dementsprechend hoch ist. Sanofi Pasteur MSD bot daraufhin seine Technologie angeblich anderen Firmen zur Übernahme an. Inzwischen bieten vor allem lateinamerikanische Pharma-Hersteller, darunter eine Firma aus Costa Rica, Kombi-Antivenine zum Selbstkostenpreis an. Im Zusammenhang mit dem Produktionsstopp von Fav-Afrique sprachen Kritiker von einem "Teufelskreis": Viele ärmere Patienten könnten sich die teuren Präparate nicht leisten, die Nachfrage bleibe somit gering und die Pharmaindustrie nehme die Seren wegen ausbleibender Gewinne vom Markt.
=== Empfehlungen zum Einsatz === Man kann davon ausgehen, dass nur bei 50 % der Giftschlangenbisse auch wirklich Gift in die Wunde gelangt, da die Schlangen auch sogenannte „Verteidigungsbisse“ oder „trockene Bisse“ ohne Giftinjektion ausführen. Durch die WHO wird der Einsatz von Antivenin bei Schlangenbissen nur dann empfohlen, wenn sich eindeutige Vergiftungssymptome am gesamten Körper oder schwere Komplikationen an der Bisswunde zeigen.
=== Nebenwirkungen === Da das so produzierte Antiserum aus tierischem Eiweiß besteht, entwickeln die meisten Patienten eine Serumkrankheit (Immunreaktion mit Fieber, Gelenkschmerzen und Hautausschlag). Es drohen außerdem schwere allergische Nebenwirkungen bis hin zum Kreislaufschock; daher werden Antiseren nur in begründeten Fällen und nachgewiesenen schweren Vergiftungen durch möglichst spezialisierte Krankenhäuser eingesetzt.
Sources: de.wikipedia.org
Bjoern M von Reumont u. a.: Modern venomics—Current insights, novel methods, and future perspectives in biological and applied animal venom research. In: GigaScience. Band 11, 18. Mai 2022, S. giac048, doi:10.1093/gigascience/giac048 (englisch). R. David G. Theakston, Damon C. Smith: Antivenoms: A Review of Current Status and Future Developments. In: BioDrugs. Band 7, Nr. 5, Mai 1997, S. 366–375, doi:10.2165/00063030-199707050-00004 (englisch). WHO: Progress in the characterization of venoms and standardization of antivenoms (= WHO Offset Publication. Band 58). World Health Organization, Geneva 1981, ISBN 978-92-4170058-0 (englisch).
Sources: de.wikipedia.org
Reversed-phase HPLC separates the sample into peaks, and the main peak is expressed as a percentage of total peak area. Mass spectrometry is then used to confirm that the molecular mass matches the expected value.
Low temperature and low moisture slow hydrolysis and oxidation, the two main degradation routes for short peptides. A desiccant limits water uptake each time the vial is opened.
No single number captures identity, counter-ion content, water content, or sterility. A purity figure from one laboratory method reflects only what that method detects, and different methods can give different values for the same sample.
It is a synthetic peptide built from fifteen amino acids, with a mass of roughly 1419 daltons. The sequence is reported to match a fragment of a protein present in human gastric juice. It is not a naturally circulating hormone.