Amino Science Labs sells research peptides exclusively to qualified researchers and laboratories for in vitro and laboratory use. Please confirm before continuing.
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Research Peptide
BPC-157 is a 15-amino acid pentadecapeptide derived from a protective gastric protein found in human gastric juice. Research demonstrates BPC-157 accelerates healing across multiple tissue types including tendons, ligaments, muscles, bones, and gastrointestinal tract. Animal studies show the peptide promotes angiogenesis through VEGFR2 activation and enhances tissue regeneration via the FAK-paxillin and nitric oxide signaling pathways. BPC-157 has demonstrated efficacy in repairing transected tendons and ligaments, healing muscle injuries, accelerating bone fracture recovery, and treating gastrointestinal ulcers and inflammatory bowel conditions. The peptide exhibits cytoprotective and anti-inflammatory properties while maintaining stability in gastric juice for over 24 hours.
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99%+ purity
HPLC verified
15AA
SEQUENCE LENGTH
Pentadecapeptide chain
100+
STUDIES
Peer-reviewed since 1991
No LD50
TOXICITY
No lethal dose established in animal models
24-72hrs
ONSET OBSERVED
In gastric lesion models
Gastric
ORIGIN
Derived from human gastric juice protein BPC
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Research
BPC-157 (Body Protection Compound-157) is a synthetic pentadecapeptide: a stable, partial sequence corresponding to a fragment of a protein identified in gastric juice. Its 15-residue chain (Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val) is not found intact in nature, and it is produced synthetically for laboratory work. Within the research literature the compound is often described as a "stable gastric pentadecapeptide," a label that reflects its notable resistance to hydrolysis in aqueous and enzymatic conditions relative to many short peptides. This characterization has made it a frequently cited model compound in mechanistic and gastrointestinal studies.
Interest in BPC-157 as a research material centers on how a small, sequence-defined peptide behaves across a range of in-vitro and preclinical systems. It is used as a reference peptide in assays exploring cellular signaling, angiogenesis-related pathways, and tissue-culture responses. The peptide has no established consumer application, and the body of work surrounding it remains preliminary and ongoing; findings from cell-based and rodent-model studies should not be extrapolated to human or animal outcomes.
Published investigations of BPC-157 are predominantly rodent-model and in-vitro in nature. Reported experimental lines of inquiry include interactions with nitric oxide (NO) system pathways, effects observed in cell-migration and wound-closure scratch assays, and studies examining vascular and connective-tissue endpoints in controlled preclinical settings. Researchers have also used it to probe growth-factor receptor expression, such as VEGFR2 signaling, in cultured endothelial cells.
These references describe experimental laboratory work only. They are not medical claims, are not evidence of safety or efficacy in humans or animals, and should not be interpreted as guidance for any use outside a controlled research environment.
Each research lot is supplied as a lyophilized white powder and characterized before release. Identity and purity are established using orthogonal analytical methods so that the material on the Certificate of Analysis (COA) matches the sequence and mass expected for the pentadecapeptide. This dual-method approach separates purity (how much of the sample is the target peptide) from identity (confirmation that the target is the correct molecule).
The COA accompanying each product is the definitive analytical record for that specific lot. Because purity and mass can vary slightly between synthesis batches, researchers should reference the COA tied to the lot number received rather than generic specifications when documenting experimental inputs. Retaining the COA alongside experimental records supports reproducibility and traceability.
As a lyophilized peptide, BPC-157 is hygroscopic and sensitive to repeated temperature cycling. Standard laboratory practice is to allow sealed vials to equilibrate to room temperature before opening to minimize condensation, and to reconstitute with an appropriate research-grade solvent under aseptic technique. Aliquoting reconstituted stock into single-use portions limits freeze-thaw cycles that can degrade peptide integrity. Detailed temperature and stability windows for lyophilized, reconstituted, and working solutions appear in the storage table on this page.
It ships as a lyophilized (freeze-dried) white powder in a sealed vial, sized by peptide mass (e.g., 5 mg or 10 mg). Lyophilization improves shelf stability for a research peptide and allows the researcher to reconstitute with a solvent of their choice under aseptic conditions when preparing in-vitro experiments.
Purity is measured by reversed-phase HPLC and reported as a percentage of total peak area, while identity is confirmed by mass spectrometry (ESI-MS or MALDI-TOF) against the theoretical mass of the 15-residue sequence. The lot-specific COA documents both values, plus appearance and net peptide content, and is the authoritative analytical record for the exact material you receive.
In the research literature it is described as a stable gastric pentadecapeptide because its 15-amino-acid sequence shows relatively high resistance to hydrolysis in aqueous and enzymatic conditions compared with many short peptides. This stability is one reason it is frequently used as a model peptide in mechanistic and cell-culture studies.
Published work is predominantly in-vitro and rodent-model, spanning cell-migration and wound-closure assays, nitric-oxide-related signaling, and angiogenesis-associated endpoints such as VEGFR2 expression in cultured endothelial cells. This research is preliminary and ongoing, describes laboratory systems only, and does not establish any human or animal outcome.
Allow the sealed vial to reach room temperature before opening to prevent condensation on the hygroscopic powder, reconstitute using aseptic technique with a research-grade solvent, and aliquot the stock to avoid repeated freeze-thaw cycles. Follow the temperature and time windows in the storage table on this page for lyophilized, reconstituted, and working solutions.
This product is sold strictly for in-vitro research and laboratory use only. It is not intended for human or animal consumption, diagnostic purposes, or therapeutic application.
By purchasing this product, you confirm that you are a qualified researcher operating within an appropriate laboratory environment and will use this compound in accordance with all applicable local, state, and federal regulations.
Amino Science Labs assumes no liability for misuse of this product outside of its intended research application.
No. This material is supplied strictly for in-vitro and laboratory research use by qualified researchers. It is not a drug, supplement, or food, is not intended for human or animal consumption or any diagnostic or therapeutic purpose, and nothing on this page constitutes medical advice.
