BPC-157 is one of the most extensively studied synthetic peptides in preclinical research. Composed of 15 amino acids (GEPPPGKPADDAGLV), it is a partial sequence derived from human gastric juice — a body protection compound, as its name suggests. Since its synthesis in the early 1990s, it has accumulated a substantial body of in vitro and in vivo research, with studies examining its interactions with a remarkably wide range of biological systems.
For researchers sourcing BPC-157 for laboratory use, understanding the compound’s molecular profile, documented research applications, and quality requirements is essential. This overview covers the current state of BPC-157 research, its technical specifications, and what to look for when selecting a supply source.
BPC-157 (Body Protection Compound 157) is a synthetic pentadecapeptide — a chain of 15 amino acids — first isolated as a fragment of human gastric juice protein. Its molecular formula is C62H98N16O22, with a molecular weight of 1,419.55 g/mol and a CAS number of 137525-51-0.
Unlike many research peptides that are derived from naturally occurring hormones or growth factors, BPC-157 is a synthetic compound with no known natural endogenous form. This makes its study particularly interesting from a pharmacological standpoint: researchers are examining a compound that appears to interact with multiple biological pathways despite having no direct natural analogue.
The compound is supplied as a white lyophilized powder, typically in vials of 5mg or 10mg. It is water-soluble and reconstituted with sterile bacteriostatic water for research applications. Proper storage at -20°C in its lyophilized form maintains compound integrity for extended periods.
| Property | Value |
|---|---|
| Full name | BPC-157 (Body Protection Compound 157) |
| Also known as | Pentadecapeptide BPC-157, PL 14736 |
| Amino acid sequence | GEPPPGKPADDAGLV |
| Molecular formula | C62H98N16O22 |
| Molecular weight | 1,419.55 g/mol |
| CAS number | 137525-51-0 |
| Purity (Official Peptides) | >99% by HPLC |
| Physical form | White lyophilized powder |
| Solubility | Water soluble |
| Storage (lyophilized) | -20°C, protected from light |
| Storage (reconstituted) | 4°C, use within 30 days |
The most extensively documented area of BPC-157 research concerns its interactions with tissue repair mechanisms. Multiple preclinical studies have examined the compound’s effects on tendon, ligament, muscle, and bone repair models.
Research published across several peer-reviewed journals has documented BPC-157’s interactions with growth factor signaling, particularly its apparent influence on VEGF (vascular endothelial growth factor) expression and angiogenesis. In tendon repair models, studies have observed accelerated collagen organization and increased fibroblast activity in BPC-157 treated samples compared to controls.
A 2010 study examining BPC-157’s effects on Achilles tendon healing in rat models observed significant differences in tendon-to-bone healing rates between treated and control groups. Similar findings have been replicated across multiple independent research groups, with studies examining rotator cuff repair, anterior cruciate ligament healing, and general musculoskeletal tissue recovery models.
For researchers investigating tissue repair pathways — particularly those examining the intersection of angiogenesis, growth factor signaling, and extracellular matrix remodeling — BPC-157 represents a well-characterized tool compound with a substantial existing literature base.
BPC-157’s origins in gastric juice protein have made it a natural subject for gastrointestinal research. The compound has been studied in models of gastric ulcer healing, inflammatory bowel disease, and intestinal permeability — with particular interest in its apparent interactions with NO (nitric oxide) synthesis pathways.
Preclinical models examining BPC-157 in the context of GI inflammation have observed interactions with COX-2 expression and prostaglandin synthesis. Its apparent cytoprotective properties in gastric mucosa models have attracted consistent research interest, with studies examining both its direct effects on mucosal tissue and its systemic interactions via the gut-brain axis.
Research groups studying intestinal barrier function have examined BPC-157 in the context of tight junction protein expression, with several studies reporting interactions with ZO-1 and claudin family proteins in treated models.
An increasingly active area of BPC-157 research involves its interactions with the central and peripheral nervous systems. Studies have examined the compound in models of traumatic brain injury, spinal cord injury, and peripheral nerve damage.
Of particular interest to neurological researchers is BPC-157’s apparent interaction with dopaminergic and serotonergic systems. Studies examining its effects in models of dopamine depletion have reported behavioral differences in treated versus control groups, with some research suggesting interactions with dopamine receptor expression.
The compound has also been studied in the context of neuroprotection — specifically in models examining oxidative stress-induced neuronal damage. Its apparent antioxidant interactions and potential influence on neurotrophic factor expression have made it a subject of interest for researchers studying neurodegenerative disease models.
BPC-157’s anti-inflammatory properties have been documented across multiple tissue types and model systems. Research has examined its interactions with NF-κB signaling pathways, cytokine expression profiles, and inflammatory cell recruitment in various model systems.
Studies examining BPC-157 in inflammatory bowel disease models have reported reductions in pro-inflammatory cytokine expression — including TNF-α and IL-6 — in treated groups compared to controls. Similar anti-inflammatory interactions have been observed in joint inflammation models, muscle injury models, and systemic inflammation research.
The precise mechanisms underlying these anti-inflammatory effects remain an active area of investigation. Current research suggests multiple potential pathways including NO system modulation, prostaglandin synthesis inhibition, and direct interaction with inflammatory signaling cascades.
One of the most consistently documented aspects of BPC-157 research is its interaction with growth factor signaling pathways — particularly those involving VEGF, EGF (epidermal growth factor), and various fibroblast growth factors.
Research examining BPC-157’s angiogenic properties has documented its apparent ability to upregulate VEGF expression in multiple tissue types. This interaction with angiogenesis pathways is of particular interest to researchers studying wound healing, ischemic tissue repair, and regenerative biology more broadly.
Studies examining the compound’s effects on fibroblast activity have reported increased collagen synthesis and accelerated extracellular matrix remodeling in treated samples — findings that have been reproduced across multiple independent research groups and have contributed to BPC-157’s reputation as one of the most consistently studied tissue repair compounds in the preclinical literature.
BPC-157 demonstrates notable stability compared to many research peptides — a property that has contributed to its utility as a research tool compound. Studies have examined its resistance to proteolytic degradation in gastric acid environments, which is consistent with its origin as a gastric-derived compound.
For in vitro research applications, BPC-157’s water solubility and stability profile make it relatively straightforward to work with compared to more hydrophobic peptides. Standard reconstitution with sterile bacteriostatic water produces a stable solution suitable for most in vitro applications.
Key considerations for BPC-157 research:
Concentration and dose range in existing literature: Published preclinical studies have used a wide range of concentrations. Researchers designing experiments should review the existing literature carefully to identify concentration ranges relevant to their specific model system.
Storage and handling: Lyophilized BPC-157 should be stored at -20°C and protected from light. Once reconstituted, solutions should be aliquoted to avoid repeated freeze-thaw cycles and stored at 4°C for short-term use.
Purity requirements: Given the sensitivity of many biological assay systems, researchers should source BPC-157 at >99% purity verified by HPLC. Lower-purity preparations may introduce confounding variables — particularly in cell-based assays where impurities can influence cellular responses independently of the target compound.
Third-party verification: Certificate of analysis documentation from independent laboratories provides confidence in both the identity and purity of the supplied compound. Researchers should request and review COA documentation before incorporating any peptide compound into their experimental workflow.
The quality of BPC-157 available in the research supply market varies considerably. For researchers whose work depends on reproducible results, compound purity and batch-to-batch consistency are not optional considerations — they are fundamental to experimental validity.
When evaluating BPC-157 sources, researchers should consider:
HPLC purity verification — The gold standard for peptide purity assessment. Reputable suppliers provide HPLC chromatograms demonstrating purity at or above 99%. Any supplier unable to provide HPLC documentation should be approached with caution.
Independent third-party testing — Manufacturer-provided certificates of analysis carry less evidentiary weight than those produced by independent analytical laboratories. Look for COA documentation from accredited third-party labs, not internal quality control reports.
Mass spectrometry identity confirmation — In addition to HPLC purity, mass spectrometry analysis confirms compound identity — that the supplied material is actually BPC-157 and not a structurally similar compound or degradation product.
Batch documentation — Reputable suppliers maintain batch-specific documentation, allowing researchers to trace the specific production run of their compound and access test results for that exact batch.
US-based supply — For domestic US researchers, sourcing from a US-based supplier eliminates customs delays, cold chain interruptions, and the regulatory uncertainties associated with international peptide imports.
Official Peptides supplies BPC-157 at >99% purity verified by HPLC analysis conducted by independent third-party laboratories. Certificates of analysis are published for every production batch and accessible via the COA viewer on every product page. Both 5mg and 10mg vials are available for research applications.
What is BPC-157 used for in research?
BPC-157 is studied in preclinical models examining tissue repair, wound healing, gastrointestinal function, neurological recovery, and anti-inflammatory mechanisms. It is not approved for human use and is intended strictly for in vitro laboratory research.
What purity should research-grade BPC-157 be?
For most research applications, >99% purity by HPLC is the appropriate standard. Lower purity preparations introduce potential confounding variables — particularly in cell-based assays where impurities can independently influence cellular responses.
How should BPC-157 be stored?
Lyophilized BPC-157 should be stored at -20°C protected from light and moisture. Once reconstituted, solutions should be stored at 4°C and used within 30 days. Avoid repeated freeze-thaw cycles by aliquoting reconstituted solutions.
What is the molecular weight of BPC-157?
BPC-157 has a molecular weight of 1,419.55 g/mol. Its molecular formula is C62H98N16O22 and its CAS number is 137525-51-0.
How does BPC-157 differ from TB-500?
BPC-157 and TB-500 are both tissue repair peptides but have distinct mechanisms and molecular profiles. BPC-157 is a 15-amino acid synthetic peptide derived from gastric juice protein, while TB-500 is a synthetic analogue of Thymosin Beta-4, a 43-amino acid protein involved in actin regulation. The two compounds are frequently co-studied in tissue repair research models. See our BPC-157 vs TB-500 comparison guide for a detailed breakdown.
Is a certificate of analysis available for Official Peptides BPC-157?
Yes. Every batch of BPC-157 supplied by Official Peptides is independently tested by a third-party laboratory. Certificates of analysis are published and accessible via the COA viewer on the BPC-157 product page.
BPC-157 is among the most thoroughly studied synthetic peptides in the preclinical research literature. Its documented interactions with tissue repair mechanisms, growth factor signaling, gastrointestinal biology, and neurological systems have made it a consistently useful tool compound across a wide range of research applications.
For researchers sourcing BPC-157, compound purity and independent verification are the critical quality parameters. Batch-specific COA documentation from accredited third-party laboratories provides the evidentiary foundation that rigorous research requires.
Official Peptides supplies BPC-157 in 5mg and 10mg vials at >99% purity, with independent third-party HPLC verification and published certificates of analysis for every production batch.
→ View BPC-157 product page and COA
This content is authored by Renata Voss, PhD, an independent research contributor specialising in peptide pharmacology and tissue repair biochemistry. All information is provided for research reference purposes only. BPC-157 is not approved for human use and is not intended for diagnostic or therapeutic purposes. For in vitro laboratory research use only.
All content is provided for research reference purposes only. For in vitro laboratory research use only.