A comprehensive overview of BPC-157 peptide structure, mechanism of action, and current research applications in laboratory settings.
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BPC-157, also known as Body Protection Compound-157, is a synthetic peptide consisting of 15 amino acids. It is derived from a protective protein found naturally in human gastric juice. The peptide has garnered significant attention in the research community due to its stability and the range of biological activities observed in preclinical studies.
Unlike many peptides that degrade rapidly in acidic environments, BPC-157 demonstrates remarkable stability across varying pH levels, making it particularly suitable for laboratory investigation. This stability is attributed to its unique amino acid sequence: Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val.
BPC-157 has a molecular weight of approximately 1419.53 g/mol with the molecular formula C62H98N16O22 (CAS Registry Number: 137525-51-0). The peptide is a partial sequence of the larger body protection compound (BPC) found in gastric juice, specifically isolated and synthesized for research applications.
The pentadecapeptide structure contains several notable features:
Research into BPC-157's mechanism of action has identified several pathways of interest. Laboratory studies suggest the peptide may interact with multiple biological systems, though the precise mechanisms continue to be investigated.
Preclinical research indicates BPC-157 may modulate the expression and activity of various growth factors. Studies in animal models have observed interactions with vascular endothelial growth factor (VEGF), fibroblast growth factor (FGF), and hepatocyte growth factor (HGF) pathways.
Laboratory investigations have explored BPC-157's relationship with the nitric oxide (NO) system. Research suggests potential interactions with NO synthase enzymes, which play roles in vascular function and cellular signaling. These interactions remain an active area of scientific inquiry.
In vitro and animal model studies have examined BPC-157's effects on angiogenesis—the formation of new blood vessels. Researchers have observed that the peptide may influence endothelial cell behavior, though the clinical significance of these findings requires further investigation.
BPC-157 is utilized in various laboratory research contexts. Its applications span multiple areas of scientific investigation:
Researchers working with BPC-157 typically employ standard peptide handling protocols, including proper storage conditions, sterile reconstitution techniques, and appropriate controls in experimental design. Some laboratories also investigate BPC-157 alongside compounds involved in cellular energy metabolism, such as those discussed in our NAD+ research overview.
Proper handling of research peptides is essential for maintaining compound integrity and experimental reproducibility. Key considerations for BPC-157 include:
When sourcing BPC-157 for research, quality verification is paramount. Key quality indicators include:
Reputable suppliers provide batch-specific COA documentation and maintain consistent quality control standards across production runs.
BPC-157 research remains primarily in the preclinical phase. The majority of published studies have been conducted using in vitro cell culture systems or animal models, with limited human clinical data available.
Key points regarding the current research landscape:
The scientific community maintains interest in BPC-157 due to the breadth of preclinical observations, though translation to clinical applications would require extensive additional research, safety studies, and regulatory review.
BPC-157 is a synthetic peptide derived from a portion of the human gastric juice protein known as Body Protection Compound. While the parent protein occurs naturally in the gastric mucosa, BPC-157 itself is a stabilized 15-amino-acid fragment produced through laboratory synthesis for research purposes.
BPC-157 is studied through various laboratory methodologies including in vitro cell culture experiments, animal model research, and molecular biology techniques. Researchers examine its interactions with growth factors, angiogenic pathways, and tissue regeneration mechanisms using standardized scientific protocols.
Research grade indicates that a peptide meets the purity and quality standards required for laboratory research applications. This typically means ≥98% purity verified through HPLC analysis, proper lyophilization, and documentation via Certificate of Analysis (COA). Research grade compounds are intended exclusively for scientific investigation, not for human or veterinary use.
BPC-157 has a molecular weight of approximately 1419.53 g/mol (CAS Registry Number: 137525-51-0). Its molecular formula is C62H98N16O22, consisting of 15 amino acids in a specific sequence that gives the peptide its characteristic stability and research properties.
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View Certificate of Analysis Explore Research-Grade PeptidesDisclaimer: This compound is intended for laboratory research use only. It is not approved for human or veterinary use.