BPC-157 5 mg / 10 mg

• 99% Purity
• RUO - Not for human or veterinary use.

Overview

BPC-157 (Body Protection Compound-157) is a synthetic peptide composed of 15 amino acids and is studied in research as a fragment associated with larger gastric-derived cytoprotective protein/peptide systems. Within experimental literature, BPC-157 is generally evaluated for mechanistic effects on cellular processes that support barrier integrity, tissue response to injury, and vascular adaptation in controlled models.

Across in vitro assays and animal studies, BPC-157 research commonly focuses on fibroblast-related biology (migration, proliferation, and cytoskeletal organization), endothelial cell signaling relevant to angiogenesis, and broader pathways involving nitric oxide-linked signaling and oxidative stress markers. These studies use defined endpoints such as collagen/ECM deposition metrics, endothelial proliferation assays, and biochemical markers of stress/inflammation to characterize how BPC-157 influences repair-associated pathways at the cellular and tissue level.

Biochemical Characteristics

Source: PubChem CID 108101

Sequence: Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val

Molecular Formula: C₆₂H₉₈N₁₆O₂₂

Molecular Weight: 1419.556 g/mol

BPC-157 is a linear peptide lacking disulfide bonds. Its proline-rich sequence contributes to conformational rigidity and reduced susceptibility to proteolytic degradation, supporting stability in aqueous experimental systems.

Research Applications

BPC-157 is used in cell culture, ex vivo, and animal model research to investigate tissue repair mechanisms and vascular recruitment processes. Typical experimental endpoints include fibroblast proliferation/migration assays, wound-closure or scratch assays, cytoskeletal organization readouts (e.g., F-actin-related staining), and signaling pathway markers associated with cell adhesion and motility (often evaluated via phosphorylation-state changes or protein expression panels in controlled systems).

A major research application involves angiogenesis and vascular adaptation studies. Researchers may quantify endothelial cell proliferation and tube formation in vitro, measure pro-angiogenic receptor signaling (including pathways discussed in the literature around VEGFR2-associated activity), and evaluate collateral vessel development in ischemia or occlusion models. These investigations often pair histologic analysis with functional perfusion or tissue viability readouts to understand vascular recruitment and restoration of blood flow in model organisms.

Additional research use-cases evaluate BPC-157 in models designed to measure oxidative stress and inflammation-linked pathways, using endpoints such as lipid peroxidation markers (e.g., MDA), reactive oxygen species readouts, and nitric oxide-related biomarkers. In pharmacology-oriented studies, BPC-157 has also been explored as a mechanistic probe in models of drug-induced tissue injury, where outcomes include lesion scoring, tissue histopathology, and electrophysiology-related markers (e.g., QTc changes) in controlled preclinical settings. All findings in these domains should be interpreted as preclinical and mechanistic, dependent on model design, application, route, and measured endpoints.

Pathway / Mechanistic Context

Mechanistic investigations indicate that BPC-157 modulates signaling pathways involved in cellular motility and vascular organization. Experimental data suggest interaction with VEGFR2-associated signaling cascades and downstream nitric oxide-related molecular processes.

Additional in vitro findings describe phosphorylation changes in focal adhesion signaling proteins involved in cytoskeletal anchoring and cell migration. These observations support use as a probe for cytoskeletal remodeling pathways in controlled experimental systems.

Preclinical Research Summary

Published preclinical literature documents investigations of BPC-157 across multiple experimental models. In rodent systems, the peptide has been studied in research examining vascular recruitment, gastrointestinal tissue integrity, and connective tissue remodeling under controlled laboratory conditions.

Additional investigations in avian and invertebrate models have explored peptide stability and tissue-level stress responses, contributing to broader understanding of conserved biological signaling mechanisms.

Form & Analytical Testing

BPC-157 is supplied as a lyophilized peptide produced via solid-phase peptide synthesis. Each lot undergoes analytical verification using high-performance liquid chromatography and mass spectrometry to confirm molecular identity and purity. Analytical data are provided to support reproducibility and consistency in laboratory workflows.

References

Sikiric P et al., Curr Pharm Des, 2018;24(18):2002-2030. Kang EA et al., Dig Dis Sci, 2013;58:3310-3317. Seiwerth S et al., Biomedicines, 2018;6(3):75.

• P. Sikiric et al., "Novel Cytoprotective Mediator, Stable Gastric Pentadecapeptide BPC 157. Vascular Recruitment and Gastrointestinal Tract ," Curr. Pharm. Des., 24(18):1990-2001, 2018.
• S. Seiwerth et al., "BPC 157 and Standard Angiogenic Growth Factors. Gastrointestinal Tract , Lessons from Tendon, Ligament, Muscle and Bone ," Curr. Pharm. Des., 24(18):1972-1989, 2018.
• C.-H. Chang et al., "The promoting effect of pentadecapeptide BPC 157 on tendon involves tendon outgrowth, cell survival, and cell migration," J. Appl. Physiol., 110(3):774-780, 2010.
• M.-J. Hsieh et al., "research potential of pro-angiogenic BPC157 is associated with VEGFR2 activation and up-regulation," J. Mol. Med., 95(3):323-333, 2017.
• T. Huang et al., "Body protective compound-157 enhances alkali-burn wound in vivo and promotes proliferation, migration, and angiogenesis in vitro," Drug Des. Devel. Ther., 9:2485-2499, 2015.