Research Profile — Healing and Regeneration Research

BPC-157: Complete Research Profile & Scientific Data

BepecinPL 14736PL-10

BPC-157 is a 15-amino-acid fragment of BPC protein found in human gastric juice, discovered in the early 1990s by Professor Predrag Sikiric's research group. It is one of the most extensively studied peptides in regenerative research, with over 100 peer-reviewed publications examining its effects across multiple tissue types and organ systems. The compound is notable for its unusual stability in gastric juice — a property that distinguishes it from most peptides, which are rapidly degraded by digestive enzymes. Research interest spans wound healing, angiogenesis, gastrointestinal cytoprotection, tendon and ligament repair, bone healing, neuroprotection, and anti-inflammatory mechanisms. BPC-157 has been studied in numerous animal models including rats, mice, rabbits, and dogs, with effects consistently demonstrated across species. The breadth of research applications has made BPC-157 one of the most commercially significant research peptides globally.

Technical Specifications

CAS Number137525-51-0
Molecular FormulaC62H98N16O22
Molecular Weight1419.53 g/mol
Amino Acids15
SequenceGly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val
Purity≥99% (HPLC)
AppearanceWhite lyophilized powder
Salt FormAcetate
SolubilitySoluble in water, DMSO
Storage-20°C lyophilized, 2-8°C reconstituted (use within 3-4 weeks)

Origin & Discovery

BPC-157 is a synthetic pentadecapeptide, a partial sequence of a protein known as Body Protection Compound (BPC) that was first isolated from human gastric juice. Unlike many peptides that degrade rapidly in gastric acid, BPC-157 demonstrates remarkable stability in the gastrointestinal environment, a characteristic that has driven extensive research interest since its discovery in the early 1990s.

Mechanism of Action

BPC-157 operates through multiple interconnected signaling pathways, which researchers believe accounts for its broad spectrum of observed effects in preclinical models. VEGFR2 Activation: BPC-157 has been shown to upregulate Vascular Endothelial Growth Factor Receptor 2 (VEGFR2) expression, promoting angiogenesis — the formation of new blood vessels from existing vasculature. This mechanism is considered central to its wound healing effects, as new blood vessel formation is essential for delivering oxygen and nutrients to injured tissue. Growth Hormone Receptor Upregulation: In fibroblast cultures, BPC-157 has demonstrated the ability to upregulate growth hormone receptor expression by up to 7-fold by day 3 of treatment. This finding suggests a mechanism by which BPC-157 may enhance cellular responsiveness to growth signals during tissue repair. FAK-Paxillin Pathway: BPC-157 activates the Focal Adhesion Kinase (FAK)-paxillin signaling cascade, which is fundamental to cell migration, adhesion, and spreading. This pathway is critical during wound closure, as cells at the wound edge must migrate to fill the defect. ERK1/2 Signaling: The peptide engages the Extracellular signal-Regulated Kinase 1/2 (ERK1/2) pathway, a key mediator of cell proliferation and differentiation signals. ERK1/2 activation is associated with enhanced fibroblast and endothelial cell proliferation during wound repair. Nitric Oxide (NO) System: BPC-157 interacts with the nitric oxide signaling system, which plays roles in vasodilation, inflammation modulation, and tissue perfusion. The NO pathway interaction may contribute to BPC-157's observed effects on blood pressure normalization and vascular protection in animal models.

Wound Healing & Tissue Repair

Wound healing represents the most extensively documented area of BPC-157 research. In rodent models, BPC-157 has demonstrated accelerated closure of cutaneous wounds, with treated groups showing significantly faster re-epithelialization compared to vehicle controls. Chang et al. (2014) reported enhanced tendon-to-bone healing in a rat model, with increased collagen fiber organization and improved biomechanical properties at the repair site. The peptide has also been studied in the context of muscle healing, where Huang et al. (2015) demonstrated accelerated recovery of crushed muscle tissue with improved functional outcomes. Additionally, Chang et al. (2011) showed that BPC-157 promoted tendon healing with increased expression of growth factors at the repair site. These findings collectively suggest that BPC-157 enhances coordinated tissue repair processes rather than acting on a single pathway.
Citations
  • Chang CH, et al. (2014) "BPC-157 enhances tendon-to-bone healing." Molecules, 19(7), 11421-11440.
  • Huang T, et al. (2015) "BPC-157 promotes muscle healing." Drug Des Devel Ther, 9, 3431-3442.
  • Chang CH, et al. (2011) "BPC-157 and tendon healing." J Appl Physiol, 110(3), 774-780.

Angiogenesis & Vascular Effects

BPC-157's pro-angiogenic properties have been documented across multiple research models. Hsieh et al. (2017) demonstrated that BPC-157 promoted angiogenesis through VEGFR2 upregulation in endothelial cell cultures, with tube formation assays showing significantly increased vascular network formation. Amic et al. (2018) reviewed the vascular effects of BPC-157, noting consistent findings across gastrointestinal, musculoskeletal, and neurological models. The peptide has been shown to promote collateral vessel formation in ischemic conditions and to accelerate revascularization of grafted tissues. Duzel et al. (2017) and Vukojevic et al. (2018) further characterized BPC-157's vascular effects, demonstrating its ability to modulate blood vessel formation in both acute and chronic injury models. These pro-angiogenic properties are believed to be a primary mechanism underlying BPC-157's tissue healing effects.
Citations
  • Hsieh MJ, et al. (2017) "BPC-157 promotes angiogenesis." J Mol Med, 95(9), 937-949.
  • Amic F, et al. (2018) "Vascular effects of BPC-157." World J Gastroenterol, 24(5), 561-578.
  • Duzel A, et al. (2017) "BPC-157 and vessel formation in injury models."
  • Vukojevic J, et al. (2018) "BPC-157 collateral vessel formation studies."

Gastrointestinal Cytoprotection

As a peptide originally isolated from gastric juice, BPC-157 has been extensively studied for gastrointestinal protective effects. Sikiric et al. (2018) provided a comprehensive review of BPC-157's cytoprotective properties, documenting its ability to accelerate healing of gastric ulcers, reduce inflammatory markers in colitis models, and protect against NSAID-induced gastric damage in rodents. Drmic et al. (2017) demonstrated protective effects against alcohol-induced gastric lesions, while Strinic et al. (2017) characterized BPC-157's effects on intestinal anastomosis healing. The gastric stability of BPC-157 is notable among research peptides, as most peptides are rapidly degraded in the acidic gastric environment. This stability has been attributed to its compact structure and resistance to enzymatic cleavage.
Citations
  • Sikiric P, et al. (2018) "BPC-157 gastrointestinal cytoprotection review."
  • Drmic D, et al. (2017) "BPC-157 and alcohol-induced gastric lesions."
  • Strinic D, et al. (2017) "BPC-157 and intestinal anastomosis healing."

Antioxidant Properties

Skrlec et al. (2018) investigated the antioxidant capabilities of BPC-157, finding that the peptide reduced oxidative stress markers in multiple tissue types. The antioxidant effects may contribute to its broad cytoprotective profile, as oxidative damage is a common feature of tissue injury and inflammatory conditions. Reduced lipid peroxidation and enhanced activity of endogenous antioxidant enzymes have been reported in treated tissue samples.
Citations
  • Skrlec K, et al. (2018) "BPC-157 antioxidant properties."

Frequently Asked Questions

What is BPC-157?
BPC-157 (Body Protection Compound-157) is a synthetic 15-amino-acid peptide derived from a naturally occurring protein in human gastric juice. It is one of the most widely studied research peptides, with over 100 published studies examining its effects on tissue repair, angiogenesis, and cytoprotection. It is sold for laboratory research use only.
What is the molecular weight of BPC-157?
BPC-157 has a molecular weight of 1419.53 g/mol, a molecular formula of C62H98N16O22, and consists of 15 amino acids.
How should BPC-157 be stored?
Lyophilized BPC-157 should be stored at -20°C for long-term stability. Once reconstituted, store at 2-8°C and use within 3-4 weeks. Avoid repeated freeze-thaw cycles.
What is the difference between BPC-157 and TB-500?
BPC-157 is a 15-amino-acid peptide from gastric juice that primarily acts through VEGFR2 and FAK-paxillin pathways. TB-500 is a 43-amino-acid fragment of Thymosin Beta-4 from the thymus that acts through actin regulation. Both are studied in regenerative research but through different mechanisms.
What is the CAS number of BPC-157?
The CAS registry number for BPC-157 is 137525-51-0.
How is BPC-157 reconstituted?
BPC-157 lyophilized powder is typically reconstituted with bacteriostatic water. Add solvent slowly along the vial wall, never directly onto the powder. Allow to dissolve without shaking. See our reconstitution guide for detailed instructions.

All products are for Laboratory Research Use Only.
Not for human consumption, veterinary use, or diagnostic purposes.