BPC-157
5mg
A peptide derived from a protective protein found in human gastric juice, studied for its ability to promote new blood vessel formation through VEGFR2 upregula…A peptide derived from a protective protein found in human gastric juice, studied for its ability to promote new blood vessel formation through VEGFR2 upregulation and activate cell migration through the FAK-paxillin pathway. Research has examined its effects across an unusually broad range of tissue types — tendon, muscle, skin, bone, and GI — making it one of the most versatile repair-focused peptides in the research catalogue.
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Certificate of Analysis
Every batch independently verified by third-party laboratories.
Batch #TL-5642336-P
BPC-157 Lab Certificates
All Trident Labs products are independently tested by accredited third-party laboratories. Results are batch-specific and provided for research transparency only. This product is not approved for human use.
The body’s own
vascular builder.
A 15-amino acid peptide derived from a protective protein in human gastric juice. Uniquely stable under physiological conditions, BPC-157 drives new blood vessel formation through VEGFR2 upregulation — restoring vascular supply to damaged tissue while simultaneously activating cell migration, fibroblast repair, and nitric oxide signaling across an unusually broad range of tissue types.
Sikiric et al. Curr Pharm Des 2018 · Chang et al. J Appl Physiol 2011 · Huang et al. Drug Des Devel Ther 2015. All data from peer-reviewed literature. For Research Use Only — Not for Human Consumption.
Manufactured in US
US-formulated & filled
Endotoxin Tested
<0.05 EU/mL verified
Independently Tested
Horizon Analytical · 6-panel COA
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BPC-157 is supplied exclusively for qualified in vitro laboratory research. Not for human administration.
This product is a research-grade synthetic peptide supplied under research use only (RUO) designation. BPC-157 is not approved by the FDA for any therapeutic indication. By purchasing, the buyer represents they are a qualified researcher using this compound solely for lawful in vitro laboratory research. Not a drug, dietary supplement, food, or medical device. For Research Use Only — Not for Human Consumption.
Born in
the stomach.
BPC-157 is derived from a partial sequence of a protective protein found in human gastric juice — a natural compound the stomach produces to protect its own lining from acid and injury. The synthetic version retains the most critical property of its parent: remarkable stability. While virtually all peptides degrade rapidly in physiological environments, BPC-157 resists enzymatic breakdown, making it a uniquely durable research tool across tissue types far beyond the GI tract.
Molecular Identity
15 AA
Pentadecapeptide
1419 Da
C62H98N16O22
Stable
Enzymatic resistance
6+
Tissue types studied
Primary Sequence
GEPPPGKPADDAGLV
CAS 137525-51-0 · Sikiric et al. Curr Pharm Des 2018
VEGFR2 → angiogenesis.
FAK → cell migration.
eNOS → NO.
BPC-157 engages three parallel signaling pathways simultaneously — vascular remodeling, cellular migration, and nitric oxide modulation. What makes VEGFR2 upregulation mechanistically distinct: BPC-157 increases receptor density at the endothelial surface, amplifying existing VEGF signal rather than adding exogenous growth factor. Lower VEGF concentrations produce higher angiogenic output.
VEGFR2 Upregulation → Angiogenesis
BPC-157 increases VEGFR2 receptor density on vascular endothelial cells — sensitizing them to ambient VEGF concentrations. Downstream: FAK and paxillin phosphorylation drives endothelial migration and lumen formation. Both sprouting angiogenesis (new capillaries) and arteriogenesis (collateral vessel enlargement) documented in ischemic muscle models.
FAK-Paxillin Pathway → Fibroblast Outgrowth
Focal adhesion kinase (FAK) and paxillin are phosphorylated in a dose-dependent manner in BPC-157-treated fibroblasts (Chang et al. J Appl Physiol 2011). F-actin formation is induced. This FAK-paxillin activation enables tendon fibroblasts to migrate toward and survive at injury sites — the mechanistic basis for accelerated tendon and ligament repair in preclinical models.
eNOS Modulation → Nitric Oxide Signaling
BPC-157 modulates endothelial nitric oxide synthase (eNOS) activity via both VEGFR2-Akt-eNOS and Src-Caveolin-1-eNOS pathways. NO is a critical vasodilator, anti-platelet agent, and tissue perfusion regulator. The dual-pathway NO modulation explains BPC-157's documented effects on vasomotor tone, blood pressure normalization, and maintained thrombocyte function in preclinical models.
JAK-2 → Cytoprotection → Gut Mucosal Repair
The JAK-2 signaling pathway mediates BPC-157's cytoprotective effects in GI tissue — originally described in gastric ulcer models where 60–70% epithelial coverage was achieved within 48 hours vs 20–30% in controls. This is the ancestral activity from which BPC-157 was derived and remains one of its strongest documented research endpoints.
Research Endpoint Areas
Angiogenesis — Tube Formation & Vessel Density
VEGFR2 upregulation quantified by western blot or flow cytometry. Tube formation assay in Matrigel (HUVEC cells). Capillary density histomorphometry in rodent ischemic models. Endothelial cell migration assay (wound scratch or Boyden chamber).
Tendon & Ligament Repair — Fibroblast Models
FAK and paxillin phosphorylation by western blot. F-actin formation by FITC-phalloidin staining. Fibroblast migration via scratch assay. Collagen fibril organization by electron microscopy. Tendon mechanical testing (tensile strength, stiffness) in rodent transection models.
Nitric Oxide & Vascular Tone Modulation
eNOS activity by fluorometric assay. NO production by Griess reagent or DAF-FM diacetate. Src-Caveolin-1-eNOS and VEGFR2-Akt-eNOS pathway characterization by western blot. Blood pressure and vascular reactivity endpoints in rodent models.
Gastrointestinal Cytoprotection & Ulcer Models
Gastric ulcer scoring, epithelial coverage measurement. Mucosal integrity via histology (H&E, Alcian blue). Oxidative stress markers: MDA, NO, ROS. JAK-2 pathway quantification. Colitis models: colon length, inflammatory cytokines (IL-6, TNF-α), myeloperoxidase activity.
One peptide.
Six tissue systems.
BPC-157 has been studied across more tissue types than almost any other research peptide — a consequence of its vascular mechanism. Any tissue that requires blood supply for repair is potentially within scope of VEGFR2-mediated angiogenesis.
Tendon & Ligament
FAK-paxillin activation drives fibroblast migration and organization. Enhanced collagen fibril formation and mechanical strength recovery in rat Achilles and patellar tendon transection models. Fastest and most consistent BPC-157 preclinical endpoint.
Key pathway: FAK-paxillin · collagen fibril organization
Gastrointestinal Tract
Original tissue of discovery. 60–70% epithelial coverage within 48h in gastric ulcer models. JAK-2-mediated cytoprotection. Studied across stomach, duodenum, colon, and anastomosis healing. Colitis model data via inflammatory marker suppression.
Key pathway: JAK-2 · mucosal cytoprotection
Skeletal Muscle
VEGFR2-mediated angiogenesis restores blood flow to ischemic muscle. In ischemic muscle models: vessel density reached 180% of baseline by day 14 vs 21-day recovery in controls. Muscle fiber survival and functional recovery endpoints documented.
Key pathway: VEGFR2 · angiogenesis · ischemia recovery
Skin & Wound Healing
Huang et al. 2015 (Drug Des Devel Ther): enhanced alkali-burn wound healing with increased proliferation, migration, and angiogenesis in vitro. VEGFR2 upregulation measured in treated HUVECs. Re-epithelialization and keratinocyte migration documented.
Key pathway: VEGFR2 · keratinocyte migration · re-epithelialization
Bone & Fracture Repair
Vascular supply is rate-limiting for bone healing. BPC-157's angiogenic mechanism directly addresses periosteal vascularization. Femur fracture models show improved callus formation and bone mineral density recovery. Osteoblast activity and trabecular architecture endpoints.
Key pathway: periosteal angiogenesis · osteoblast support
Brain-Gut Axis & CNS
BPC-157 has been studied in dopaminergic and serotonergic modulation models. Brain-gut axis research documents interactions with monoamine neurotransmitter systems. Neuroprotection endpoints in rodent brain injury models. Unique pathway among tissue repair peptides.
Key pathway: dopaminergic / serotonergic modulation
All data from preclinical research. Independent replication limited — majority of published studies from Sikiric et al. (Zagreb). Research use only.
Full specification.
Molecular and analytical data from peer-reviewed literature and Trident Labs batch records.
Long-term
-20°C
Lyophilized sealed. Stable 24 months. Avoid frost-free freezers.
In solution
4°C
Stable 7–14 days. Single-use aliquots recommended.
Solvent
Sterile H2O
Reconstitute in sterile water or acetic acid 0.1%. 0.5–1 mg/mL.
Stability
High
Uniquely resistant to gastric acid and plasma proteases vs most peptides.
For Research Use Only — Not for Human Consumption. BPC-157 is not an approved drug. Supplied exclusively for in vitro laboratory research by qualified researchers. Not a drug, dietary supplement, food, or medical device.
| Common Name | BPC-157 / Body Protection Compound 157 |
| Sequence | GEPPPGKPADDAGLV |
| CAS Number | 137525-51-0 |
| Molecular Formula | C62H98N16O22 |
| Molecular Weight | 1,419.53 Da |
| Structure | 15-AA pentadecapeptide · derived from human gastric juice protective protein |
| Primary Targets | VEGFR2 (angiogenesis) · FAK/paxillin (cell migration) · eNOS (NO) · JAK-2 (cytoprotection) |
| Signaling | VEGFR2-Akt-eNOS · Src-Caveolin-1-eNOS · FAK-paxillin · Egr-1 · PI3K/Akt |
| Stability | Resistant to gastric acid, plasma proteases — uniquely stable among research peptides |
| Origin | Partial sequence of human gastric juice protective protein — Sikiric et al. (Zagreb) |
| Tissue breadth | Tendon · ligament · muscle · GI · bone · skin · cornea · brain-gut axis |
| Form | Lyophilized powder · sealed glass vial |
| Purity | ≥99% HPLC · Mass Spec verified · 6-panel COA · Horizon Analytical |
| Endotoxin | <0.05 EU/mL · LAL-tested · Horizon Analytical |
| Regulatory | RUOIn Vitro Research Use Only — Not for Human Consumption |
Indexed research on BPC-157.
Independent peer-reviewed studies. Not Trident Labs claims. For Research Use Only.
BPC 157 and Standard Angiogenic Growth Factors — VEGFR2, FAK-Paxillin, eNOS
Seiwerth S, Rucman R, Turkovic B, Sever M, et al.
Comprehensive review establishing BPC-157’s angiogenic mechanism. Documents VEGFR2 upregulation, downstream FAK-paxillin phosphorylation for endothelial cell migration, and dual eNOS activation (VEGFR2-Akt-eNOS and Src-Caveolin-1-eNOS pathways) for NO modulation. Reviews tissue healing across tendon, ligament, muscle, and GI in preclinical models. Provides mechanistic framework distinguishing BPC-157 from standard VEGF administration — receptor sensitization vs growth factor addition. Curr Pharm Des 2018;24(18):1972–1989.
BPC-157-Mediated FAK-Paxillin Phosphorylation and Fibroblast Outgrowth in Tendon Injury
Chang CH, Tsai WC, Hsu YH, Pang JH.
Key mechanistic study documenting dose-dependent FAK and paxillin phosphorylation in BPC-157-treated tendon fibroblasts. F-actin formation confirmed by FITC-phalloidin staining. Cell migration significantly enhanced in scratch assay and Boyden chamber. Tendon explant outgrowth dramatically increased compared to controls. Provides the cellular mechanism underlying BPC-157’s tendon healing effects observed in vivo — FAK-paxillin activation as the migration driver. J Appl Physiol 2011;110(2):309–314. PMID: 21071594.
BPC-157 Enhances Wound Healing with Angiogenesis in Alkali-Burn Injury Model
Huang T, Zhang K, Sun L, et al.
Alkali-burn wound healing study demonstrating BPC-157 efficacy both in vivo (rat cornea model) and in vitro (HUVEC cells). In vitro: increased HUVEC proliferation, migration, and tube formation with VEGFR2 upregulation measured by western blot. In vivo: accelerated wound healing with increased neovascularization histomorphometry. First study with direct in vitro VEGFR2 measurement providing mechanistic confirmation of the angiogenic pathway. Drug Des Devel Ther 2015;9:2485–2499. PMID: 25995618.
BPC 157 Therapy: Targeting Angiogenesis and Nitric Oxide — 2025 Systematic Review
Sikiric P, Sever M, et al.
2025 systematic synthesis covering BPC-157’s NO system modulation — both cytotoxic and protective NO functions. Documents VEGFR2-Akt-eNOS and Src-Caveolin-1-eNOS as the dual pathways for vasomotor tone signaling. Reviews vasopressor effects, thrombocyte function maintenance without coagulation interference, and vascular repair across occlusion/ischemia models. Addresses the concentration-dependent duality of NO signaling and how BPC-157 achieves a modulatory rather than unidirectional effect. Pharmaceuticals (Basel) 2025. PMC.
VEGF Upregulation and Enhanced Angiogenesis in Muscle and Tendon Injury Following BPC-157
Brcic L, Staresinic M, Novinscak T, Sikiric P, Seiwerth S.
Documents VEGF upregulation and enhanced angiogenesis in rat muscle and tendon injury models following BPC-157 administration. Enhanced capillary density at repair sites. Notably: no direct pro-angiogenic effect in cell-culture controls alone — effect requires in vivo context, suggesting BPC-157’s angiogenic activity is mediated through tissue-level signaling crosstalk beyond direct VEGFR2 activation. J Physiol Pharmacol 2009;60 Suppl 7:11–20. PMID: 20388944.
Emerging Use of BPC-157 in Orthopaedic Sports Medicine — Systematic Review
Vasireddi A et al.
2025 systematic review (PMC12313605) of BPC-157 in orthopaedic and sports medicine research. Documents concentration of published studies from Sikiric et al. (Zagreb) group, with limited independent replication noted explicitly. Reviews tendon, ligament, bone, and muscle preclinical data. VEGFR2, FAK-paxillin, and NO mechanisms covered. Contextualizes evidence quality and research design limitations. Provides balanced assessment of the current preclinical evidence base for musculoskeletal repair research applications. Orthop J Sports Med 2025. PMC12313605.
Independent peer-reviewed research — not Trident Labs claims. BPC-157 supplied for in vitro research use only. Not for human consumption.
References
Seiwerth S, Rucman R, Turkovic B, et al.
BPC 157 and standard angiogenic growth factors: gastrointestinal tract healing, lessons from tendon, ligament, muscle and bone healing
Chang CH, Tsai WC, Hsu YH, Pang JH.
Pentadecapeptide BPC 157 enhances the growth hormone receptor expression in tendon fibroblasts
Huang T, Zhang K, Sun L, et al.
Body protective compound-157 enhances alkali-burn wound healing in vivo and promotes proliferation, migration, and angiogenesis in vitro
Sikiric P, Sever M, et al.
BPC 157 therapy: targeting angiogenesis and nitric oxide’s cytotoxic and damaging actions
Brcic L, Staresinic M, Novinscak T, Sikiric P, Seiwerth S.
VEGF upregulation and angiogenesis in muscle and tendon injury after BPC-157 treatment
Vasireddi A, et al.
Emerging use of BPC-157 in orthopaedic sports medicine: a systematic review
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