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BPC-157 + TB-500

BPC-157 + TB-500 represents a co-formulated research preparation combining two well-characterized peptides — Body Protection Compound-157 (CAS 137525-51-0) and Thymosin Beta-4 fragment TB-500 (CAS 775...

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Certificate of Analysis included with every order.

Technical Specifications

Purity≥98%
FormLyophilized powder
Storage-20°C
Molecular Weight1419.53 Da (BPC) / 4963.50 Da (TB)
SequenceBPC-157 5mg + TB-500 5mg per vial
CAS Number137525-51-0 / 77591-33-4

About This Peptide

BPC-157 + TB-500 represents a co-formulated research preparation combining two well-characterized peptides — Body Protection Compound-157 (CAS 137525-51-0) and Thymosin Beta-4 fragment TB-500 (CAS 77591-33-4) — into a single lyophilized vial containing 5 mg of each peptide at ≥98% purity. This combination, supplied under internal code BPC-157 + TB-500, is of particular interest to investigators studying tissue repair signaling and cellular regeneration in preclinical model systems. Each component has an established independent literature base, and the co-formulation allows parallel or synergistic pathway interrogation within a single experimental framework.

BPC-157 is a synthetic pentadecapeptide (molecular weight 1419.53 Da) derived from a conserved sequence region of human gastric juice protein BPC. Its sequence (Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val) confers notable stability under physiological conditions, making it a practical tool in in vitro assays and rodent model studies. BPC-157 has been extensively investigated in gastric mucosal biology, angiogenesis research, and tendon/ligament cell culture models. TB-500, a synthetic analogue of the conserved actin-binding domain of Thymosin Beta-4 (molecular weight 4963.50 Da), is studied for its role in actin sequestration, endothelial cell migration, and inflammatory cytokine modulation. Together, BPC-157 + TB-500 enables researchers to probe complementary but mechanistically distinct regenerative signaling axes within the same experimental design.

Both peptides are supplied as a co-lyophilized powder, formulated for reconstitution in aqueous buffer prior to use. Storage at −20 °C is recommended to maintain structural integrity. The lyophilized format minimizes degradation during shipping and provides researchers with a stable starting material for dose-response studies, cell-based assays, and small-animal preclinical models. BPC-157 + TB-500 is intended exclusively for laboratory research applications. For research use only. Not for human consumption.

Research Applications

≥98% purity. Lyophilized powder. Storage: -20°C. For research purposes only.

Mechanism of Action

BPC-157 exerts its studied effects primarily through modulation of the nitric oxide (NO) signaling axis and interaction with the growth hormone receptor pathway, including upregulation of VEGFR2 (KDR/Flk-1) expression in endothelial cells. Preclinical data indicate that BPC-157 can activate FAK-paxillin and ERK1/2 signaling cascades, facilitating cytoskeletal reorganization relevant to cell migration and proliferation assays. It has also been reported to influence the expression of EGR-1 and other early-response transcription factors in fibroblast and tendon cell cultures, providing molecular entry points for investigators working in connective tissue biology.

TB-500 functions principally as a G-actin sequestering peptide, binding monomeric actin via its LKKTET motif and thereby modulating actin dynamics, lamellipodia formation, and directional cell motility. In endothelial cell models, TB-500 has been linked to upregulation of integrin-linked kinase (ILK) and downstream activation of Akt/PI3K pathways, effects that are studied in the context of neovascularization and wound healing research. When examined alongside BPC-157, the two peptides may offer complementary inputs into overlapping angiogenic and cytoprotective networks — BPC-157 engaging receptor-mediated NO and VEGF pathways while TB-500 modulates cytoskeletal and migratory machinery — making BPC-157 + TB-500 a useful dual-probe tool for dissecting these interconnected signaling hierarchies in controlled in vitro and in vivo settings.

Research Applications

BPC-157 + TB-500 is utilized across a range of preclinical and in vitro research contexts where investigators seek to characterize peptide-mediated effects on regenerative, angiogenic, and cytoprotective signaling. Representative research application areas include:

  • Tendon and ligament cell culture models: Assessment of fibroblast proliferation, collagen synthesis, and extracellular matrix remodeling in response to individual or combined peptide treatment.
  • Angiogenesis and endothelial biology: Tube formation assays, scratch/wound healing assays, and VEGFR2 expression profiling in human umbilical vein endothelial cell (HUVEC) systems.
  • Gastrointestinal mucosal research: Investigation of BPC-157-mediated cytoprotective effects on gastric epithelial cell lines under oxidative or inflammatory stress conditions.
  • Actin dynamics and cell motility studies: Use of TB-500's actin-sequestering properties to dissect lamellipodia formation, focal adhesion kinetics, and directional migration in 2D and 3D culture matrices.
  • Rodent preclinical injury models: Subcutaneous or local administration studies examining histological and biochemical outcomes in standardized soft-tissue or musculoskeletal injury paradigms.
  • Cytokine and inflammatory mediator profiling: Multiplex assay-based characterization of how BPC-157 + TB-500 modulates pro- and anti-inflammatory cytokine secretion in macrophage or co-culture systems.

Storage & Handling Guidelines

Proper storage and handling are essential to maintain peptide integrity and ensure reliable research results. All Pepitiva Biolabs peptides are supplied as lyophilized (freeze-dried) powder, which provides excellent long-term stability when stored correctly. Store lyophilized peptides at -20°C for long-term storage or 2-8°C for short-term use. Once reconstituted, peptide solutions should be stored at 2-8°C and used within the timeframe specified in the product documentation. Always use sterile bacteriostatic water for reconstitution and handle peptides in a clean laboratory environment to prevent contamination. Avoid repeated freeze-thaw cycles, as thermal stress can cause peptide degradation and loss of biological activity.

Quality Control & Certification

This product is manufactured under strict quality control protocols and has been verified through comprehensive analytical testing. Each batch undergoes reverse-phase HPLC analysis for purity determination and electrospray ionization mass spectrometry (ESI-MS) for molecular identity confirmation. A detailed Certificate of Analysis (COA) is available for download, documenting purity percentage, molecular weight verification, appearance, and recommended storage conditions. Pepitiva Biolabs maintains batch-level traceability from synthesis through delivery, ensuring complete transparency and quality assurance for your research.

Frequently Asked Questions

Is this product approved for human use?

No. This product is intended exclusively for in vitro scientific research and laboratory use. It is not approved for human or veterinary use, not intended for diagnostic or therapeutic purposes, and should not be administered to humans or animals under any circumstances.

How do I reconstitute this peptide?

Add sterile bacteriostatic water slowly to the vial, directing the stream against the glass wall rather than directly onto the lyophilized powder. Gently swirl the vial until the powder is fully dissolved — do not shake vigorously. The recommended reconstitution volume depends on your desired concentration. Refer to the product documentation for specific guidance.

Can I get a Certificate of Analysis (COA)?

Yes. A Certificate of Analysis is included with every order and is also available for download from the product page. The COA documents HPLC purity, mass spectrometry identity confirmation, batch number, production date, and storage recommendations.

For research use only. Not for human consumption.

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