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BPC-157

$104 - $800

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80mg pack · 2 x 40mg vials · $1.30/mg$104
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Buy BPC-157 (40mg vials) from Peptides Partners

Laboratories and academic institutions looking to buy BPC-157 in higher-yield formats can secure high-purity, laboratory-grade compounds directly from Peptides Partners. The 40mg vial presentation provides an extended experimental capacity, specifically formulated for high-throughput screening, multi-plate cellular assays, and repeated-measure research designs. When scaling experimental protocols, sourcing larger mass configurations minimizes lot-to-lot baseline variability across multiple culture batches, ensuring continuity in analytical data collection.

Peptides Partners is dedicated to providing verified research peptides tailored strictly to in vitro and preclinical experimental applications. High-mass presentations like the 40mg vial eliminate the requirement to reconstitute numerous smaller units throughout extensive longitudinal trials. Every batch synthesized for our catalog undergoes strict verification protocols to ensure structural fidelity, exact mass identification, and high analytical integrity, assisting researchers in maintaining verifiable laboratory standards.

Whether your research facility focuses on connective tissue biology, cellular migration kinetics, or microvascular endothelial cell response, our platform provides a reliable, dependable supply chain. By maintaining strict operational controls and specialized peptide synthesis standards, Peptides Partners supports investigators in achieving reproducible, publication-ready research outcomes.

What is BPC-157?

BPC-157, chemically recognized as Body Protection Compound 157, is a synthetic pentadecapeptide composed of 15 amino acids. Its specific primary sequence is Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val. This distinct arrangement yields an approximate molecular weight of 1419.5 Da. The peptide represents a stable partial sequence derived from a naturally occurring, high-molecular-weight protective protein originally isolated from gastric secretions.

Unlike many native regulatory peptides that exhibit rapid enzymatic degradation in biological solutions, BPC-157 displays unique structural stability. Its structural composition includes multiple proline residues, which impart conformational rigidity to the peptide backbone. This architecture confers notable resistance to hydrolytic cleavage and enzymatic breakdown by common proteases in diverse experimental environments, making it a prominent subject of interest within the category of cellular repair peptides.

In analytical biochemistry and pharmacology, BPC-157 is evaluated as a stable synthetic peptide capable of withstanding environmental fluctuations that typically degrade linear oligopeptides. Because it lacks a registered Chemical Abstracts Service (CAS) standard index number, precise identification relies on sequence confirmation, tandem mass spectrometry, and high-performance liquid chromatography. Researchers frequently categorize BPC-157 among signaling peptides that influence tissue remodeling, cellular defense cascades, and intercellular matrix interactions.

Research effects studied

BPC-157 has been studied in preclinical and basic science research for its complex involvement in cellular survival pathways, extracellular matrix modulation, and vascular response mechanisms. Over several decades of laboratory investigation, published literature has highlighted multiple biochemical and cellular pathways:

  • Vascular Endothelial Growth Factor (VEGF) Pathway Activation: Preclinical investigations have observed that BPC-157 influences the expression of VEGF and its associated receptor VEGFR2 in endothelial cell cultures. In vitro tube formation and scratch assays demonstrate that the peptide is associated with enhanced endothelial cell migration, organizing cellular structures into primitive capillary-like networks.
  • Focal Adhesion Kinase (FAK) and Paxillin Signaling: Research into connective tissue cellular models, particularly isolated tendon fibroblasts (tenocytes) and ligament explants, indicates that BPC-157 promotes the phosphorylation of FAK and paxillin. This intracellular phosphorylation cascade is integral to cellular adhesion, cytoskeletal remodeling, and cell motility during mechanical or chemical stress models.
  • Extracellular Matrix (ECM) Synthesis: In fibroblast cultures, exposure to BPC-157 has been correlated with increased transcriptional activity of Type I and Type III collagen genes. Investigators study these dynamics to elucidate the fundamental cellular mechanisms regulating tendon-to-bone and ligament remodeling following mechanical trauma in vitro.
  • Nitric Oxide (NO) System Modulation: Preclinical models investigating cellular homeostasis suggest that BPC-157 acts as a modulator of nitric oxide production. It has been observed interacting with both endothelial nitric oxide synthase (eNOS) and inducible nitric oxide synthase (iNOS), exerting a stabilizing influence on vascular tone and inflammatory signaling in stressed tissue cultures.
  • Epithelial Integrity and Tight Junction Regulation: Studies utilizing intestinal epithelial monolayers (such as Caco-2 cell models) have examined the peptide’s capacity to maintain transepithelial electrical resistance (TEER). Researchers have observed upregulated expression of structural tight junction proteins, including zonula occludens-1 (ZO-1), occludin, and specific claudin isoforms, in response to chemical insults.
  • Cytoprotective Gene Expression: Preclinical studies suggest that BPC-157 influences the expression of early growth response gene 1 (Egr-1), as well as downstream target genes involved in cellular proliferation, cytokine regulation, and cellular survival under hypoxic or oxidative stress conditions.

How to use in the laboratory

Standardized handling and laboratory preparation protocols are critical when working with high-mass 40mg vials of research peptides. Proper reconstitution maintains peptide integrity and ensures consistent working concentrations across scientific assays. Reconstitution must be carried out within a certified biological safety cabinet or laminar flow clean bench using aseptic methodology.

Appropriate laboratory procedures include the following steps:

  • Solvent Selection: Depending on the experimental endpoint, appropriate reconstitution diluents include sterile bacteriostatic water (containing 0.9% benzyl alcohol for multidose laboratory testing), sterile water for injection, or sterile physiological buffers such as phosphate-buffered saline (PBS, pH 7.4). Solvents containing oxidizing agents or extreme pH values should be avoided to prevent deamidation or peptide fragmentation.
  • Equilibration: Remove the lyophilized vial from cold storage and allow it to equilibrate to ambient room temperature (20°C to 25°C) for approximately 20 to 30 minutes before introducing liquid. This prevents condensation from forming within the vial upon opening or puncture, which could alter moisture content and concentration accuracy.
  • Reconstitution Technique: Using a sterile laboratory syringe, slowly introduce the selected diluent down the inner glass wall of the vial. Do not spray diluent directly onto the lyophilized cake. Allow the solvent to passively wet the powder, followed by gentle swirling or rocking of the vial. Never vortex or vigorously shake the solution, as high shear forces can induce mechanical denaturation or aggregation of the peptide chains.
  • Aliquot Strategy: Because 40mg yields a substantial quantity of working material, researchers should calculate target working volumes and aliquot the reconstituted solution into sterile, low-protein-binding microcentrifuge tubes. Aliquoting mitigates the risk of contamination and avoids subjecting the main stock to repeated freeze-thaw cycles.
  • Laboratory Record-Keeping: Accurately document the reconstitution date, the specific diluent used, lot number, total volume, and final calculated concentration (e.g., mg/mL) directly on the vial label and within the institutional laboratory notebook. Every aliquot should be cataloged with an internal tracking ID to preserve procedural traceability.

Pack sizes and price per mg

Peptides Partners provides volume-scaled packaging for the 40mg BPC-157 presentation to assist research teams in optimizing procurement budgets for ongoing, long-term studies. The tiered purchasing options detailed below outline total yields, price structures, and corresponding costs per milligram:

Pack Size Total Milligrams Total Price Price per mg
2 vials x 40mg 80 mg $104 $1.30 / mg
5 vials x 40mg 200 mg $240 $1.20 / mg
10 vials x 40mg 400 mg $440 $1.10 / mg
20 vials x 40mg 800 mg $800 $1.00 / mg

Acquiring larger pack volumes allows laboratories conducting sustained high-throughput experiments to lower their marginal cost per milligram from $1.30 down to $1.00. This unit economy is particularly advantageous for experimental pipelines requiring daily media changes, extensive replication across microtiter plates, or cross-laboratory inter-assay comparisons.

Storage and handling

Maintaining the structural stability of BPC-157 requires adherence to temperature, humidity, and light exposure guidelines throughout the life cycle of the product.

  • Lyophilized Storage: In its dry, lyophilized powder form, BPC-157 demonstrates high baseline stability. For long-term archiving, store vials at -20°C in a manual-defrost freezer. For extended storage exceeding 12 months, deep cryogenic storage at -80°C is recommended. Lyophilized vials may be stored temporarily at refrigerated temperatures (2°C to 8°C) for short durations without significant loss of analytical purity, provided they remain sealed and desiccated.
  • Protection from Moisture and Light: Peptide vials should be kept in secondary containers with desiccant packs to prevent ambient humidity from penetrating the closure system. In addition, store vials away from direct ultraviolet (UV) radiation and intense ambient light, which can catalyze degradation of sensitive peptide residues.
  • Reconstituted Solution Storage: Once dissolved, the liquid peptide should be stored at 2°C to 8°C for immediate experimental use (typically within 7 to 14 days when prepared with bacteriostatic diluents). For storage extending beyond this window, aliquots must be frozen at -20°C or -80°C. Repeated freeze-thaw cycles must be strictly avoided, as the formation of ice crystals can disrupt the physical conformation of the peptide.

Quality and documentation

Every lot of BPC-157 available through Peptides Partners is synthesized following stringent chemical protocols to ensure consistency across laboratory investigations. Ensuring reproducible research outputs requires rigorous quality verification at every stage of the manufacturing process.

Each batch is subjected to comprehensive analytical evaluation, including High-Performance Liquid Chromatography (HPLC) to evaluate chromatographic purity and identify any trace synthesis artifacts. Mass Spectrometry (MS) analysis, utilizing electrospray ionization (ESI) or matrix-assisted laser desorption/ionization (MALDI), is simultaneously performed to verify the exact monoisotopic and average molecular mass of the 15-amino acid sequence against theoretical values.

Laboratories sourcing research peptides from Peptides Partners can request batch-specific Certificates of Analysis (CoA) confirming peptide identity and analytical profiles. Our products are provided strictly for research, development, and laboratory testing purposes, ensuring our research partners receive well-documented, reliable materials for academic and industrial investigations.

Frequently asked questions

What is the molecular weight and sequence of BPC-157?

BPC-157 is a 15-amino acid pentadecapeptide with the designated primary amino acid sequence Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val. It possesses an approximate molecular weight of 1419.5 Da. The peptide’s sequence is verified through mass spectrometry to ensure the molecular mass corresponds to theoretical calculations without structural deviations.

Why choose a 40mg vial configuration over smaller unit sizes?

A 40mg vial is designed specifically for experimental programs that consume larger quantities of peptide over an extended duration, such as high-density cell culture assays, extensive replication trials, or continuous microfluidic perfusion models. Selecting a larger unit size significantly reduces batch-to-batch variation, limits the labor required for multiple reconstitutions, and provides lower procurement costs per milligram for institutional researchers.

What diluents are suitable for reconstituting BPC-157 in laboratory models?

Suitable diluents depend on the requirements of the downstream assay. For repeated sampling over a two-week period, bacteriostatic water containing 0.9% benzyl alcohol is commonly utilized to prevent microbial growth. For immediate application in cell culture media, sterile water for injection (WFI) or sterile physiological buffers such as phosphate-buffered saline (PBS, pH 7.4) are standard, provided the reconstituted solution is used promptly or divided into frozen aliquots.

Is BPC-157 approved for clinical or veterinary therapeutic applications?

No. BPC-157 supplied by Peptides Partners is manufactured and distributed exclusively for research, laboratory, and scientific experimentation. It is not approved by regulatory agencies, including the U.S. Food and Drug Administration (FDA) or the European Medicines Agency (EMA), for clinical use, veterinary treatment, human administration, diagnostic testing, or incorporation into pharmaceutical formulations.

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