🎁 Code: '500freebie' - Spend $500, add an item from Other Peptides, get it for free (exclusions apply)
🚚 Free Shipping when you spend $350 or more
Two of the most extensively studied peptides in this context are BPC-157 and TB-500. Both peptides offer unique properties that have made them the focus of numerous studies, particularly in the fields of tissue healing and regenerative medicine. This article delves into the amino acid structures, cryo-electron microscopy (cryo-EM) studies, mechanisms of action, and research potential of BPC-157 and TB-500, providing a comprehensive comparison for researchers interested in these promising compounds.
BPC-157, also known as Body Protection Compound-157, is a synthetic peptide derived from a naturally occurring protein found in gastric juice. It is a pentadecapeptide, consisting of 15 amino acids with the sequence:
Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val.
The structure of BPC-157 is highly stable, which is essential for its activity in various biological environments. The presence of glycine (Gly) at the N-terminus and valine (Val) at the C-terminus contributes to its stability and bioactivity. The peptide’s compact size and specific sequence allow it to interact with various cellular receptors and signaling pathways, promoting tissue repair and modulating inflammatory responses.
Cryo-EM studies have provided critical insights into the molecular interactions of BPC-157 with various cellular targets. These studies have shown that BPC-157 can interact with integrin receptors on the cell surface, which play a crucial role in cell adhesion, migration, and tissue repair. The cryo-EM images reveal that BPC-157 binds to integrins in a specific orientation, stabilizing the receptor and enhancing its interaction with the extracellular matrix (ECM). This interaction is thought to be a key mechanism by which BPC-157 promotes tissue healing and regeneration.
Additionally, cryo-EM has shown that BPC-157 can modulate the activity of growth factor receptors, such as the vascular endothelial growth factor (VEGF) receptor. This modulation enhances angiogenesis, the formation of new blood vessels, which is crucial for tissue repair and regeneration. The ability of BPC-157 to influence these fundamental biological processes at the molecular level underscores its potential as a therapeutic peptide in regenerative medicine.
BPC-157’s mechanisms of action are multifaceted, involving the modulation of various signaling pathways and cellular processes. One of the primary mechanisms is its ability to enhance angiogenesis by upregulating VEGF expression and stabilizing endothelial cells. This process is vital for tissue repair as it ensures an adequate blood supply to the injured area, facilitating nutrient delivery and waste removal.
Furthermore, BPC-157 has been shown to modulate the inflammatory response, reducing pro-inflammatory cytokines and promoting the production of anti-inflammatory molecules. This dual action helps in controlling excessive inflammation, which can be detrimental to tissue healing. BPC-157 also influences the production of growth factors and ECM components, further contributing to its regenerative properties.
Research has also indicated that BPC-157 can interact with the dopaminergic and serotonergic systems, suggesting potential neuroprotective effects. These interactions could open new avenues for research into neuroregeneration and the treatment of neurological disorders.
BPC-157’s ability to promote tissue repair, modulate inflammation, and potentially influence neuroprotective pathways positions it as a peptide of significant interest in various fields of research. Studies are ongoing to explore its applications in wound healing, gastrointestinal health, musculoskeletal injuries, and even neuroregeneration. The peptide’s stability and bioactivity make it a strong candidate for further preclinical and clinical studies, with the potential to become a key tool in regenerative medicine.
TB-500 is a synthetic derivative of thymosin beta-4, a naturally occurring protein involved in cellular repair and regeneration. TB-500 is specifically designed to mimic the active region of thymosin beta-4, consisting of the following amino acid sequence:
Ac-Ser-Asp-Lys-Pro-Asp-Met-Ala-Glu-Ile-Glu-Lys-Phe-Asp-Lys-Ser-Lys-Leu-Lys-Lys-Thr-Glu-Ser.
This peptide sequence includes critical amino acids responsible for binding to actin and modulating cellular processes such as migration, proliferation, and differentiation. The acetylation at the N-terminus (Ac-Ser) enhances the peptide’s stability, allowing it to remain active in various biological environments. TB-500’s structure enables it to interact with a wide range of cellular targets, making it a versatile tool in research focused on tissue repair and regeneration.
Cryo-EM studies of TB-500 have revealed its interaction with actin, a protein that plays a fundamental role in cell motility, structure, and integrity. TB-500 binds to actin filaments, promoting their polymerization and stabilization. This interaction is crucial for enhancing cell migration, which is a key process in wound healing and tissue repair. The cryo-EM images show that TB-500 not only stabilizes actin filaments but also prevents their depolymerization, ensuring the structural integrity of cells during tissue repair processes.
Additionally, TB-500 has been observed to interact with other components of the cytoskeleton, such as microtubules and intermediate filaments, further supporting its role in cellular repair and regeneration. These interactions highlight TB-500’s potential to influence various cellular processes critical for maintaining tissue homeostasis and promoting healing.
TB-500’s primary mechanism of action revolves around its interaction with actin and other cytoskeletal components, which are essential for cell movement and structural integrity. By promoting actin polymerization, TB-500 enhances cell migration, a critical step in tissue repair. This process is particularly important in wound healing, where cells must migrate to the site of injury to facilitate tissue regeneration.
Furthermore, TB-500 has been shown to upregulate the production of laminin, a key component of the basal lamina, and collagen, which are crucial for tissue integrity and repair. By promoting the production of these ECM components, TB-500 helps in maintaining tissue structure and accelerating the healing process.
TB-500 also modulates the inflammatory response by reducing the levels of pro-inflammatory cytokines and increasing anti-inflammatory cytokines. This modulation helps in creating an optimal environment for tissue repair, reducing the risk of chronic inflammation that can hinder the healing process.
The potential of TB-500 in promoting tissue repair and regeneration makes it a valuable peptide in research focused on wound healing, musculoskeletal injuries, and cardiovascular health. Its ability to modulate the cytoskeleton and ECM components, combined with its anti-inflammatory properties, positions TB-500 as a versatile peptide with broad applications in regenerative medicine. Ongoing research is exploring its potential in treating a variety of conditions, including cardiac injuries, chronic wounds, and fibrotic diseases.
When discussing TB-500 and Thymosin Beta-4 (TB4), it’s important to understand the distinctions between these two peptides and their roles in research. TB-500 is a specific fragment of the larger TB4 molecule, particularly encompassing amino acids 17-23 of TB4. This makes TB-500 a much smaller peptide compared to the full TB4 molecule. The fragment TB-500 is thought to concentrate more directly on promoting healing processes, whereas the full TB4 peptide is researched for its broader systemic effects, including tissue repair, anti-inflammatory actions, and cellular regeneration.
However, in practice, most of the TB-500 peptides available for research, including the one offered by our laboratory, are actually the full TB4 molecule rather than just the TB-500 fragment. This is typically noted on lab analysis reports as “TB-500 (TB4),” reflecting the fact that what is being sold as TB-500 is, in reality, the complete TB4 molecule. The two are often conflated in the marketplace, despite their technical differences and potentially distinct biological effects.
The full TB4 molecule is more extensively studied, given its comprehensive role in healing and systemic health, while TB-500, being a smaller segment, is less studied but speculated to be more focused on specific healing mechanisms. For researchers, this distinction is crucial, as it influences the scope and interpretation of experimental results. Our ongoing efforts are directed towards sourcing the actual TB-500 fragment to ensure accuracy in research, but currently, what we provide is the full TB4 molecule, labeled as TB-500.
This nuanced difference is important for researchers to consider, as TB-500 and TB4, while related, are not identical and may have differing impacts depending on the specific research focus.
While both BPC-157 and TB-500 are peptides involved in tissue repair and regeneration, their amino acid structures and origins are quite distinct. BPC-157 is a pentadecapeptide derived from a naturally occurring gastric protein, while TB-500 is a synthetic derivative of thymosin beta-4, designed to mimic the active region of the parent protein. The structural differences between the two peptides result in distinct mechanisms of action and biological effects.
BPC-157 primarily works by promoting angiogenesis, modulating the inflammatory response, and interacting with various growth factors and receptors involved in tissue repair. Its ability to enhance blood vessel formation and stabilize cellular interactions makes it particularly effective in healing tissues and reducing inflammation.
In contrast, TB-500’s mechanism of action centers around its interaction with actin and other cytoskeletal components, promoting cell migration and maintaining cellular structure. TB-500 is especially effective in processes that require extensive cell movement, such as wound healing and tissue regeneration.
Cryo-EM studies have provided valuable insights into the molecular interactions of both peptides. BPC-157’s interaction with integrins and growth factor receptors supports its role in angiogenesis and tissue stabilization. Meanwhile, TB-500’s binding to actin and other cytoskeletal elements underscores its ability to promote cell migration and structural integrity during tissue repair.
Both peptides hold significant promise in regenerative medicine, but their applications may differ based on their mechanisms of action. BPC-157 is particularly suited for research in gastrointestinal health, neuroprotection, and tissue repair, where angiogenesis and inflammation modulation are critical. TB-500, with its focus on cytoskeletal modulation and cell migration, is ideal for research in wound healing, musculoskeletal injuries, and cardiovascular health.
For researchers interested in exploring the potential of BPC-157 and TB-500, it is crucial to source these peptides from a reliable supplier to ensure quality and purity. Polaris Peptides offers high-quality BPC-157 and TB-500, adhering to rigorous quality control standards to provide research-grade peptides suitable for advanced studies. Researchers looking to buy BPC-157 or buy TB-500 can trust Polaris Peptides as a dependable source for their research needs.
BPC-157 is known for promoting angiogenesis, modulating inflammation, and supporting tissue repair. It has potential applications in wound healing, gastrointestinal health, and neuroregeneration.
TB-500 primarily focuses on enhancing cell migration and stabilizing the cytoskeleton, which is crucial for wound healing and tissue regeneration. BPC-157, on the other hand, is more involved in promoting blood vessel formation and modulating inflammatory responses.
While both peptides have distinct mechanisms of action, their combined use in research could potentially enhance tissue repair by leveraging their complementary effects on angiogenesis, inflammation modulation, and cell migration.
Polaris Peptides is a reputable supplier of research-grade BPC-157 and TB-500, offering high-quality products that meet rigorous standards for purity and potency.
Both peptides have unique properties that contribute to tissue repair and regeneration. BPC-157 excels in angiogenesis and inflammation control, while TB-500 is highly effective in promoting cell migration and maintaining cellular integrity, making them both valuable tools in regenerative medicine research.
At Polaris Peptides, we are dedicated to supporting the scientific community by supplying high-quality peptides designed exclusively for research and development endeavors of professionals. Our products are crafted for investigative purposes and are not suitable for direct human consumption or consumers, nor are they intended for clinical or therapeutic use. We uphold a strict policy to ensure our peptides are recognized distinctly from prescription medications as an entity committed to research.
Polaris Peptides is a chemical supplier. Polaris Peptides is not a compounding pharmacy or chemical compounding facility as defined under 503A of the Federal Food, Drug, and Cosmetic act. Polaris Peptides is not an outsourcing facility as defined under 503B of the Federal Food, Drug, and Cosmetic act.
Products
Legal
Customer Service
The information and statements provided by Polaris Peptides have not been assessed by the US Food and Drug Administration. Our products, alongside any claims related to them, are not formulated to diagnose, treat, cure, or prevent any condition or disease.
For complete confidence in our quality commitment, we offer a Money Back Guarantee under specific Terms and Conditions. See our Our Guarantee page for complete details.
Polaris Peptides is part of Polaris Bioactives LLC.
© 2025 Polaris Peptides. All Rights Reserved.
Discount Applied Successfully!
Your savings have been added to the cart.
Join our Polaris Insiders program to get rewarded for loyalty with exclusive deals, news about upcoming products, and more.
You must be 18 years old or older in order to access our website. Please verify your age.