TB-500

TB-500 Peptide Overview

TB-500 is a 43-residue synthetic peptide that mimics the biological activity of Thymosin Beta-4. This protein is naturally expressed in high concentrations in tissues requiring high turnover or frequent repair. TB-500 is specifically investigated for its ability to regulate the actin cytoskeleton, thereby facilitating the rapid migration of cells to wound sites. Its application in preclinical research covers a diverse spectrum, including the treatment of myocardial ischemia, neural degeneration, and orthopedic injuries involving slow-healing tissues.

TB-500 Peptide - 10mg Overview

The 10mg TB-500 research vial contains a synthesized fragment corresponding to the active region of Thymosin Beta-4. By isolating the residues responsible for actin-binding (LKKETEQ), TB-500 provides a potent tool for studying cellular motility and structural reorganization. Research indicates that the peptide modulates inflammatory signaling and promotes endothelial cell proliferation, making it a key subject in the study of wound healing and tissue engineering.

TB-500 Peptide Structure

The molecular integrity of TB-500 is verified through rigorous analytical processes.

Structure Solution Formula: Carbon 212, Hydrogen 350, Nitrogen 56, Oxygen 78, Sulfur 1

Component

Technical Detail

Product

TB-500 Lyophilized Peptide

Purity

98 percent or Higher

Weight

4.96 kDa

State

Solid Crystalline Powder

Acidity

pH 5 to 7 after reconstitution

Shelf Life

24 Months (Frozen)

TB-500 Peptide Mechanism of Action

TB-500 serves as the primary actin-sequestering molecule in mammalian cells. By binding to globular actin (G-actin), the peptide prevents spontaneous polymerization and maintains a ready-to-use pool of monomers. When a cell needs to move, divide, or repair its membrane, TB-500 releases these monomers to form filaments (F-actin). This dynamic control of the cytoskeleton is the fundamental process that allows for cell migration, tissue remodeling, and the physical repair of structural damage.

TB-500 Research

1. TB-500 and Neurologic Function

TB-500 is studied for its ability to promote the healing of the nervous system. In animal models of brain injury, the peptide has been shown to increase oligodendrocyte activity, which leads to improved myelination and motor coordination. It also demonstrates a protective effect on spinal cord neurons by reducing oxidative damage.

2. TB-500 and Blood Vessel Growth

The angiogenic properties of TB-500 are a primary focus of regenerative medicine. The peptide increases the expression of VEGF and facilitates the remodeling of the extracellular matrix. This allows for the rapid development of new capillary networks, which are essential for the survival of recovering tissues.

3. TB-500 and Hair Growth

Animal studies have established a link between TB-500 and hair follicle stem cell activation. Mice treated with the peptide show significantly faster hair regrowth and an increase in follicle density, suggesting a role for the peptide in treating conditions related to follicle dormancy.

4. TB-500 and Antibiotic Synergy

In research involving bacterial eye infections, TB-500 has been shown to enhance the antibacterial effects of ciprofloxacin. The peptide reduces the host's inflammatory response while simultaneously promoting tissue repair, leading to faster recovery times and lower bacterial counts.

5. TB-500 and Cardiovascular Health

TB-500 protects the heart by preventing cell death after a heart attack. It promotes the migration of epicardial cells and helps build collateral blood vessels, which bypass blocked arteries and restore blood flow to the cardiac muscle.

6. TB-500 and Neurodegenerative Diseases

By stimulating autophagy, TB-500 assists cells in clearing out damaged proteins. This process is vital for protecting the brain from the protein buildup associated with Alzheimer’s and other neurodegenerative conditions.

7. TB-500 Has Wide Application

Due to its influence on nearly every tissue type, TB-500 is one of the most versatile peptides in research. Its ability to coordinate repair across multiple systems—including the heart, brain, and skin—ensures its continued prominence in biomedical science.

Article Author

This literature review was compiled, edited, and organized by Dr. Daniel C. Crockford, Ph.D. Dr. Crockford is a respected biomedical scientist recognized for his extensive research on thymosin beta-4 and its synthetic counterpart, TB-500. His work has played a major role in expanding scientific understanding of the peptide’s involvement in angiogenesis, tissue regeneration, and cellular repair. Through numerous studies and collaborative reviews, Dr. Crockford has contributed to defining the therapeutic and biological potential of thymosin beta-4 analogues in cardiovascular, neurological, and regenerative medicine.

Scientific Journal Author

Dr. Daniel C. Crockford has conducted comprehensive studies on thymosin beta-4 and its related compounds, examining their structural properties, actin-binding dynamics, and biological effects on processes such as wound healing, blood vessel formation, and cardiac recovery. His research—along with that of collaborators including N. Turjman, C. Allan, J. Angel, K.M. Malinda, I. Bock-Marquette, D. Philp, and A.L. Goldstein—has significantly advanced the current understanding of thymosin beta-4’s molecular mechanisms and its role in promoting tissue repair and regeneration. Dr. Crockford is widely regarded as one of the principal contributors to the early scientific investigation of thymosin beta-4 and its derivative, TB-500. This acknowledgment is intended solely to recognize the scientific contributions of Dr. Crockford and his colleagues. It should not be interpreted as an endorsement or promotional statement. Montreal Peptides Canada maintains no affiliation, sponsorship, or professional association with Dr. Crockford or any researchers mentioned herein.

Reference Citations

Malinda KM, et al. Thymosin Beta-4 accelerates wound healing. J Invest Dermatol. 1999;113(3):364–368.

Xu B, et al. Thymosin Beta-4 enhances ligament healing in rats. Regul Pept. 2013;184:1-5.

Bock-Marquette I, et al. Thymosin Beta-4 activates integrin-linked kinase and promotes cardiac repair. Nature. 2004;432(7016):466-472.

Srivastava D, et al. Cardiac repair with thymosin Beta-4 and cardiac reprogramming factors. Ann NY Acad Sci. 2012;1270:66-72.

Santra M, et al. Thymosin Beta-4 regulation of microRNA-146a in inflammation. J Biol Chem. 2014;289 (28):19508-19518.

Philp D, et al. Thymosin Beta-4 and tissue regeneration. J Invest Dermatol. 2004;123(4):802-809.

Crockford D, et al. Thymosin beta-4: structure and function review. Ann NY Acad Sci. 2010;1194:179–189.

Goldstein AL, et al. History and development of thymosins. Ann N Y Acad Sci. 2007;1112:1-13.

Bock-Marquette I, et al. Thymosin Beta-4 supports myocardial migration and survival. Nature. 2004;432:466-472.

Crockford D, Turjman N, Allan C, Angel J. Thymosin Beta-4: structure and function review. Ann N Y Acad Sci. 2010;1194:179-189.

Storage Instructions

All products are produced through a lyophilization (freeze-drying) process, which preserves stability during shipping for approximately 3 to 4 months. After reconstitution with bacteriostatic water, peptides must be stored in a refrigerator to maintain their effectiveness. Once mixed, they remain stable for up to 30 days.

Lyophilization, also known as cryodesiccation, is a specialized dehydration method in which peptides are frozen and exposed to low pressure. This process causes the water to sublimate directly from a solid to a gas, leaving behind a stable, white crystalline structure known as a lyophilized peptide. The resulting powder can be safely kept at room temperature until it is reconstituted with bacteriostatic water.

For extended storage periods lasting several months to years, it is recommended to keep peptides in a freezer at -80 degrees Celsius. Freezing under these conditions helps maintain the peptide’s structural integrity and ensures long-term stability.

Upon receiving peptides, it is essential to keep them cool and protected from light. For short-term use—within a few days, weeks, or months—refrigeration below 4 degrees Celsius is sufficient. Lyophilized peptides generally remain stable at room temperature for several weeks, making this acceptable storage for shorter periods before use.

Best Practices For Storing Peptides

Proper storage of peptides is critical to maintaining the accuracy and reliability of laboratory results. Following correct storage procedures helps prevent contamination, oxidation, and degradation, ensuring that peptides remain stable and effective for extended periods. Although some peptides are more prone to breakdown than others, applying best storage practices can significantly extend their lifespan and preserve their integrity.

Upon receipt, peptides should be kept cool and shielded from light. For short-term use—ranging from a few days to several months—refrigeration below 4 degrees Celsius is suitable. Lyophilized peptides generally remain stable at room temperature for several weeks, making this acceptable for shorter storage durations.

For long-term preservation over several months or years, peptides should be stored in a freezer at -80 degrees Celsius. Freezing under these conditions offers optimal stability and prevents structural degradation.

It is also essential to minimize freeze-thaw cycles, as repeated temperature fluctuations can accelerate degradation. Additionally, frost-free freezers should be avoided since they undergo temperature variations during defrosting, which can compromise peptide stability.

Preventing Oxidation and Moisture Contamination

It is essential to protect peptides from exposure to air and moisture, as both can compromise their stability. Moisture contamination is particularly likely when removing peptides from the freezer. To avoid condensation forming on the cold peptide or inside its container, always allow the vial to reach room temperature before opening.

Minimizing air exposure is equally important. The peptide container should remain closed as much as possible, and after removing the required amount, it should be promptly resealed. Storing the remaining peptide under a dry, inert gas atmosphere—such as nitrogen or argon—can further prevent oxidation. Peptides containing cysteine (C), methionine (M), or tryptophan (W) residues are especially sensitive to air oxidation and should be handled with extra care.

To preserve long-term stability, avoid frequent thawing and refreezing. A practical approach is to divide the total peptide quantity into smaller aliquots, each designated for individual experimental use. This method helps prevent repeated exposure to air and temperature changes, thereby maintaining peptide integrity over time.

Storing Peptides In Solution

Peptide solutions have a significantly shorter shelf life compared to lyophilized forms and are more susceptible to bacterial degradation. Peptides containing cysteine, methionine, tryptophan, aspartic acid, glutamine, or N-terminal glutamic acid residues tend to degrade more rapidly when stored in solution.

If storage in solution is unavoidable, it is recommended to use sterile buffers with a pH between 5 and 6. The solution should be divided into aliquots to minimize freeze-thaw cycles, which can accelerate degradation. Under refrigerated conditions at 4 degrees Celsius, most peptide solutions remain stable for up to 30 days. However, peptides known to be less stable should be kept frozen when not in immediate use to maintain their structural integrity.

Peptide Storage Containers

Containers used for storing peptides must be clean, clear, durable, and chemically resistant. They should also be appropriately sized to match the quantity of peptide being stored, minimizing excess air space. Both glass and plastic vials are suitable options, with plastic varieties typically made from either polystyrene or polypropylene. Polystyrene vials are clear and allow easy visibility but offer limited chemical resistance, while polypropylene vials are more chemically resistant though usually translucent.

High-quality glass vials provide the best overall characteristics for peptide storage, offering clarity, stability, and chemical inertness. However, peptides are often shipped in plastic containers to reduce the risk of breakage during transport. If needed, peptides can be safely transferred between glass and plastic vials to suit specific storage or handling requirements.

Peptide Storage Guidelines: General Tips

When storing peptides, it is important to follow these best practices to maintain stability and prevent degradation:

• Store peptides in a cold, dry, and dark environment.
• Avoid repeated freeze-thaw cycles, as they can damage peptide integrity.
• Minimize exposure to air to reduce the risk of oxidation.
• Protect peptides from light, which can cause structural changes.
• Do not store peptides in solution long term; keep them lyophilized whenever possible.
• Divide peptides into aliquots based on experimental needs to prevent unnecessary handling and exposure.