TB-500

TB-500

TB-500 is a highly purified, synthetic peptide derived from the active region of thymosin beta-4 (T beta 4), a ubiquitous protein naturally present in nearly all human and animal cells. While the endogenous T beta 4 protein is composed of 43 amino acid residues, TB-500 is the truncated, bioactive core. It is primarily investigated for its potential to modulate cellular processes critical for tissue regeneration, cellular migration (motility), and angiogenesis (the formation of new blood vessels). Preclinical research has extensively explored its possible role in enhancing the repair and recovery of various tissues, including skeletal muscle, tendons, ligaments, and cardiovascular structures.

TB-500 Peptide - 10mg Overview

The 10mg TB-500 product is synthesized to isolate the active functional core of thymosin beta-4, corresponding specifically to the amino acid residues 17–23, which is the sequence LKKETEQ. This short, highly conserved segment is responsible for the molecule's potent function in binding actin and regulating cell movement. The peptide is hypothesized to regulate actin polymerization, a foundational cytoskeletal process that facilitates rapid and enhanced cell migration to sites of injury, thereby promoting accelerated tissue repair.

Furthermore, laboratory studies indicate that TB-500 may influence the expression of microRNA-146a. This microRNA is implicated in regulating inflammatory signaling pathways, which in turn supports endothelial cell growth, angiogenesis, and the wound healing cascade.

In experimental settings, TB-500 is often utilized over the full-length T beta 4 protein due to its design as a shorter, optimized synthetic analogue. This modification provides the research molecule with greater stability and targeted bioactivity, making it an effective tool for controlled in vitro and in vivo research applications.

TB-500 Peptide Mechanism of Action

TB-500 operates by mimicking the core function of thymosin beta-4 (T beta 4), whose main biological activity is to interact with actin proteins. Actin is one of the most fundamental structural elements in eukaryotic cells, forming the microfilaments that comprise the cell's cytoskeleton. These microfilaments are essential for maintaining cell shape, safeguarding cell membrane integrity, enabling cell movement (motility), and participating in necessary steps of cell division. In muscle tissue, actin is a key component required for the contraction process.

T beta 4 and its derivatives, like TB-500, act as actin-sequestering molecules. They efficiently capture individual actin units, known as actin monomers, protecting them from degradation and maintaining them in a readily available, high-concentration pool. This reserve ensures that actin monomers are immediately available for rapid assembly (polymerization) into new microfilaments whenever the cell receives a signal for movement, growth, or structural rearrangement, such as during the response to tissue injury.

Feature

Thymosin Beta-4 (T beta 4)

TB-500 Peptide

Origin

Naturally occurring protein

Synthetic analogue

Amino Acid Length

43 residues

7 residues (LKKETEQ)

Primary Biological Role

Actin-sequestering, cell function regulation

Targeted actin-sequestering, repair modulation

Experimental Use

Broader systemic studies

Targeted bioactivity and stability studies

TB-500 (Thymosin Beta-4) Peptide Sequence

The precise, active sequence of the TB-500 heptapeptide is:

L-Lys-Lys-Glu-Thr-Glu-Gln-Lys

This sequence mirrors the crucial actin-binding domain located at amino acid residues 17 through 23 of the naturally occurring thymosin beta-4.

TB-500 Structure Solution Formula (Example for 5mg/mL Concentration):

To achieve a 5mg per milliliter concentration, combine 10mg of lyophilized TB-500 peptide powder with 2 milliliters of an appropriate solvent, such as Bacteriostatic Water for Injection.

TB-500 Research

1. TB-500 and Neurologic Function

Studies conducted in rat models have provided evidence that TB-500 actively promotes the repair and remodeling of injured tissues within both the central nervous system (CNS) and the peripheral nervous system (PNS). While the full extent of the mechanism is still being clarified, existing data suggests that TB-500 stimulates the activity of oligodendrocytes—cells that provide crucial support and insulation for neurons. This enhanced activity is associated with increased formation of blood vessels (neovascularization) and stimulation of neuronal proliferation and growth in damaged areas of the brain and spinal cord, leading to demonstrable laboratory and behavioral improvements in motor function, cognition, and behavioral metrics.

Further investigations indicate that TB-500 may play a role in reducing oxidative stress following severe spinal cord injury and improving the viability and survival of transplanted neural stem or progenitor cells (NSPCs), thereby lending support to spinal regeneration efforts. These findings position TB-500 and related T beta 4 derivatives as highly promising research compounds for exploring treatments for severe spinal cord injuries and potentially assisting in functional recovery.

2. TB-500 and Blood Vessel Growth (Angiogenesis)

Both TB-500 and T beta 4 are recognized as powerful inducers of VEGF (Vascular Endothelial Growth Factor) production, a key signaling molecule that drives the formation of new capillaries essential for tissue repair and hair growth. However, researchers theorize that TB-500’s function in angiogenesis is multifaceted, extending beyond simple VEGF stimulation. It is proposed that the peptide contributes directly to multiple phases of blood vessel development, including the remodeling of the extracellular matrix, and supporting processes such as vasculogenesis, angiogenesis, and the differentiation of early mesenchymal cells into specialized endothelial cells that form the vessel lining. This theory is substantiated by findings where T beta 4 deficiency impaired blood vessel growth, while external administration of the peptide enhanced capillary formation and promoted the necessary recruitment of pericytes following acute tissue injury.

3. TB-500 and Hair Growth

The correlation between T beta 4 and the regulation of the hair follicle cycle was initially observed incidentally in laboratory experiments. Mice lacking the T beta 4 gene were found to have significantly delayed hair regrowth after being shaved compared to control mice. Conversely, mice engineered to produce elevated levels of T beta 4 displayed markedly accelerated hair regrowth. Detailed microscopic analysis confirmed that the high T beta 4-expressing mice possessed a greater number of hair shafts and clusters of hair follicles, suggesting the peptide's direct involvement in modulating the anagen (growth) phase of the hair cycle.

4. TB-500 and Antibiotic Synergy

The global rise of infections resistant to conventional treatments underscores the urgent need for new therapeutic strategies. Recent studies on T beta 4 and related compounds offer a novel approach. In murine models of eye infection caused by Pseudomonas aeruginosa, combining T beta 4 with ciprofloxacin, a standard antibiotic, resulted in a substantial enhancement of the antibiotic's effectiveness. This combination accelerated healing, dramatically reduced inflammation, and promoted quicker recovery. Within days, researchers documented fewer bacterial colonies, lower neutrophil (white blood cell) counts, and decreased levels of inflammatory reactive oxygen species. This groundbreaking research is the first to indicate that TB-500 and its related peptides could act as a potent adjuvant, significantly boosting and complementing the therapeutic action of established antibiotics.

5. TB-500 and Cardiovascular Health

Over the last two decades, comprehensive studies have demonstrated that T beta 4 and its analogues confer various protective and restorative advantages to both the cardiovascular and renal systems, though the precise biochemical network is complex. Current research suggests these benefits are mediated by several mechanisms. Primarily, TB-500 supports the development of collateral circulation (alternative blood vessels), which is crucial for both prevention and restoration of blood flow following ischemic events. It also actively promotes the required migration of endothelial cells and improves the survival rate of cardiomyocytes (heart muscle cells) after myocardial infarction. Furthermore, TB-500 appears to modulate signaling pathways to help control inflammation and reduce fibrosis, effectively limiting detrimental scar tissue formation.

Recent advancements in hydrogel-based delivery systems incorporating T beta 4 have demonstrated enhanced angiogenesis and increased movement of epicardial heart cells. These localized effects accelerate recovery from ischemic damage and may reduce the risk of long-term complications by minimizing permanent scarring.

6. TB-500 and Neurodegenerative Diseases

Progress in developing effective treatments for neurodegenerative conditions, such as Alzheimer’s and prion-related disorders, has been slow. However, contemporary research examining T beta 4’s influence on the immune system’s capacity to process misfolded proteins has revealed that the peptide enhances autophagy. Autophagy (or "self-eating") is a key cellular maintenance process that acts as the central nervous system’s primary defense mechanism against neurodegeneration by helping cells clear damaged or toxic components. By improving this natural, protective mechanism, T beta 4 research provides an early, vital step toward potential therapeutic approaches for these debilitating diseases.

7. TB-500 Has Wide Application

Because of its fundamental role in regulating cellular structure and function (specifically via the actin cytoskeleton), the biological influence of TB-500 extends across nearly all tissue types in the body. This broad physiological impact has driven immense research exploring its diverse potential. Studies consistently suggest TB-500 is a valuable research subject for investigating cardiovascular and neurological conditions, enhancing antibiotic performance, and promoting wide-ranging tissue regeneration. This makes it one of the most intensively studied peptides in contemporary biomedical research, a trend expected to accelerate in the future.

TB-500 has been observed to exhibit a favorable profile with minimal reported side effects and good bioavailability following both oral and subcutaneous administration in numerous animal studies. It is imperative to note that experimental dosages effective in animal models do not directly translate to or imply effectiveness in humans. TB-500 is sold exclusively for research purposes and is strictly intended for laboratory and educational use only. It is not authorized for administration or consumption by humans or animals.

Article Author

This comprehensive literature review was compiled, edited, and organized by Dr. Daniel C. Crockford, Ph.D. Dr. Crockford is a highly respected biomedical scientist widely recognized for his extensive research focusing on thymosin beta-4 (T beta 4) and its synthetic analogue, TB-500. His foundational work has been instrumental in expanding the scientific community's understanding of the peptide’s critical involvement in angiogenesis, tissue regeneration, and cellular repair processes. Through numerous peer-reviewed studies and collaborative reviews, Dr. Crockford has made significant contributions toward defining the biological activities and potential therapeutic scope of T beta 4 analogues in the fields of cardiovascular, neurological, and regenerative medicine.

Dr. Crockford has dedicated his career to conducting comprehensive studies on thymosin beta-4 and related compounds, meticulously 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 profoundly advanced the current understanding of T beta 4’s molecular mechanisms and its crucial role in promoting tissue repair and regeneration.

Dr. Crockford is widely acknowledged as one of the principal contributors to the early, fundamental 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 esteemed colleagues to the field of peptide research. It must under no circumstances be interpreted as an endorsement, promotion, or statement of affiliation. The distributing company maintains no affiliation, sponsorship, or professional association with Dr. Crockford or any of the researchers mentioned herein.

Reference Citations

• Malinda KM, et al. Thymosin beta 4 accelerates wound healing. J Invest Dermatol. 1999;113(3):364–368. https://www.sciencedirect.com/science/article/pii/S0022202X15405950
• Xu B, et al. Thymosin beta 4 enhances ligament healing in rats. Regul Pept. 2013;184:1-5. https://pubmed.ncbi.nlm.nih.gov/23523891/
• Bock-Marquette I, et al. Thymosin beta 4 activates integrin-linked kinase and promotes cardiac repair. Nature. 2004;432(7016):466-472. https://doi.org/10.1038/nature03000
• Srivastava D, et al. Cardiac repair with thymosin beta 4 and cardiac reprogramming factors. Ann NY Acad Sci. 2012;1270:66-72. https://pubmed.ncbi.nlm.nih.gov/23259435/
• Santra M, et al. Thymosin beta 4 regulation of microRNA-146a in inflammation. J Biol Chem. 2014;289(28):19508-19518. https://pubmed.ncbi.nlm.nih.gov/24860091/
• Philp D, et al. Thymosin beta 4 and tissue regeneration. J Invest Dermatol. 2004;123(4):802-809. https://pubmed.ncbi.nlm.nih.gov/15373782/
• Crockford D, et al. Thymosin beta-4: structure and function review. Ann NY Acad Sci. 2010;1194:179–189. https://pubmed.ncbi.nlm.nih.gov/20536459/
• Goldstein AL, et al. History and development of thymosins. Ann N Y Acad Sci. 2007;1112:1-13. https://pubmed.ncbi.nlm.nih.gov/17656565/
• Bock-Marquette I, et al. Thymosin beta 4 supports myocardial migration and survival. Nature. 2004;432:466-472. https://pubmed.ncbi.nlm.nih.gov/15565145/
• Crockford D, Turjman N, Allan C, Angel J. Thymosin beta 4: structure and function review. Ann N Y Acad Sci. 2010;1194:179-189. https://pubmed.ncbi.nlm.nih.gov/20536459/

REGULATORY DISCLAIMER: ALL ARTICLES AND PRODUCT INFORMATION PROVIDED ON THIS WEBSITE ARE FOR INFORMATIONAL AND EDUCATIONAL PURPOSES ONLY. The products offered on this website are furnished for in-vitro studies only (Latin: in glass, performed outside of the living body). These products are not medicines or drugs and have not been approved by the FDA or any other regulatory body to prevent, treat, or cure any medical condition, ailment, or disease. Bodily introduction of any kind into humans or animals is strictly forbidden by law.

STORAGE

Storage Instructions

All TB-500 products are produced via lyophilization (freeze-drying), a specialized dehydration method that preserves molecular stability. This process ensures the product maintains its integrity during transport, typically for a period of approximately three to four months at ambient shipping temperatures.

• Lyophilization is a process where peptides are frozen and then exposed to a high vacuum. This causes the water to undergo sublimation, transforming directly from a solid (ice) to a gas (vapor) without passing through the liquid phase. The result is a highly stable, white crystalline powder known as a lyophilized peptide.
• The resulting powder is stable for extended periods and can be safely kept at room temperature until the user is ready for reconstitution with a sterile solvent, such as bacteriostatic water.
• Once reconstituted with bacteriostatic water, the peptide solution must be stored in a refrigerator to maintain maximum effectiveness, remaining stable for up to 30 days.

Best Practices For Storing Peptides

Following correct storage protocols is crucial for maintaining the accuracy, purity, and reliability of experimental results. Proper storage prevents contamination, oxidation, and molecular degradation, ensuring the peptide remains stable and effective for its intended lifespan.

Storage State

Recommended Temperature

Maximum Duration

Key Storage Practice

Lyophilized (Short-Term)

Below 4 degrees Celsius (39 degrees Fahrenheit), Refrigerated

Few days to several months

Must be protected from light

Lyophilized (Long-Term)

-80 degrees Celsius (-112 degrees Fahrenheit), Freezer

Several months to years

Avoid repeated freeze-thaw cycles

Reconstituted in Solution

4 degrees Celsius (39 degrees Fahrenheit), Refrigerated

Up to 30 days

Store in sterile buffers, aliquot contents

• 
  Upon Receipt: Peptides should be immediately kept cool and shielded from light. For short-term use (from a few days up to a few months), standard refrigeration below 4 degrees Celsius (39 degrees Fahrenheit) is suitable. Lyophilized peptides generally remain stable at ambient temperature for several weeks, making this acceptable for very brief storage before use.
• Long-Term Preservation: For storage periods that span several months to multiple years, the optimal method is freezing at -80 degrees Celsius (-112 degrees Fahrenheit). This deep-freeze condition offers the best stability and protection against structural degradation.
• Avoid Temperature Fluctuations: It is critical to minimize freeze-thaw cycles, as repeated temperature shifts rapidly accelerate degradation. Specifically, frost-free freezers must be avoided, as their regular defrost cycles cause temperature variations that compromise peptide stability.

Preventing Oxidation and Moisture Contamination

Protecting peptides from exposure to air and moisture is essential, as both rapidly compromise molecular stability.

• Moisture Contamination: Moisture risk is highest when removing cold vials from the freezer. To prevent condensation from the ambient air forming on the cold powder or inside the vial, always allow the vial to reach room temperature before opening it.
• Air Exposure: The container should remain closed as much as possible. After removing the necessary amount, the vial must be promptly resealed. Storing the remaining peptide under a dry, inert gas atmosphere (such as nitrogen or argon) can further mitigate oxidation. Peptides containing specific residues like cysteine (C), methionine (M), or tryptophan (W) are highly sensitive to air oxidation and require extra handling precautions.
• Aliquoting Strategy: To preserve long-term integrity, avoid frequent thawing and refreezing by dividing the total peptide quantity into smaller, single-use aliquots upon receipt. This reduces repeated exposure to air and temperature changes, thereby maintaining the peptide's structural integrity over time.

Storing Peptides In Solution

Peptide solutions have a significantly shorter shelf life than their lyophilized forms and are more vulnerable to chemical and bacterial degradation. Peptides containing cysteine (Cys), methionine (Met), tryptophan (Trp), aspartic acid (Asp), glutamine (Gln), or N-terminal glutamic acid (Glu) residues are known to degrade more rapidly when kept in solution.

• Solvent Conditions: If storage in solution is necessary, it is highly recommended to use sterile buffers with an optimal pH range between 5 and 6.
• Aliquoting: The solution should be immediately divided into aliquots to minimize the damaging effects of repeated freeze-thaw cycles.
• Stability: Under refrigerated conditions at 4 degrees Celsius (39 degrees Fahrenheit), most peptide solutions remain stable for up to 30 days. However, peptides with known instability should be kept frozen when not in immediate use to best maintain their structural integrity.

Peptide Storage Containers

Containers used for peptide storage must be clean, durable, chemically inert, and sized appropriately to minimize excess headspace above the peptide powder or solution.

• Suitable Materials: Both glass and various plastic vials are used. Plastic options typically include polystyrene or polypropylene:
• Polystyrene: Offers clarity for easy visibility but provides limited chemical resistance.
• Polypropylene: Is more chemically resistant but typically translucent.
• Glass: High-quality glass vials are generally preferred for offering the best combination of clarity, stability, and chemical inertness for long-term storage.
• Transfer Note: Peptides are often shipped in plastic vials to minimize the risk of breakage during transit. Researchers can safely transfer peptides between glass and plastic containers as needed to suit specific storage or experimental handling requirements.