TB-500
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TB-500 Peptide – 10mg
TB-500 is a synthetic peptide analogue of thymosin beta-4 (Tβ4), a naturally occurring protein present in nearly all human and animal cells. TB-500 consists of 43 amino acids and is of interest in research for its potential role in angiogenesis, cellular migration, and tissue regeneration. Preclinical studies have examined TB-500 for its effects on muscle, ligament, tendon, and cardiovascular tissue repair.
Overview
TB-500 is derived from the active region of thymosin beta-4 responsible for actin binding and cellular motility, specifically amino acid residues 17–23 (LKKTETQ). This sequence is thought to regulate actin polymerization, enabling enhanced cell migration to sites of injury and repair. Experimental data indicate that TB-500 may upregulate microRNA-146a, which modulates inflammatory signaling pathways, and may facilitate endothelial cell proliferation, new blood vessel growth, and wound remodeling.
Unlike the full-length thymosin beta-4 protein, TB-500 is a shorter, synthetic peptide, which may offer improved stability and targeted activity in experimental systems.
Chemical Makeup
- Molecular Formula: C212H350N56O78S
- Molecular Weight: 4963 g/mol
- Amino Acid Sequence: SDKPDMAEIEKFDKSKLKKTETQEKNPLPSKETIEQEKQAGES
- Other Known Titles: Thymosin Beta-4 fragment, Synthetic Tβ4 analogue
Research and Clinical Studies
Wound Healing and Angiogenesis
In murine wound models, TB-500 increased re-epithelialization rates and wound contraction, supporting its proposed role in tissue regeneration. Its angiogenic potential has been linked to enhanced endothelial migration and vascular remodeling.
Ligament and Tendon Models
Preclinical studies on medial collateral ligament injury reported improved collagen organization and tensile strength following TB-500 exposure, suggesting a potential role in connective tissue repair.
Muscle and Cardiac Regeneration
Animal models of myocardial infarction have shown that TB-500 may activate integrin-linked kinase (ILK) and protein kinase B (Akt), supporting cardiomyocyte survival, angiogenesis, and cardiac tissue repair.
Neurological Injury
Experimental investigations indicate TB-500 may assist in neuronal recovery and remyelination, potentially by modulating inflammatory signaling and supporting oligodendrocyte differentiation.
Inflammation Regulation
By increasing microRNA-146a expression, TB-500 appears to suppress Toll-like receptor–linked pathways (IRAK1 and TRAF6), reducing inflammatory cytokine signaling.
TB-500 peptide is available for research and laboratory purposes only. Not for human consumption.
References
- Malinda KM, et al. Thymosin β4 accelerates wound healing. J Invest Dermatol. 1999;113(3):364–368. https://www.sciencedirect.com/science/article/pii/S0022202X15405950
- Xu B, et al. Thymosin β4 enhances ligament healing in rats. Regul Pept. 2013;184:1–5. https://pubmed.ncbi.nlm.nih.gov/23523891/
- Bock-Marquette I, et al. Thymosin β4 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 β4 and cardiac reprogramming factors. Ann N Y Acad Sci. 2012;1270:66–72. https://pubmed.ncbi.nlm.nih.gov/23259435/
- Santra M, et al. Thymosin β4 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 β4 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 N Y 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 β4 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 β4: structure and function review. Ann N Y Acad Sci. 2010;1194:179–189. https://pubmed.ncbi.nlm.nih.gov/20536459/
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How do I know the peptides I order are exactly what the label says?
Every vial we sell comes from a lab that follows current Good Manufacturing Practices (cGMP). That means each step of production is documented and controlled. Before a batch is released, it’s tested by independent third-party labs for purity, identity, and sterility. Certificates of analysis are available so you can see the exact test results.
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Yes. The labs we work with use ISO-certified clean rooms where air quality, equipment, and handling procedures are tightly regulated. Staff are trained to pharmaceutical-grade standards. This ensures the peptides are produced in an environment that minimizes contamination risks.
What about shipping? Do the peptides remain stable in transit?
Peptides in lyophilized (freeze-dried) form are stable at room temperature for transport. Once you receive them, refrigeration is recommended to maintain long-term integrity. We package every order securely to prevent damage and ship promptly, so your vials arrive in optimal condition.
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We operate under strict in-house protocols that follow current Good Manufacturing Practices (cGMP). That means our team oversees the entire process from sourcing raw amino acids to the final lyophilized vial. Nothing is outsourced or repackaged. This gives us full control over purity, consistency, and sterility, and it’s why we can stand behind every single vial we ship.
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Store them in the refrigerator, away from direct light and heat. If you need to keep them longer, some peptides can be stored frozen. Each vial comes with clear handling instructions so you know the proper conditions for stability.
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