TB-500 is a synthetic fragment of Thymosin Beta-4, a naturally occurring peptide studied for its role in cell migration, connective tissue and recovery research.
| Purity | ≥99% (LC-MS verified) |
| Form | Lyophilized powder, preservative free |
| Storage | Cool and dry; refrigerate after reconstitution |
| Batch | COA available on request |
TB-500 is a synthetic fragment of Thymosin Beta-4, a naturally occurring peptide studied for its role in cell migration, connective tissue and recovery research.
TB-500 is a synthetic peptide corresponding to the active region of thymosin beta-4, a naturally occurring 43-amino-acid protein present in most mammalian cells and one of the most abundant actin-binding proteins in the body. The fragment reproduces the actin-binding domain that carries most of the biological activity attributed to the parent protein.
Supplied as lyophilized powder, preservative free and sealed under vacuum. Each lot is verified by third-party HPLC and LC-MS, with the certificate of analysis tied to the lot number on the vial.
Supplied for laboratory research use only. Not for human consumption.
Thymosin beta-4 binds monomeric G-actin and regulates its availability for polymerisation into F-actin filaments. Because the actin cytoskeleton governs how cells change shape and move, this binding activity is the mechanism most often invoked in the migration findings reported across the literature.
In vitro studies have examined the migration of endothelial cells, keratinocytes and fibroblasts, which is the process underlying tissue coverage in wound models. Researchers have used these assays to characterise the fragment's activity independently of the full parent protein.
A separate strand of work concerns the formation of new capillary structures in endothelial assays, examining thymosin beta-4 and its fragments alongside other angiogenic signalling molecules.
Some of the most cited work involves cardiac tissue after induced injury and corneal epithelial models, both selected because they allow migration and coverage to be measured directly.
The literature is predominantly preclinical — cell culture and animal models. TB-500 has not completed human clinical trials and is not an approved drug.
Concentration is set by the volume of diluent added. For a 10mg vial, 2mL of bacteriostatic water yields 5mg/mL. Calculate the working concentration your protocol requires rather than following a generic figure.
| State | Temperature | Practical shelf life |
|---|---|---|
| Lyophilized, sealed | −20 °C | 24+ months |
| Lyophilized, sealed | 2–8 °C | ~12 months |
| Lyophilized, sealed | Room temperature | Weeks — transit only |
| Reconstituted, bacteriostatic water | 2–8 °C | ~3–4 weeks |
| Reconstituted, sterile water | 2–8 °C | Same session |
Lyophilized peptide is stable enough to survive shipping at ambient temperature, which is why cold-chain courier service is not required for transit. Long-term storage is a different matter — material intended to be held for months belongs in a freezer.
Protect from light, and avoid repeated freeze-thaw cycles. Each cycle causes measurable degradation, so dividing a reconstituted stock into single-use aliquots before freezing is preferable to thawing and refreezing one vial repeatedly.
Every lot is tested by an independent laboratory using two orthogonal methods. HPLC (high-performance liquid chromatography) establishes purity as a percentage of total peptide content, separating the target compound from truncated sequences and synthesis by-products. LC-MS (liquid chromatography–mass spectrometry) confirms molecular identity by mass.
Both matter. Purity alone is insufficient — a 99% pure sample of the wrong compound is still the wrong compound. Together the two tests establish identity and quality, which is why TB-500 is released only after both pass.
The certificate of analysis references the lot number printed on your vial label. Request the COA for your lot at [email protected].
Peer-reviewed studies indexed in PubMed. Each links to the abstract and, where a free copy exists, to the full text. We link primary sources rather than summarising them second-hand.
Compounds studied alongside this one, or acting through related pathways.
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