Also known as Thymosin Beta-4 fragment
Synthetic fragment of thymosin β4 studied for cell migration and tissue repair.
TB-500 corresponds to the active actin-binding region of thymosin β4. Preclinical studies report effects on endothelial cell migration, angiogenesis, and wound healing.
TB-500 is a synthetic peptide corresponding to the actin-binding region of thymosin β4, a naturally occurring protein involved in cell migration and tissue repair. By sequestering G-actin, thymosin β4 influences cytoskeletal dynamics, and TB-500 is studied as a fragment that reproduces part of this activity.
As with BPC-157, the evidence for TB-500 is largely preclinical and it is not FDA-approved; it is also a prohibited substance in regulated sport. Research interest centers on endothelial cell migration, angiogenesis, and wound healing, with cardiac and dermal repair among the contexts studied.
G-actin sequestration; modulation of cell migration and angiogenesis.
Behind every vial of TB-500 is the same exacting pipeline every research peptide runs — but the chemistry plays out differently for this molecule. Here is how TB-500, specifically, is brought into being.
On paper, TB-500 is C38H68N10O14 — about 889 daltons of precisely arranged atoms. Before a single bond is made, the target sequence, salt form, and purity threshold are written down as the contract the finished material must meet.
Assembling TB-500 means roughly 7 coupling cycles on the synthesizer — one protected residue added at a time, which is also 7 chances for an incomplete coupling to seed a deletion impurity. It is a short sequence, which makes the build comparatively tractable — but short does not mean trivial, and purity is still won or lost downstream.
The crude mixture — TB-500 plus its deletions and side products — is then separated on preparative HPLC, and where the cut is taken decides the difference between a genuinely pure peptide and a barely-passable one.
A real batch of TB-500 proves itself: identity confirmed by mass spectrometry against its ~889 Da, purity read directly off an analytical HPLC trace, water and counterion content measured. That batch-specific certificate of analysis is the only honest way to know what is actually in a vial of TB-500 — and a short, cold, accountable chain of custody is how that purity survives the trip to your bench.
Producing TB-500 to a genuine purity spec means solid-phase synthesis, preparative HPLC purification, and batch quality control — none of it cheap, and none of it something you can verify by eye.
Don't judge a vial by its cake. A fluffy, good-looking lyophilized powder reflects bulking agents and freeze-drying parameters — not purity. Insist on a batch-specific certificate of analysis.
Recent clinical trials and publications mentioning TB-500, pulled automatically from ClinicalTrials.gov and PubMed and refreshed daily. Listings are unfiltered search results, not curated endorsements.
TB-500 is a synthetic peptide based on the actin-binding region of thymosin β4, studied in preclinical models for cell migration and tissue repair.
TB-500 corresponds to the active actin-binding fragment of the larger thymosin β4 protein, reproducing part of its cytoskeletal activity.
No — it is not FDA-approved and is prohibited by the World Anti-Doping Agency. This page is a research and educational reference.
Research contexts include wound healing, angiogenesis, cardiac repair, and hair-follicle biology, primarily in animal and cell models.
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