THYMOSIN β4 PEPTIDE
In stock
TB-500 is the synthetic version of thymosin beta-4, a peptide found in nearly every cell in the body, where it helps organize actin — the internal scaffolding cells use to hold their shape and move around.
That role makes it a favorite in cell-migration and wound-model research, with a growing body of cardiovascular work alongside. It's often paired with BPC-157 in repair-focused study designs.
Keep the sealed vials in the fridge and out of direct light — they’ll hold up for a long time that way. Once a vial is mixed, keep it refrigerated and use it within the window your protocol calls for.
Every batch we sell is tested by an independent U.S. lab before it goes up for sale — that report is the certificate of analysis, and a copy is included with every order. Want the one for your exact vial? Email the lot number printed on the label to [email protected] and we’ll send it over within one business day.
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Also referenced as: thymosin beta-4 · Tβ4
TB-500 is the synthetic form of thymosin beta-4, a 43-amino-acid peptide found in nearly every cell in the body and in high concentration in blood platelets and wound fluid. Its day job is cytoskeletal: it binds and sequesters G-actin, the building block cells polymerize into the internal scaffolding they use to hold shape and move.
Controlling actin availability makes Tβ4 a master regulator of cell migration — and migration is the first act of nearly every repair process, which is what pulled this peptide from basic cell biology into wound-healing research.
The wound-model literature is the deepest: dermal and corneal healing studies where Tβ4 exposure changes how quickly cells move into a wound bed and organize new tissue. Endothelial work sits alongside it — tube-formation and vessel-sprouting assays tied to the same migratory machinery.
A distinct cardiovascular thread has grown over the past two decades, studying Tβ4 in cardiac injury models, including work on epicardial cell activation after ischemic damage. For labs, the appeal is a single, well-characterized molecule that connects cytoskeletal mechanics to tissue-level repair outcomes.
Supplied lyophilized in 10 mg and 20 mg vials at 98.5% verified purity with endotoxin under 0.5 EU/mg. As a longer peptide it deserves gentle handling: minimize freeze–thaw cycles, store lyophilized at −20 °C, and keep reconstituted material cold and short-lived.
It is the natural counterpart to BPC-157 in recovery-line study designs — same models, different mechanism — and the two are frequently run as parallel arms.
The published record runs deeper than any product page should. For the primary literature, browse TB-500 studies on PubMed. For how every batch we sell is verified, see how we test.
From our research library: How to read a certificate of analysis. · BPC-157, mapped honestly. · BPC-157 vs TB-500. · Reconstitution calculator.
No. TB-500 is supplied strictly for laboratory research. It is not for human or veterinary use, and every order requires agreement to our research-use policy.
Functionally, yes — TB-500 is the name the research-supply world uses for synthetic thymosin beta-4. The peptide sequence is that of the native human protein, produced synthetically rather than extracted.
Actin is the protein cells polymerize to move and change shape. Tβ4 holds actin monomers in reserve, so raising or lowering it changes how readily cells migrate. Migration assays — wound closure, tube formation — are where that shows up measurably.
The current batch is 98.5% pure by HPLC, tested by an independent US laboratory before sale — along with identity confirmation and endotoxin screening below 0.5 EU/mg. The certificate of analysis is included with every order, and the report for any specific vial is available by emailing its lot number.
TB-500 is available in 10mg and 20mg vials of lyophilized powder. Quantity discounts apply automatically at checkout.
Keep sealed vials frozen at −20 °C and away from light. Once reconstituted, hold the solution at 2–8 °C and use it within the window your laboratory protocol defines.
