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Thymosin Beta-4 Actin-Binding Fragment
Also known as Tβ4 17-23 (Leu-Lys-Lys-Thr-Glu-Thr-Gln)
TB-500 Fragment 17-23 is the seven-residue actin-binding region of thymosin beta-4, studied in research on tissue repair and cell migration.
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This product is intended strictly for laboratory research use within Canada. It is not approved by Health Canada for the diagnosis, treatment, cure, or prevention of any disease. Not for human or veterinary use.
By purchasing, you confirm the material will be used solely for lawful research purposes in accordance with applicable Canadian regulations.
TB-500 Fragment 17-23 is the seven-residue actin-binding region of thymosin beta-4, studied in research on tissue repair and cell migration.
Experimental models examine whether the short fragment reproduces activities of the full-length parent protein.
Third-party tested for purity, ID, quantity.
Thymosin beta-4 is a 43-residue actin-sequestering protein, and its central 17-23 segment contains the actin-binding motif. Research has mapped biological activities of thymosin beta-4 to short peptide sequences, and examined whether a synthetic peptide containing the actin-binding domain promotes dermal wound repair.
Analytical work has characterized the N-terminal acetylated 17-23 fragment specifically, in the context of identifying material sold as TB-500. Researchers should note that products marketed as TB-500 vary between the full-length protein and this fragment.
Thymosin beta-4 was characterized as an actin-sequestering protein, with subsequent structure-activity work localizing several of its effects to short internal sequences.
The 17-23 fragment gained separate attention through analytical chemistry and doping-control research, which characterized the acetylated peptide found in commercial TB-500 preparations.
Research relevant to this fragment focuses on the actin-binding domain of thymosin beta-4 and whether short sequences reproduce parent-protein activity. Frameworks evaluate dermal wound repair, cell migration, and analytical identification under controlled conditions.
No. Eppix Labs products are supplied exclusively for laboratory research. We do not provide dosing, administration, or usage guidance.
Each unit contains the labeled quantity of TB-500 Fragment 17-23. Independent third-party analysis verifies purity, identity, and net content per batch.
The unit contains only the research compound. Any laboratory materials required for reconstitution or experimental procedures must be sourced separately.
Duration depends entirely on research design, storage conditions, and laboratory protocol.
Biological activities of thymosin beta4 defined by active sites in short peptide sequences
PubMedThymosin beta 4 and a synthetic peptide containing its actin-binding domain promote dermal wound repair in db/db diabetic mice and in aged mice
PubMedSynthesis and characterization of the N-terminal acetylated 17-23 fragment of thymosin beta 4 identified in TB-500, a product suspected to possess doping potential
PubMedThymosin β4 inhibits PDGF-BB induced activation, proliferation, and migration of human hepatic stellate cells via its actin-binding domain
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