TB-500 Fragment 17-2310mg
TB-500 Fragment 17-23 Canada — 10 mg Lyophilized Vials
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.
3 of the 4 areas below are addressed directly by a paper cited on this page.
Addressed on this page by Philp 2003, Shah 2018. Each is linked to its source record in the references below, so what was measured — and in what system — can be read rather than taken on trust.
Addressed on this page by Philp 2003. Each is linked to its source record in the references below, so what was measured — and in what system — can be read rather than taken on trust.
Addressed on this page by Shah 2018, Philp 2003. Each is linked to its source record in the references below, so what was measured — and in what system — can be read rather than taken on trust.
No paper cited on this page reports on analytical or preparations. This heading marks where TB-500 Fragment 17-23 is discussed in the category rather than a question the cited literature answers, and it is worth knowing which of these areas has work behind it and which does not.
The references section of this page cites 4 primary papers published between 2003 and 2018 — a limited but non-trivial record. Every citation is linked to its PubMed or DOI record so it can be read rather than taken on trust, and the summaries above describe what those papers report rather than what the compound is claimed to do.
Research compounds attract claims that outrun their evidence. Below are the ones most often encountered for TB-500 Fragment 17-23, set against what the papers cited on this page actually report. Where the record is thin or contested, that is stated rather than smoothed over.
TB-500 Fragment 17-23 is also referred to as TB frag, the 17-23 fragment, and technically as Tβ4 17-23 (Leu-Lys-Lys-Thr-Glu-Thr-Gln).
TB-500 Fragment 17-23 is commonly described online in connection with faster healing from injury and improved recovery. In the research literature the same compound is filed under actin-binding domain structure-activity research, dermal wound-repair models and cell-migration and tissue-repair frameworks.
The 4 papers cited on this page, published between 2003 and 2018 (1 in animal models) describe laboratory and animal work. None reports a controlled trial in humans. Findings in cell culture or in a rodent model describe what happened in that system; they do not establish that the same occurs in humans, and this compound is not approved for human use.
Nothing above is a statement of what this material does. It is a summary of what has been published and what has not. Eppix Labs supplies research materials only and provides no dosing, administration or protocol guidance.
Verification for TB-500 Fragment 17-23 is per lot, not per product. The current 10mg lot TBFR-CA-26G-10 returned 99.94% purity, 11.12 mg measured, 111.2% of the labelled 10 mg, assayed by Janoshik. Those figures are the laboratory's, published in full rather than reduced to a badge.
Purity is half the number. It states what fraction of the material in the vial is TB-500 Fragment 17-23; it says nothing about how much material is in the vial, and a short-filled vial can return a purity result that is entirely accurate. The figure that answers the second question is measured mass against expected content — for TB-500 Fragment 17-23, this lot measured 111.2% of its labelled 10 mg. Both numbers are published for every lot, whichever way they fall.
The lot code printed on the vial matches the code on the certificate for TB-500 Fragment 17-23. Matching the two is what confirms the unit in hand came from the batch that was tested — a certificate not tied to a lot code proves nothing about any particular unit.
Researchers who buy TB-500 Fragment 17-23 in Canada through Eppix Labs receive the lot described by the certificate above: the code printed on the vial label is the code on the certificate, and both are searchable on the batch verification page.
TB-500 Fragment 17-23 is supplied as lyophilized powder. In the dry state the material is comparatively stable, which is why it ships at ambient temperature without a cold chain; once reconstituted it is a peptide in solution and the handling constraints tighten considerably. At 7 residues it is short enough to be produced by solid-phase synthesis, and the published sequence on this page is what an identity assay is checked against.
Repeated freeze-thaw cycling is the handling error most likely to degrade material of this class, because each cycle concentrates solutes at the ice boundary. Where a protocol calls for the same vial across multiple sessions, the published literature generally describes aliquoting after reconstitution rather than re-freezing the whole volume.
Vials may appear empty on arrival. Lyophilized material collects at the base of the vial and is often not visible until the vial is inspected under direct light.
Reconstitution materials are sourced separately. The reconstitution calculator on this site works out concentrations for a given volume, but it is an arithmetic tool for laboratory record-keeping and not a protocol.
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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