TB-500 Fragment 17-23
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.
Mix & Match
1 vial — no vial discount yet.
Add 2 more vials for 5% off.
After that, 10% at 5 vials, 20% at 10 vials.
This product is intended strictly for laboratory research use within the United States. It is not approved by the FDA 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 U.S. federal, state, and local 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.
Coming Soon
The certificate of analysis for the 10mg lot is being finalised and will be published here as soon as the lab returns it.
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.
Actin-binding domain structure-activity research
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.
- Philp, D. et al. (2003) — Thymosin beta 4 and a synthetic peptide containing its actin-binding domain promote dermal wound repair in db/db diabetic mice and in aged mice
- Shah, R. et al. (2018) — Thymosin β4 inhibits PDGF-BB induced activation, proliferation, and migration of human hepatic stellate cells via its actin-binding domain
Dermal wound-repair models
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.
- Philp, D. et al. (2003) — Thymosin beta 4 and a synthetic peptide containing its actin-binding domain promote dermal wound repair in db/db diabetic mice and in aged mice
Cell-migration and tissue-repair frameworks
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.
- Shah, R. et al. (2018) — Thymosin β4 inhibits PDGF-BB induced activation, proliferation, and migration of human hepatic stellate cells via its actin-binding domain
- Philp, D. et al. (2003) — Thymosin beta 4 and a synthetic peptide containing its actin-binding domain promote dermal wound repair in db/db diabetic mice and in aged mice
Analytical characterization of TB-500 preparations
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.
Every lot of TB-500 Fragment 17-23 is independently assayed before it is released, and the certificate for the lot shipped is published rather than summarised. Where a certificate for a current lot is not yet posted, the lot has not yet been released against it.
Researchers who buy TB-500 Fragment 17-23 in the United States through Eppix Labs receive a batch-labelled vial whose certificate is published against that lot code, so the material can be matched to its analysis rather than to a generic specification.
- Lyophilized storage
- −20 °C long-term; stable at room temperature in transit
- After reconstitution
- 2–8 °C
- Light
- Protect from UV and direct light
- Freeze-thaw
- Avoid repeated cycles
- Vehicle
- Bacteriostatic water in most published protocols
- Format
- Lyophilized powder
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.
- 1 × sealed glass vial in the strength selected (10mg / Single Vial, 10mg / 5-Pack, 10mg / 10-Pack available), batch-labelled
- Batch documentation for the lot shipped, once its certificate is published
- Discreet outer packaging with no product names on the exterior
- FedEx, tracked, typically 1–3 business days domestically
- Bacteriostatic water or any other reconstitution vehicle
- Syringes, needles or filters
- Dosing, administration or protocol guidance of any kind
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
PubMedRelated
You May Also Like
Next-generation GLP receptor agonist studied for metabolic signaling and nutrient partitioning pathways
From$79.99
Dual incretin receptor agonist studied for glucose regulation, metabolic signaling, and weight pathway research
From$39.99
Studied in metabolic research for its effects on glucose regulation, appetite signaling, and energy balance.
From$59.99
Long-acting amylin analog engineered for appetite signaling, metabolic control, and energy balance research
From$99.99