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TB-500

TB-500 is a synthetic 17-amino-acid acetylated peptide corresponding to a fragment of thymosin β4 (Tβ4), the small actin-sequestering protein expressed broadly across mammalian tissues. Studied in preclinical wound-healing, cardiac-repair, corneal-healing, and limb-ischemia models with G-actin sequestration and integrin-linked kinase signalling as the dominant mechanistic findings.

Definition

TB-500 — full name N-acetyl thymosin β4 LKKTETQ fragment, in common research-supply usage referring to either the full 43-amino-acid synthetic thymosin β4 sequence or the active LKKTETQ fragment — is the research-supply form of the small actin-binding protein thymosin β4. The parent protein is one of the most abundant intracellular polypeptides in mammalian cells, where it functions as a G-actin-sequestering protein that maintains a pool of unpolymerised actin monomers available for cytoskeletal remodelling. Tβ4 carries an N-terminal acetylation that is reproduced on the synthetic supply form.

The compound is studied across multiple preclinical research literatures — dermal wound healing, corneal-epithelial repair, cardiac repair after ischemic injury, limb-ischemia revascularisation, hair-follicle biology, kidney injury, and inflammatory-disease models. No major regulatory authority has cleared the compound for therapeutic use in humans or animals. Research-grade TB-500 is supplied as a lyophilised powder for laboratory research applications only.

How TB-500 is studied in peptide research

The canonical mechanism for TB-500’s tissue-repair findings is twofold: G-actin sequestration via a defined actin-binding site on the peptide (PMID 11579089), and activation of integrin-linked kinase with downstream PI3K-Akt and survival signalling documented in cardiac and endothelial cell models (PMID 15565145). The endothelial-cell migration literature dates to the original Malinda HUVEC work (PMID 9194528). Limb-ischemia and cardiac-repair findings extend the framing across in-vivo revascularisation models (PMID 32945357, PMID 22236126). Dermal-healing review consolidates the published wound-healing literature for the compound (PMID 27450738).

TB-500 and BPC-157 are frequently paired in research-handling contexts because their mechanisms are mechanistically distinct but functionally complementary — BPC-157 acts via VEGFR2-Akt-eNOS angiogenic signalling on the endothelium, while TB-500 acts via integrin-linked kinase and actin-cytoskeletal remodelling — and the combined-research literature is the basis for the Wolverine Stack research bundle in the Ronin catalog. For deeper coverage of the combined research see the BPC-157 and TB-500 combined research studies article and the BPC-157 vs TB-500 research comparison.

Related terms

Where TB-500 appears in the Ronin catalog

References

  1. Malinda KM et al. Thymosin beta 4 stimulates directional migration of human umbilical vein endothelial cells. FASEB J 1997;11(6):474-481. [PMID 9194528]
  2. Yarmola EG et al. Formation and implications of a ternary complex of profilin, thymosin beta 4, and actin. J Biol Chem 2001;276(49):46094-46101. [PMID 11579089]
  3. Bock-Marquette I et al. Thymosin beta4 activates integrin-linked kinase and promotes cardiac cell migration, survival and cardiac repair. Nature 2004;432(7016):466-472. [PMID 15565145]
  4. Dubé KN et al. Thymosin β4 protein therapy for cardiac repair. Curr Pharm Des 2012;18(6):813-817. [PMID 22236126]
  5. Kleinman HK et al. Thymosin β4 Promotes Dermal Healing. Vitam Horm 2016;102:251-275. [PMID 27450738]
  6. Lv S et al. Thymosin-β 4 induces angiogenesis in critical limb ischemia mice via regulating Notch/NF-κB pathway. Int J Mol Med 2020;46(4):1347-1358. [PMID 32945357]

Glossary entries describe research-context use of peptide-research terminology. They do not constitute medical, veterinary, or clinical advice. TB-500 is sold strictly as a research-grade reagent for laboratory and bench research applications.

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