
Cytoprotective Peptides
TB-500
5mgC₂₁₂H₃₅₀N₅₆O₇₈S
Key Research Findings
- Goldstein et al. — characterisation of the Tβ4 sequence and actin-binding domain.
- Published cell-culture assays on keratinocyte and endothelial cell migration.
- Storage stability characterised in lyophilised form at −20 °C.
Overview
TB-500 is a synthetic peptide supplied at the molecular weight of the full 43-residue thymosin beta 4 sequence, the actin-sequestering peptide originally isolated from calf thymus. Thymosin beta 4 is among the most abundant peptides in mammalian cells and the principal reservoir of monomeric G-actin in the cytoplasm. The name TB-500 is used commercially for both the full sequence and for shorter fragments carrying the LKKTETQ actin-binding motif, so the molecular weight on the quick facts panel is worth checking against whatever a protocol calls for. We supply it as a lyophilised powder at 5mg per vial with an independent certificate of analysis.
Mechanism of Action
The defining activity is actin sequestration. Cassimeris and colleagues showed that thymosin beta 4 holds the majority of unpolymerised G-actin in resting human polymorphonuclear leukocytes, acting as a buffer that keeps monomer available without allowing spontaneous filament assembly [1]. Because the actin cytoskeleton drives cell shape and locomotion, most in-vitro work with this peptide concerns migration assays. Ryu and colleagues reported cooperation between the peptide and hypoxia inducible factor 1 alpha in tumour cell migration models [2], and Moon and colleagues characterised it as hypoxia responsive in its own right [3]. The peptide is water soluble and does not require an organic co-solvent, which makes it straightforward to reconstitute compared with more hydrophobic sequences. Not intended for human or veterinary use.
Research Effects
Actin Polymerisation
Extensive ResearchReported in cell-culture assays as a G-actin sequestering peptide affecting F-actin assembly.
Cell-Migration Assays
Moderate ResearchPublished in-vitro studies report effects on keratinocyte and endothelial cell migration.
Cytokine-Expression Studies
Moderate ResearchAnimal-model studies report changes in TNF-α and related cytokine expression under controlled conditions.
References
- [1]Cassimeris L, Safer D, Nachmias VT, Zigmond SH. Thymosin beta 4 sequesters the majority of G-actin in resting human polymorphonuclear leukocytes. J Cell Biol. 1992. PMID 1447300 · doi:10.1083/jcb.119.5.1261
- [2]Ryu YK, Lee YS, Lee GH, et al.. Cooperation of actin-sequestering protein, thymosin beta-4 and hypoxia inducible factor-1alpha in tumor cell migration. Oncol Rep. 2010. PMID 20878135 · doi:10.3892/or_00000997
- [3]Moon EY, Song JH, Yang KH. Actin-sequestering protein, thymosin beta-4, is a novel hypoxia responsive regulator. Clin Exp Metastasis. 2010. PMID 20821256 · doi:10.1007/s10585-010-9350-z
Cited for the molecular pathways described above. Listing a study is not a claim about any outcome in humans.
Laboratory Research Only — All information on this page is provided for scientific research purposes only. This is a certified reference material sample sold and distributed for laboratory research only.
Quick Facts
Research Status Key
Featured in Bundles
TB-500 is included in the following Zenterex research peptide bundles.
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