Thymosin β4 Acetate

Thymosin β4 is a 43 amino acid peptide which is regarded as the main intracellular G-actin sequestering peptide. Extracellular thymosin β4 may contribute to physiological processes such as angiogenesis, wound healing and regulation of inflammation.

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CAT No: 10-101-35

CAS No: 77591-33-4 (net)

Synonyms/Alias: Fx Peptide; Thymosin beta4; Thymosin beta 4; Thymosin beta(4); Thymosin β4; Tβ4; Tb4; Thymosin beta-4; Thymosin β-4; Thymosin β 4; TB-500

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M.F/Formula	C212H350N56O78S
M.W/Mr.	4963.49
Sequence	Ac-Ser-Asp-Lys-Pro-Asp-Met-Ala-Glu-Ile-Glu-Lys-Phe-Asp-Lys-Ser-Lys-Leu-Lys-Lys-Thr-Glu-Thr-Gln-Glu-Lys-Asn-Pro-Leu-Pro-Ser-Lys-Glu-Thr-Ile-Glu-Gln-Glu-Lys-Gln-Ala-Gly-Glu-Ser-OH
Labeling Target	G-actin monomers
Application	Thymosin β4 has been tested in multicenter trials in patients with bed sores, ulcers caused by venostasis, epidermolysis bullosa simplex and chronic neurotrophic corneal epithelial defects. And it was found to promote repair.
Biological Activity	Thymosin β4 Acetate is a 43 amino acid peptide which is regarded as the main intracellular G-actin sequestering peptide.
Areas of Interest	Cosmetic Peptides & Dermatology Inflammation Research Regenerative Medicine

Source#	Synthetic
Solubility	−20°C
BoilingPoint	N/A
References	Thymosin-β4 (Tβ4) sequesters actin monomers to help maintain the high concentrations of unpolymerized actin in higher eukaryotic cells. Despite more than two decades of research investigating the Tβ4–actin interaction, the X-ray structure of the full-length Tβ4:actin complex remained unresolved. Here, we report two X-ray structures of Tβ4:actin complexes. The first structure reveals that Tβ4 has two helices that bind at the barbed and pointed faces of actin, whereas the second structure displays a more open actin nucleotide binding cleft and a disruption of the Tβ4 C-terminal helix interaction. These structures, combined with biochemical assays and molecular dynamics simulations, reveal how Tβ4 prevents monomeric actin from joining actin filaments but participates in the exchange of actin with profilin to ensure controlled actin polymerization. Xue, B., Leyrat, C., Grimes, J. M., & Robinson, R. C. (2014). Structural basis of thymosin-β4/profilin exchange leading to actin filament polymerization. Proceedings of the National Academy of Sciences, 111(43), E4596-E4605. The downstream consequences of inflammation in the adult mammalian heart are formation of a non-functional scar, pathological remodelling and heart failure. In zebrafish, hydrogen peroxide released from a wound is the initial instructive chemotactic cue for the infiltration of inflammatory cells, however, the identity of a subsequent resolution signal(s), to attenuate chronic inflammation, remains unknown. Here we reveal that thymosin β4-sulfoxide lies downstream of hydrogen peroxide in the wounded fish and triggers depletion of inflammatory macrophages at the injury site. This function is conserved in the mouse and observed after cardiac injury, where it promotes wound healing and reduced scarring. In human T-cell/CD14+ monocyte co-cultures, thymosin β4-sulfoxide inhibits interferon-γ, and increases monocyte dispersal and cell death, likely by stimulating superoxide production. Thus, thymosin β4-sulfoxide is a putative target for therapeutic modulation of the immune response, resolution of fibrosis and cardiac repair. Evans, M. A., Smart, N., Dubé, K. N., Bollini, S., Clark, J. E., Evans, H. G., ... & Mills, K. (2013). Thymosin β4-sulfoxide attenuates inflammatory cell infiltration and promotes cardiac wound healing. Nature communications, 4, 2081.
Melting Point	N/A

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