Thymosin β4 Acetate promotes wound healing, tissue repair, and cell regeneration. Buy Thymosin beta 4 peptide powder for research on recovery and regenerative medicine.
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
Thymosin β4 Acetate is a synthetic peptide corresponding to the naturally occurring Thymosin beta 4, a highly conserved 43-amino acid protein found in many mammalian tissues. As a member of the β-thymosin family, it plays a critical role in actin sequestration and cytoskeletal organization, making it a subject of intense study in cell biology, wound healing, and tissue regeneration research. The acetate form offers enhanced stability and solubility, facilitating its use in a wide range of experimental settings. Its biochemical significance extends to the modulation of cell migration, differentiation, and angiogenesis, positioning it as a valuable tool for elucidating cellular mechanisms and pathways.
Cell motility research: Thymosin β4 Acetate is widely used in studies investigating the regulation of cell movement, particularly due to its ability to bind G-actin and prevent actin polymerization. By modulating the availability of actin monomers, the peptide enables researchers to dissect the molecular events underlying cytoskeletal dynamics and cellular migration. This is especially relevant in the context of embryogenesis, tissue repair, and metastasis models, where precise control of cell motility is essential for experimental reproducibility and mechanistic insight.
Angiogenesis assays: The peptide is frequently applied in in vitro and in vivo models to explore the molecular mechanisms driving new blood vessel formation. Its role in promoting endothelial cell migration and capillary-like structure formation makes it a key reagent for studying angiogenic processes. Researchers utilize Thymosin β4 derivatives to investigate the signaling pathways involved in vascular development, tissue engineering, and regenerative biology, contributing to a deeper understanding of how cellular microenvironments influence neovascularization.
Wound healing and tissue regeneration studies: Thymosin β4 Acetate serves as a model peptide for elucidating the cellular and molecular responses involved in tissue repair. Its capacity to modulate inflammation, enhance keratinocyte and fibroblast migration, and influence extracellular matrix remodeling is leveraged in a variety of experimental systems, including scratch assays, organotypic cultures, and three-dimensional tissue models. The peptide's multifaceted actions provide insight into the coordinated events that underpin efficient tissue regeneration.
Peptide signaling pathway analysis: Researchers employ Thymosin β4 Acetate to probe intracellular signaling networks associated with cell survival, differentiation, and stress responses. Its interactions with actin and other cytoskeletal proteins allow for the investigation of downstream effectors such as integrins, kinases, and transcription factors. By incorporating this peptide into biochemical and proteomic workflows, scientists can map the influence of cytoskeletal regulators on gene expression and cellular adaptation to environmental cues.
Peptide synthesis and structural studies: Thymosin β4 Acetate is also valuable as a reference standard and substrate in peptide chemistry and structural biology. Its well-defined sequence and established biological activity make it suitable for validating analytical methods, optimizing peptide synthesis protocols, and serving as a model for studying peptide folding, stability, and interactions. Structural investigations utilizing techniques such as NMR spectroscopy or X-ray crystallography benefit from the availability of this synthetic peptide, enabling detailed characterization of its conformational properties and binding interfaces.
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.
1. Adipose tissue is a key organ for the beneficial effects of GLP-2 metabolic function
3. SERS spectrum of the peptide thymosin‐β4 obtained with Ag nanorod substrate
5. Cell-based adhesion assays for isolation of snake venom’s integrin antagonists
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