TB500 Fragment (17-13)

TB500 Fragment (17-13) is a synthetic heptapeptide corresponding to residues 17-23 of thymosin beta-4, the central actin-binding motif of the parent 43-residue sequence. With the amino acid sequence LKKTETQ, this research peptide is supplied as a defined active-site fragment for use in actin-binding research, structure-activity research, and cellular-process research in controlled laboratory settings.

The LKKTETQ sequence has been characterized in laboratory research studies as the region of thymosin beta-4 that contributes most directly to monomeric G-actin engagement. Mutational and structural research has mapped this heptapeptide to the central actin-binding region of the parent molecule, and synthetic LKKTETQ has been investigated as a discrete research compound that retains key actin-binding research activity in cellular models (Sosne et al., 2003, FASEB Journal; Sosne et al., 2010, Annals of the New York Academy of Sciences).

In laboratory research studies, TB500 Fragment (17-13) is used to investigate how an isolated actin-binding domain compares to the full-length thymosin beta-4 sequence in cytoskeletal dynamics research, cellular-process research, and inflammatory-pathway research. The defined seven-residue structure also makes it a useful comparator in structure-activity research alongside TB-500 and other Tβ4-derived research peptides.

The peptide is supplied as a lyophilized powder to ensure optimal stability during storage and handling.

Thymosin beta-4 is a 43-amino-acid intracellular actin-sequestering research peptide widely distributed across mammalian cell types. Structural research has identified a central region spanning residues 17-23 (sequence LKKTETQ) as the principal actin-binding motif within the parent peptide. This heptapeptide is conserved across beta-thymosin family members and has been mapped in mutational and crystallographic research as a key contact region for monomeric G-actin.

TB500 Fragment (17-13) is supplied as a synthetic version of this central actin-binding motif. Investigation of the heptapeptide as a standalone research compound has supported laboratory research studies of structure-activity research, in which the isolated active-site fragment is compared to the full-length thymosin beta-4 sequence in actin-binding research and cellular-process research models.

By supplying a discrete, sequence-defined actin-binding fragment, TB500 Fragment (17-13) enables laboratory research studies that distinguish the contribution of the central actin-binding motif from the broader cytoskeletal dynamics research activity of the full-length parent peptide. This makes it a valuable reference compound in comparative thymosin beta-4 research and structure-function research.

1. Actin-Binding Research at the Central Tβ4 Motif

TB500 Fragment (17-13) corresponds to the central actin-binding motif of thymosin beta-4 (residues 17-23, LKKTETQ). In laboratory research studies, this heptapeptide engages monomeric G-actin and contributes to research on how the isolated actin-binding domain modulates cytoskeletal dynamics research compared with the full-length parent peptide.

2. Structure-Activity Research

By isolating residues 17-23 of thymosin beta-4, TB500 Fragment (17-13) supports structure-activity research that distinguishes the contribution of the central actin-binding motif from the broader sequence context of the full-length peptide. Comparative research with TB-500 enables investigation of how active-site fragments perform in actin-binding research and cellular-process research models.

3. Cellular-Process Research Signalling

Laboratory research studies have examined how the LKKTETQ heptapeptide engages cellular-process research models, including endothelial and epithelial migration research. These investigations support research on actin-binding domain pharmacology in cellular-pathway research.

4. Inflammatory-Pathway Research

Research models have investigated how the LKKTETQ fragment modulates inflammatory-pathway research markers and cytokine-signalling research, providing a defined active-site research tool alongside the full-length thymosin beta-4 sequence.

Research Applications

Conclusion

TB500 Fragment (17-13) is a defined synthetic heptapeptide corresponding to the central actin-binding motif of thymosin beta-4 (residues 17-23, LKKTETQ). Its discrete sequence makes it a valuable reference compound in actin-binding research, structure-activity research comparing active-site fragments with the full-length parent peptide, and cellular-process research. By supplying the isolated central actin-binding region, TB500 Fragment (17-13) supports laboratory research studies of cytoskeletal dynamics research and thymosin beta-4 active-site pharmacology.

Research Use Disclaimer

This product is intended for research and laboratory use only. It is designed exclusively for in vitro research purposes. All information provided is for educational and research reference only. This product is not intended for human or animal use. It is not a drug, food, or cosmetic and must not be marketed, labeled, or used as such. Use and handling are restricted to trained and qualified professionals.