Thymosin-beta 4 is a small, actin-sequestering protein belonging to the thymosin-beta family that is found at high concentrations within the spleen, thymus, and peritoneal macrophages, where it is most notably responsible for the organization of cytoskeletal structure. In mammalian tissues, this protein acts as a modulator for the polymerization/depolymerization of actin through the formation of a 1:1 complex with the monomer G (globular)-actin, and inhibits actin's polymerization to form F (filamentous) actin, which together with other proteins binds microfilaments to construct the cytoskeleton. Commonly found at significant quantities within the brain, lungs, liver, kidneys, testes, and heart, Thymosin-beta 4 has also been shown to be synthesized by cells unrelated to the reticuloendothelial system, such as myoblasts and fibroblasts, and expressed at irregular levels by several hemopoietic cell lines, malignant lymphoid cells and myeloma cells. In addition to regulating actin polymerization, research has also found Thymosin-beta 4 to stimulate the secretion of hypothalamic luteinizing hormone-releasing hormone and luteinizing hormone, inhibit the migration of peritoneal macrophages, induce phenotypic changes in T cell lines during early host defense mechanisms, and inhibit the progression of hematopoietic pluripotent stem cells into the s-phase.
Recombinant protein corresponding to human Thymosin Beta 4, a single non-glycosylated polypeptide chain containing 43aa, expressed in E. coli.
Suitable for use in SDS-PAGE. Other applications not tested.
Optimal dilutions to be determined by the researcher.
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Storage and Stability:
Lyophilized powder may be stored at -20°C. Reconstitute with sterile dH2O, 0.1% BSA. Aliquot to avoid repeated freezing and thawing. Store at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.