Thymosin beta 4 Recombinant Protein

Thymosin-β4 is a small, actin-sequestering protein belonging to the thymosin-β 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-β4 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-β4 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 Human/Murine/Rat Thymosin-β4 is a 5.2 kDa glycoprotein containing 45 amino acid residues.

The recombinant protein is stable for at least 2 years from date of receipt at -20˚ C. Reconstituted protein is stable for at least 3 months when stored in working aliquots with a carrier protein at -20˚ C. As with any protein, exposing the recombinant protein to repeated freeze / thaw cycles is not recommended. When working with proteins care should be taken to keep recombinant protein at a cool and stable temperature.