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The three mammalian isoforms of TGF-β, namely TGF-β1, β2, and β3, activate the same receptor and provoke similar biological responses. These versatile cytokines oversee cell proliferation, growth, differentiation, and motility, along with orchestrating the synthesis and placement of the extracellular matrix. They play vital roles in various physiological activities like embryogenesis, tissue restructuring, and wound healing. Typically, they are secreted in latent complexes, stored at cell surfaces and within the extracellular matrix.
For the biologically active TGF-β isoform to emerge from its latent state, the complex undergoes proteolytic processing or experiences conformational shifts induced by proteins like thrombospondin-1. While the precise role of TGF-β3 remains unclear, its expression pattern hints at involvement in regulating certain developmental processes.
Recombinant Human TGF-β3 comprises two identical 112 amino acid polypeptide chains connected by a single disulfide bond, weighing 25.0 kDa.
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