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Description
Ultra-LEAF? Purified anti-human/mouse TGF-β1. TGF-β1 is a multifunctional cytokine that plays pivotal roles in diverse biological processes. TGF-β1 is synthesized as a 390 amino acid precursor that is cleaved by furin, localized in the trans-Golgi network, in residue 278.? Furin processes the TGF-β1 precursor at the carboxyl side of the consensus sequence RHRR which precedes the NH2-terminal Ala 279 residue of the mature TGF-β1. The TGF-β1 precursor includes?the latency-associated peptide (LAP dimer) in the N-terminal portion and the 25 kD portion that constitutes the mature TGF-β1 in the C-terminal. LAP dimer and the TGF-β1 mature protein remain non-covalently associated after furin cleavage and this complex does not bind to the TFG-β1 receptor. In addition, the TGF-β1 latent complex is joined covalently through LAP to LTBP. The TGF-β1 active form requires dissociation from LAP. Some activators can release TGF-β1 from LAP such as thrombospondin-1, reactive oxygen species, and the integrins avb6 and avb8.Mouse TGF-β1 converts na?ve T cells into regulatory T (Treg) cells that prevent autoimmunity. Although human TGF-β1 is widely used for inducing FOXP3+ in vitro, it might not be an essential factor for human Treg differentiation. Th17 murine can be induced from na?ve CD4+ T cells by the combination of TGF-β1 and IL-6 or IL-21. Nevertheless, the regulation of human Th17 differentiation is distinct. TGF-β1 seems to have dual effects on human Th17 differentiation in a dose-dependent manner. While TGF-β1 is required for the expression of RORgt, in human na?ve CD4+ T cells from cord blood, TGF-β1 can inhibit the function of RORgt at high doses. By using serum-free medium, it has been clarified that the optimum conditions for human Th17 differentiation are TGF-β1, IL-1b, and IL-2 in combination with IL-6, IL-21, or IL-23.