Recombinant Mouse TGF-béta1 (carrier-free) 25 µg

TGF-β1 is synthesized in cells as a 390-amino acid protein. Furin cleaves the protein at residue 278, yielding an N-terminal cleavage product which corresponds to the latency-associated peptide (LAP), and the 25 kD C-terminal portion of the precursor constitutes the mature TGF-β1. In addition to furin, some other activators can release TGF-β from LAP. TGF-β activators include proteases that degrade LAP, thrombospondin-1, reactive oxygen species, and the integrins αvβ6 and αvβ8. TGF-β is involved in regulating homeostasis of different Treg populations (naïve, inducible, peripheral) in both mouse and humans, although its specific roles remain the subject of active investigation. Th17 murine can be induced from naïve 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 RORct, in human naive CD4+ T cells from cord blood, TGF-β1 can inhibit the function of RORct at high doses. By using serum-free medium, it has been clarified that the optimum conditions for human Th17 differentiation are TGF-β1, IL-1β, and IL-2 in combination with IL-6, IL-21 or IL-23.;