TGFBI (human, recombinant)

TGF-beta-induced ig-h3 precursor (TGFBI) is a TGF-beta-responsive extracellular protein. It is composed of an N-terminal signal peptide and cysteine-rich domain, four fasciclin 1 (FAS) repeats, and a C-terminal arginine-glycine-aspartate (RGD) motif. TGFBI is expressed in the mesenchyme during development and in the extracellular matrix in many tissues, including the cornea, bone, and kidney, in the adult. Its production is induced by TGF-beta, and it inhibits cell adhesion by interacting with collagens, fibronectin, laminin, and vitronectin. In animal models, TGFBI acts as a tumor suppressor during cancer initiation and promotes progression during later stages, but both effects are dependent on cancer type. Mutations in TGFBI are associated with corneal dystrophies and lead to protein aggregation in the cornea and severe visual impairment or blindness. Cayman's TGFBI (human, recombinant) protein consists of 671 amino acids, has a calculated molecular weight of 74 kDa, and a predicted N-terminus of Gly24 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is approximately 65 kDa due to glycosylation. Glycosylated proteins or proteins with compact beta-sheet domains, such as TGFBI, bind less SDS or retain partial tertiary structure even under reducing conditions.