TGFBI (human, recombinant)

TGF-β-induced ig-h3 precursor (TGFBI) is a TGF-β-responsive extracellular protein.¹ 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.¹ 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.² Its production is induced by TGF-β, and it inhibits cell adhesion by interacting with collagens, fibronectin, laminin, and vitronectin.^2,3 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.³ Mutations in TGFBI are associated with corneal dystrophies and lead to protein aggregation in the cornea and severe visual impairment or blindness.^2,3 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.

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1. Runager, K., Enghild, J.J., and Klintworth, G.K. Focus on molecules: Transforming growth factor beta induced protein (TGFBIp). Exp. Eye Res. 87(4), 298-299 (2008).

2. Andersen, R.B., Karring, H., Møller-Pedersen, T., et al. Purification and structural characterization of transforming growth factor beta induced protein (TGFBIp) from porcine and human corneas. Biochemistry 43(51), 16374-16384 (2004).

3. Corona, A., and Blobe, G.C. The role of the extracellular matrix protein TGFBI in cancer. Cell. Signal. 84, 110028 (2021).