TGFBI Human, 182 a.a.

Transforming Growth Factor Beta (TGF-β) is a multifunctional cytokine that plays a crucial role in regulating various cellular processes, including cell growth, differentiation, apoptosis, and extracellular matrix production. The TGF-β family consists of over 30 related cytokines, which act in a context-dependent manner . One of the key proteins in this family is the Transforming Growth Factor Beta-Induced (TGFBI) protein, which is encoded by the TGFBI gene.

The TGFBI protein, also known as BIGH3, is a 68 kDa protein that contains an RGD (Arg-Gly-Asp) motif, which is found in many extracellular matrix proteins and is involved in cell adhesion . This protein binds to type I, II, and IV collagens and plays a role in cell-collagen interactions. It is induced by TGF-β and acts to inhibit cell adhesion . Mutations in the TGFBI gene are associated with various types of corneal dystrophy, including Thiel-Behnke and Reis-Bucklers types .

The TGF-β signaling pathway is a critical regulator of numerous cellular processes. It functions through both canonical SMAD-mediated processes and noncanonical pathways involving MAPK cascades, PI3K/AKT, Rho-like GTPases, and NF-κB signaling . This intricate signaling system is finely tuned by interactions between canonical and noncanonical pathways and plays key roles in both physiological and pathological conditions, including tissue homeostasis, fibrosis, and cancer progression .

TGF-β signaling has paradoxical actions. Under normal physiological conditions, it promotes cell quiescence and apoptosis, acting as a tumor suppressor . However, in pathological states such as inflammation and cancer, it triggers processes that facilitate cancer progression and tissue remodeling, thus promoting tumor development and fibrosis . The dual roles of TGF-β signaling in both fibrosis and cancer highlight its complex behavior across different cellular contexts .

Human recombinant TGFBI (182 amino acids) is a truncated form of the full-length TGFBI protein. Recombinant proteins are produced through recombinant DNA technology, which involves inserting the gene encoding the protein of interest into an expression system, such as bacteria or mammalian cells, to produce the protein in large quantities. This technology allows for the production of proteins that are identical to their natural counterparts, enabling researchers to study their functions and potential therapeutic applications.

Recombinant TGFBI proteins are used in various research applications to study their roles in cell adhesion, migration, and signaling. They are also used to investigate the mechanisms underlying corneal dystrophies and other diseases associated with TGFBI mutations. Additionally, TGFBI proteins are being explored as potential therapeutic targets for conditions such as fibrosis and cancer, where TGF-β signaling plays a significant role .