Recombinant Human TGFB1 protein

Transforming growth factor beta 1 (TGFB1) is a multifunctional cytokine belonging to the TGF-β superfamily, first identified in the 1980s for its ability to induce anchorage-independent growth in fibroblasts. It plays pivotal roles in regulating cell proliferation, differentiation, apoptosis, immune response, and extracellular matrix remodeling. Mature TGFB1 is a 25 kDa homodimeric protein derived from proteolytic cleavage of a latent precursor. Its signaling occurs through serine/threonine kinase receptors (TGFBR1/2), activating SMAD-dependent and non-canonical pathways (e.g., MAPK, PI3K) to mediate context-dependent cellular responses.

Recombinant TGFB1 is produced using mammalian expression systems (e.g., CHO or HEK293 cells) to ensure proper post-translational modifications, particularly the formation of disulfide-linked dimers critical for bioactivity. The protein is typically purified via chromatography and rigorously tested for endotoxin levels and functional consistency using cell-based assays like luciferase reporter systems or SMAD phosphorylation analyses.

In research, recombinant TGFB1 is widely used to study mechanisms underlying fibrosis, cancer progression (dual roles in tumor suppression and metastasis), immune tolerance, and wound healing. It serves as a therapeutic target in clinical trials for diseases ranging from idiopathic pulmonary fibrosis to advanced cancers, with inhibitors like monoclonal antibodies and kinase modulators in development. However, its pleiotropic nature – acting as both a tumor suppressor in early-stage cancers and a promoter of invasion in advanced malignancies – underscores the complexity of harnessing TGFB1 signaling therapeutically. Recent advances in structural biology and conditional knockout models have refined understanding of its spatiotemporal regulation, driving innovation in tissue-specific drug delivery strategies.