| Products/Services Used | Details | Operation |
|---|---|---|
| Custom Vector Construction | In contrast, stable transfection of these lines with a HA-GARP construct with a blastacidin resistance cassette followed by selection and sorting resulted in high surface expression of TGF-b1/GARP or TGF-b1 (R249A)/GARP, as measured by anti-HA (clone 5E11D8, GenScript, Piscataway, NJ) or anti LAP | Get A Quote |
Integrin αvβ8 binds with exquisite specificity to latent transforming growth factor-β (L-TGF-β). This binding is essential for activating L-TGF-β presented by a variety of cell types. Inhibiting αvβ8-mediated TGF-β activation blocks immunosuppressive regulatory T cell differentiation, which is a potential therapeutic strategy in cancer. Using cryo-electron microscopy, structure-guided mutagenesis, and cell-based assays, we reveal the binding interactions between the entire αvβ8 ectodomain and its intact natural ligand, L-TGF-β, as well as two different inhibitory antibody fragments to understand the structural underpinnings of αvβ8 binding specificity and TGF-β activation. Our studies reveal a ... More
