T cell Ig- and mucin-domain-containing molecules (TIMs) are a family of transmembrane proteins expressed by various immune cells. TIM-3 is an inhibitory molecule that is induced following T cell activation. TIM-3 is expressed by exhausted T cells in the settings of chronic infection and cancer, and tumor-infiltrating T cells that co-express PD-1 and TIM-3 exhibit the most severe exhausted phenotype. Tumor-infiltrating dendritic cells also express TIM-3. TIM-3 expression on DCs was found to suppress innate immunity by reducing the immunogenicity of nucleic acids released by dying tumor cells. Research studies show that heterodimerization of TIM-3 with CEACAM-1 is critical for the inhibitory function of TIM-3, and co-blockade of TIM-3 and CEACAM-1 enhanced antitumor responses in a mouse model of colorectal cancer. Its binding to Galectin-9 induces a range of immunosuppressive functions which enhance immune tolerance and inhibit anti-tumor immunity. TIM-3 ligation attenuates CD8+ and Th1 cell responses and promotes the activity of Treg and myeloid derived suppressor cells. In addition, dendritic cell-expressed TIM-3 dampens inflammation by enabling the phagocytosis of apoptotic cells and the cross-presentation of apoptotic cell antigens.
Recombinant Human TIM-3 Fc Chimera produced in HEK293 cells is a polypeptide chain containing 412 amino acids with the C-terminal human IgG1 Fc fragment. A fully biologically active molecule, rhTIM-3 has a molecular mass of 60-65 kDa analyzed by reducing SDS-PAGE and is obtained by chromatographic techniques at GenScript.
Recombinant Human EGF-R/ErbB1 Fc Chimera produced in CHO cells is a polypeptide chain containing 854 amino acids with the C-termimal human IgG1 Fc fragment. A fully biologically active molecule, rhEGF-R/ErbB1 has a molecular mass of 12-125 kDa analyzed by reducing SDS-PAGE and is obtained by chromatographic techniques at GenScript.