Galectin-9 is a cytoplasmic protein that contains two galectin domains. Galectin-9 is an S-type lectin that is over-expressed in Hodgkin's disease tissue. Galectin-9 binds galactosides and has high affinity for the Forssman pentasaccharide. Galectin-9 plays a role in thymocyte-epithelial interactions relevant to the biology of the thymus and Inhibits cell proliferation. Galectin-9 is a ligand for HAVCR2 TIM3 and induces T-helper type 1 lymphocyte (Th1) death. In addition, Galectin-9 suppresses tumor cell metastasis by interfering with the associations CD44, VCAM-1, Integrin α4β1
Galectin-9 Protein, Mouse, Recombinant (GST) is expressed in E. coli expression system with N-GST tag. The predicted molecular weight is 58 KDa and the accession number is O08573-2.
T cell immunoglobulin and mucin domain 3 is a member of the TIM family of immune regulating molecules. Mature cynomolgus TIM3 consists of a 182 amino acid (aa)extracellular domain (ECD), a 21 aa transmembrane segment, and a 78 aa cytoplasmic tail. TIM3 is up-regulated on several populations of activated myeloid cells (macrophage, monocyte, dendritic cell, microglia, mast cell) and T cells (Th1, CD8+, NK, Treg). Its binding to Galectin9 induces a range of immunosuppressive functions which enhance immune tolerance and inhibit anti-tumor immunity. TIM3 ligation attenuates CD8+ and Th1 cell responses and promotes the activity of Treg and myeloid derived suppressor cells. TIM3 interactions with Galectin-9 can trigger immune stimulatory effects, such as the coactivation of NK cell cytotoxicity.