Galectin-9 was first isolated from mouse embryonic kidney in 1997 as a 36 kDa beta-galactoside lectin protein . It contains two carbohydrate recognition domains (CRDs) connected by a linker peptide, making it a tandem-repeat type galectin . The human recombinant form of Galectin-9 is typically produced in E. coli and has a molecular weight of approximately 34-37 kDa .
Galectin-9 plays a significant role in various biological processes:
Recombinant human Galectin-9 is widely used in research to study its effects on cell proliferation, apoptosis, and immune responses. It has been shown to support the adhesion of Jurkat cells, a type of human T cell leukemia . Additionally, it is used to investigate its potential therapeutic applications in cancer and autoimmune diseases.
Recombinant human Galectin-9 is typically produced in E. coli and purified to a high degree of purity (>95%) using SDS-PAGE under reducing conditions . The protein is lyophilized and can be stored at -20°C to -80°C for up to 12 months. Once reconstituted, it should be stored at 4-8°C for short-term use or at -20°C for longer-term storage .