CD74 is primarily known for its role as a chaperone molecule for Major Histocompatibility Complex (MHC) class II proteins. It assists in the folding and intracellular trafficking of newly synthesized MHC class II molecules . CD74 self-assembles into trimers, forming a scaffold that facilitates the assembly of MHC class II molecules .
CD74 is critical in the antigen presentation process. It binds to MHC class II molecules in the endoplasmic reticulum, preventing premature binding of peptides. Once the MHC class II-CD74 complex reaches the endosomal/lysosomal compartments, CD74 is degraded, allowing antigenic peptides to bind to MHC class II molecules. This process is essential for the presentation of antigens to CD4+ T cells, which are vital for initiating immune responses .
CD74 is highly expressed in several hematological and solid cancers. Its ability to activate pathways associated with tumor cell survival and proliferation makes it a significant target for cancer research . Over the past 16 years, CD74 has emerged as a commonly detected fusion partner in multiple oncogenic fusion proteins .
Recombinant human CD74 is produced using various expression systems, including Chinese Hamster Ovary (CHO) cells and HEK293 cells . The recombinant protein is often tagged with polyhistidine or other tags to facilitate purification and detection. It is used in research to study its role in immune responses, cancer, and other diseases.
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