HLA-DOB, a member of the human leukocyte antigen (HLA) class II family, plays a role in antigen presentation by loading peptides onto MHC class II molecules for immune recognition. Located near the HLA-DQ and HLA-DR gene clusters on chromosome 6. HLA-DOB encodes the beta chain of the heterodimeric HLA-DO protein, which associates with HLA-DM to regulate peptide editing in antigen-presenting cells. Unlike other HLA class II molecules, HLA-DO (composed of DOA and DOB chains) is not expressed on the cell surface but functions intracellularly to modulate HLA-DM activity, fine-tuning the selection of peptides presented to CD4+ T cells.
Antibodies targeting HLA-DOB are primarily used in research to investigate its expression, interaction with HLA-DM, and role in immune regulation. They are critical tools for studying autoimmune diseases, infections, and cancer, where altered antigen presentation may contribute to pathogenesis. For example, HLA-DOB polymorphisms have been linked to autoimmune conditions like type 1 diabetes and lupus. These antibodies enable detection via techniques like Western blot, flow cytometry, and immunohistochemistry, helping to elucidate tissue-specific expression patterns in B cells, dendritic cells, or thymic epithelial cells. Challenges include its low abundance and intracellular localization, requiring sensitive detection methods. Understanding HLA-DOB's regulatory mechanisms through antibody-based studies may inform therapeutic strategies targeting antigen presentation pathways.