UbiquitinD (UbD), also known as FAT10 or HLA-F adjacent transcript 10. is a ubiquitin-like protein involved in post-translational modification and proteasomal degradation of target proteins. Unlike canonical ubiquitin, UbD contains two ubiquitin-like domains and is encoded by a gene within the major histocompatibility complex (MHC) class I region. It functions through covalent conjugation to substrates in a process requiring the E1 enzyme UBA6 and E2 enzyme USE1. marking proteins for degradation via the 26S proteasome.
UbD plays roles in immune regulation, cell cycle control, and stress responses. Its expression is tightly regulated, with low levels in most tissues but significant upregulation under inflammatory conditions (e.g., by cytokines like TNF-α and IFN-γ). This links UbD to pathological processes such as cancer, autoimmune diseases, and neurodegeneration. For instance, abnormal UbD accumulation has been observed in hepatocellular carcinoma and Alzheimer's disease models.
UbiquitinD antibodies are essential tools for detecting UbD-protein conjugates, studying degradation pathways, and exploring disease mechanisms. They enable techniques like Western blot, immunofluorescence, and immunohistochemistry to analyze UbD expression patterns, substrate interactions, and cellular localization. Research using these antibodies continues to clarify UbD's dual roles in protein quality control and inflammation-mediated pathologies.