Ubiquitin B (UBB) is a member of the ubiquitin family, critical for protein degradation via the ubiquitin-proteasome system (UPS). As a post-translational modifier, ubiquitin tags proteins for proteasomal breakdown, regulating cellular processes like DNA repair, immune response, and apoptosis. UBB, encoded by a polyubiquitin gene, is one of four ubiquitin precursors in humans. Unlike monomeric ubiquitin, UBB is expressed as a linear fusion protein requiring proteolytic processing to release functional ubiquitin monomers.
UBB-specific antibodies are vital tools for studying ubiquitination dynamics. They detect endogenous UBB in tissues or cells, helping researchers visualize ubiquitin-conjugated proteins in pathological conditions such as neurodegenerative diseases (e.g., Alzheimer’s and Parkinson’s) or cancers, where UPS dysfunction leads to abnormal protein aggregation. These antibodies are often used in techniques like Western blotting, immunohistochemistry (IHC), or immunofluorescence (IF) to assess ubiquitination levels or subcellular localization. Some UBB antibodies also distinguish full-length UBB from its mutant forms, like UBB+1—a frameshift variant linked to aging and neurodegeneration.
Research using UBB antibodies has advanced understanding of protein quality control mechanisms and disease pathogenesis. However, cross-reactivity with other ubiquitin isoforms (e.g., UBA, UBC) requires careful validation to ensure specificity. Despite this, UBB antibodies remain indispensable for exploring UPS-related pathways and therapeutic strategies targeting ubiquitination.