The USP47 antibody is a crucial tool for studying ubiquitin-specific protease 47 (USP47), a deubiquitinating enzyme (DUB) belonging to the ubiquitin-specific protease family. USP47 regulates protein stability by removing ubiquitin chains from target substrates, thereby counteracting proteasomal degradation. It plays diverse roles in cellular processes, including DNA damage repair, cell cycle progression, and Wnt/β-catenin signaling. USP47 is implicated in maintaining genomic stability by interacting with proteins like NEIL1 and PCNA, and its dysregulation has been linked to cancers, neurodegenerative disorders, and inflammatory diseases.
Antibodies targeting USP47 enable researchers to investigate its expression, localization, and molecular interactions through techniques like Western blotting, immunoprecipitation, and immunofluorescence. These tools are essential for elucidating USP47's physiological functions and pathological contributions, particularly its context-dependent roles as either an oncogene or tumor suppressor. Recent studies also explore USP47's potential as a therapeutic target, with inhibitors under investigation for cancer treatment. Due to its structural complexity and homology with other DUBs, high-specificity USP47 antibodies are critical to avoid cross-reactivity. Ongoing research aims to clarify its regulatory networks, substrate profiles, and tissue-specific roles, driving demand for reliable antibodies in both basic and translational studies.