UBAC2 (Ubiquitin-associated domain-containing protein 2), also known as KPC2. is a component of the linear ubiquitin chain assembly complex (LUBAC), which plays a critical role in regulating NF-κB signaling and inflammatory responses. It functions as a ubiquitin-binding adaptor, facilitating the assembly of linear polyubiquitin chains on substrate proteins via interactions with HOIP (the catalytic subunit of LUBAC) and other regulatory proteins. This post-translational modification is essential for activating immune and cell death pathways, particularly in response to cytokines like TNF-α or microbial infections. UBAC2 has been implicated in various cellular processes, including apoptosis, innate immunity, and DNA damage repair. Dysregulation of UBAC2 or LUBAC activity is linked to autoimmune diseases, chronic inflammation, and cancer. Antibodies targeting UBAC2 are valuable tools for studying its expression, localization, and molecular interactions in both physiological and pathological contexts. They are widely used in techniques such as Western blotting, immunoprecipitation, and immunofluorescence to elucidate UBAC2's role in ubiquitination-dependent signaling networks. Recent studies also explore UBAC2's potential as a therapeutic target or biomarker in inflammation-related disorders.