The USP5 antibody is a research tool designed to detect and analyze ubiquitin-specific protease 5 (USP5), a member of the deubiquitinating enzyme (DUB) family. USP5. also known as isopeptidase T, plays a critical role in maintaining cellular ubiquitin homeostasis by cleaving unanchored ubiquitin chains, thereby recycling free ubiquitin for reuse in protein degradation pathways. It specifically recognizes the C-terminal diglycine motif of ubiquitin, enabling it to disassemble polyubiquitin chains and prevent their nonspecific degradation via the proteasome. USP5 is implicated in diverse cellular processes, including DNA repair, cell cycle regulation, and stress response, and dysregulation of its activity has been linked to neurodegenerative diseases, cancer, and immune disorders.
Antibodies targeting USP5 are widely used in molecular and cellular biology to study its expression, localization, and interaction partners. They are essential for techniques like Western blotting, immunoprecipitation, and immunofluorescence to investigate USP5's role in physiological and pathological contexts. Researchers also utilize USP5 antibodies to explore therapeutic strategies, such as inhibiting USP5 to modulate ubiquitin-dependent pathways in disease models. Validated USP5 antibodies typically demonstrate specificity for human, mouse, or rat homologs, and their performance is confirmed across applications using knockout controls or siRNA-based knockdown. Understanding USP5's function through antibody-based assays contributes to deciphering its regulatory mechanisms and potential as a drug target.