The HuR antibody targets the RNA-binding protein HuR (Human Antigen R), encoded by the *ELAVL1* gene. A member of the ELAV/Hu protein family, HuR is ubiquitously expressed and plays a critical role in post-transcriptional gene regulation by stabilizing target mRNAs and modulating their translation. It binds to AU-rich elements (AREs) in the 3' untranslated regions (UTRs) of mRNAs involved in cellular processes such as proliferation, survival, inflammation, and stress responses. Dysregulation of HuR is linked to cancer, neurodegeneration, and autoimmune diseases, making it a focus of therapeutic research.
HuR antibodies are widely used in research to study its expression, localization, and function. In normal conditions, HuR resides predominantly in the nucleus but shuttles to the cytoplasm under stress or specific signaling, where it stabilizes mRNAs like those encoding cytokines, oncoproteins, and cell cycle regulators. Antibodies against HuR enable detection via techniques like Western blot, immunohistochemistry (IHC), and immunofluorescence (IF), helping to correlate its subcellular distribution with disease states, particularly cancer progression and chemoresistance.
Commercial HuR antibodies are typically validated for specificity using knockout cell lines or siRNA-mediated knockdown. Researchers rely on these reagents to explore HuR's role in mRNA metabolism and its potential as a biomarker or therapeutic target.