Phospho-Nucleolin (Thr76) antibodies are specialized tools used to study the post-translational modification of nucleolin, a multifunctional protein predominantly located in the nucleolus. Nucleolin plays critical roles in ribosome biogenesis, chromatin organization, and regulation of gene expression, with its activity often modulated by phosphorylation. The Thr76 phosphorylation site is associated with nucleolin’s functional dynamics during cellular stress, DNA damage response, or cell cycle progression. This modification may influence nucleolin’s shuttling between nuclear and cytoplasmic compartments, its interaction with nucleic acids, or its role in stabilizing specific mRNAs.
Antibodies targeting phospho-nucleolin (T76) enable researchers to detect and quantify this modification under various experimental conditions, such as chemotherapy-induced stress or radiation exposure. They are widely used in techniques like Western blotting, immunofluorescence, and immunoprecipitation to explore nucleolin’s involvement in cancer biology, apoptosis, and viral infection mechanisms. Dysregulation of nucleolin phosphorylation has been implicated in tumorigenesis, making these antibodies valuable for studying oncogenic signaling pathways or evaluating therapeutic responses.
Validation of phospho-specificity typically involves phosphatase treatment or comparison with non-phosphorylated controls. Researchers must ensure antibody specificity to avoid cross-reactivity with other phospho-epitopes, as nucleolin contains multiple phosphorylation sites. Overall, these antibodies provide insights into how post-translational modifications fine-tune nucleolin’s diverse cellular functions.