The Phospho-p53 (Ser6) antibody is designed to detect p53 protein phosphorylated at serine 6. a post-translational modification critical for regulating the tumor suppressor activity of p53. The p53 protein plays a central role in maintaining genomic stability by inducing cell cycle arrest, DNA repair, or apoptosis in response to cellular stress, such as DNA damage. Phosphorylation at specific serine residues, including Ser6. modulates p53 stability, localization, and transcriptional activity.
Serine 6 phosphorylation is primarily associated with the early activation of p53 following stress signals. Studies suggest that this modification may be mediated by kinases like protein kinase C (PKC) or casein kinase 1 (CK1), though the precise regulatory mechanisms remain under investigation. Phosphorylation at Ser6 has been linked to enhanced p53 stability by potentially interfering with its ubiquitination and degradation by MDM2. a key negative regulator. Additionally, it may cooperate with other phosphorylation events (e.g., at Ser15 or Ser20) to fine-tune p53’s transcriptional activity toward target genes involved in cell fate decisions.
This antibody is widely used in cancer research to study p53 activation dynamics, DNA damage response pathways, and tumorigenesis. Its specificity enables detection of the phosphorylated form in techniques like Western blotting, immunofluorescence, or immunohistochemistry, aiding in the exploration of p53’s role in both normal physiology and disease.