The Acetyl-p53 (Lys382) antibody is a specialized tool used to detect acetylation of the tumor suppressor protein p53 at lysine residue 382. p53 plays a central role in regulating cell cycle arrest, DNA repair, apoptosis, and genomic stability in response to cellular stress, such as DNA damage or oncogenic signaling. Post-translational modifications, including acetylation, tightly modulate p53’s activity, stability, and interactions with target genes. Acetylation at Lys382 (human; Lys379 in mice) occurs primarily in the C-terminal regulatory domain of p53. a region critical for modulating its DNA-binding affinity. This modification is catalyzed by histone acetyltransferases (HATs) like p300/CBP and counteracted by deacetylases (HDACs).
Acetylation at Lys382 is associated with enhanced transcriptional activation of p53 target genes, promoting cell cycle arrest or apoptosis. It often occurs in response to DNA damage, hypoxia, or other stress signals. The Acetyl-p53 (Lys382) antibody enables researchers to study this specific modification in experimental settings, such as Western blotting, immunoprecipitation, or immunofluorescence, to assess p53 activation status in cancer models, DNA damage studies, or drug screening. Dysregulation of p53 acetylation is linked to tumorigenesis, as mutated or inactivated p53 fails to induce protective responses. This antibody thus serves as a critical reagent in understanding p53’s role in cancer biology, therapeutic resistance, and the functional impact of epigenetic regulation on tumor suppression pathways.