A Tailored Phospho-p53 Library Probes Antibody Specificity and Recognition Limitations.

ABSTRACT: The tumor suppressor protein p53, known as the "guardian of the genome," is regulated by a complex network of post-translational modifications. Phosphorylations at 7 Ser/Thr residues within the N-terminal transactivation domain 1 (TAD1) play a role in p53 activation, yet their precise mechanisms of action remain elusive due to challenges in accessing well-defined phosphorylated isoforms. To address this limitation, this study harnesses a recently developed approach for the semisynthesis of site-specifically phosphorylated p53 to generate a comprehensive library of singly phosphorylated p53 including all TAD1 sites: Ser6, Ser9, Ser15, Thr18, Ser20, Ser33, and Ser37. The library was then used to probe the specificity of common p53 antibodies in western blot analysis. This study's results con

SUBMITTER: Hess M 

PROVIDER: S-EPMC12278346 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature