p53 (Phospho-Ser³⁹²) Polyclonal Antibody

p53 is a transcription factor and tumor suppressor encoded by TP53 in humans with roles in cell cycle arrest, apoptosis, senescence, differentiation, and DNA repair.^1,2 It is composed of two N-terminal intrinsically disordered transactivation domains (TADs), a proline-rich domain (PRD), a DNA-binding domain (DBD), a tetramerization domain (TD), and an intrinsically disordered C-terminal domain.¹ p53 is ubiquitously expressed, with protein levels increasing under conditions of extra- or intracellular stress, such as DNA damage, oncogene activation, oxidative stress, or hypoxia.³ It is activated and translocated to the nucleus in response to cellular stress via post-translational modifications, such as phosphorylation, methylation, and acetylation, where it binds p53 consensus DNA-binding elements and regulates transcription of its target genes in a cell-, tissue-, and stress signal type-specific manner.^1,3 p53 is phosphorylated at Ser³⁹² by IκB kinase β (IKKβ) in glutamine-deficient cancer cells.⁴ Loss-of-function and/or gain-of-function mutations in TP53 occur in approximately 50% of human cancers.² Cayman's p53 (Phospho-Ser³⁹²) Polyclonal Antibody can be used for Western blot (WB) applications. This antibody recognizes p53 at ~53 kDa from human and rat samples.

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1. Liu, Y., Tavana, O., and Gu, W. p53 Modifications: Exquisite decorations of the powerful guardian. J. Mol. Cell Biol. 11(7), 564-577 (2019).

2. Stein, Y., Rotter, V., and Aloni-Grinstein, R. Gain-of-function mutant p53: All the roads lead to tumorigenesis. Int. J. Mol. Sci. 20(24), 6197 (2019).

3. Yue, X., Zhao, Y., Xu, Y., et al. Mutant p53 in cancer: Accumulation, gain-of-function and therapy. J. Mol. Biol. 429(11), 1595-1606 (2017).

4. Gabra, M.B.I., Yang, Y., Lowman, X.H., et al. IKKβ activates p53 to promote cancer cell adaptation to glutamine deprivation. Oncogenesis 7(11), 93 (2018).