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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 Loss-of-function and/or gain-of-function mutations in TP53 occur in approximately 50% of human cancers.2 Cayman’s p53 (N-Term) Rabbit Monoclonal Antibody (RM387) can be used for immunohistochemistry (IHC) and Western blot (WB) applications.
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1. p53 Modifications: Exquisite decorations of the powerful guardian. J. Mol. Cell Biol. 11(7), 564-577 (2019).
2. Gain-
3. Mutant p53 in cancer: Accumulation, gain-