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.WARNING This product is not for human or veterinary use.
