Recombinant Human TP53 protein

**Background of TP53 Recombinant Protein**

The TP53 gene, located on chromosome 17p13.1. encodes the p53 protein, a critical tumor suppressor involved in maintaining genomic stability. Often termed the "guardian of the genome," p53 functions as a transcription factor that regulates cell cycle arrest, DNA repair, apoptosis, and senescence in response to cellular stress, such as DNA damage, hypoxia, or oncogenic activation. Structurally, p53 contains distinct domains: an N-terminal transactivation domain, a central DNA-binding domain (DBD), a tetramerization domain, and a C-terminal regulatory domain. Mutations in TP53 are observed in over 50% of human cancers, typically disrupting its DNA-binding capacity and impairing tumor-suppressive functions.

Recombinant TP53 protein is engineered in vitro using expression systems (e.g., *E. coli*, mammalian cells*) to produce functional or mutant forms of p53 for research and therapeutic applications. This protein retains key biochemical properties, enabling studies on p53-DNA interactions, post-translational modifications (e.g., phosphorylation, acetylation), and interactions with regulators like MDM2. which targets p53 for degradation. Recombinant p53 is vital for elucidating mechanisms of carcinogenesis, drug resistance, and mutant p53 gain-of-function effects.

In drug discovery, TP53 recombinant protein aids in screening compounds that restore wild-type p53 activity or disrupt oncogenic mutant p53. It also supports gene therapy strategies, such as delivering functional TP53 via viral vectors. Despite challenges—including p53's complex regulation and mutation heterogeneity—recombinant p53 remains a cornerstone in cancer biology, offering insights into personalized therapies targeting TP53 pathways.