The tumor suppressor p53 plays a critical role in cellular anticancer defence by inducing cell cycle arrest or apoptosis upon DNA damage or pyrimidine nucleotide starvation. Its upregulation in response to stress signals leads to the transcriptional activation of genes like p21waf1, involved in cell cycle progression, and Bcl-2, involved in apoptosis. Structurally, p53 comprises an N-terminal transactivation, central DNA-binding, oligomerization, and C-terminal regulatory domains. Phosphorylation, particularly at Ser15, is pivotal for p53 activation and stability.
This antibody recognizes one of the most common mutations on the human p53 tumour suppressor protein at residue 175 (Arginine to Histidine; R175H). The antibody also recognizes the mouse equivalent (p53 R172H).
Located in the DNA binding domain, this hotspot mutation is crucial for structural stability as it sits at the zinc-binding site near the DNA binding interface.
The R175H mutation has been implicated in several different cancers including but not limited to cancer of the breast, pancreatic, bone, ovarian, lung, colorectal and prostate.
References: Hwang et. al., Cell Reports, vol. 22 (2018): 299-312.
Chiang et. al., Cancers (Basel), Aug 13; 13(16): 4088.
Product Overview
Key info about the protein can be found under Product Information > Specifications and Features.
Alternative names: Cellular tumor antigen p53, Antigen NY-CO-13, Phosphoprotein p53, Tumor suppressor p53
