P53 is the most important tumor suppressor gene, with broad and powerful functions. Since the discovery of p53 protein in 1979, p53 has been a "star molecule" in molecular biology and oncology. Using p53 as a keyword search in the PubMed database, over 100000 articles can be found.

Bcl-2 is the first discovered anti cell death gene that has been shown to prevent various stimuli induced cell apoptosis, including serum deprivation, heat shock, and chemotherapy agents. In addition, Bcl-2 can also inhibit certain forms of necrotic cell death, such as necrosis induced by hypoxia and respiratory depression.

Caspase is a group of proteases existing in the cytoplasm. Its full name is cysteinyl aspartate specific proteinase. One of the important common features of caspases is that their active sites all contain cysteine, which enables them to specifically cleave peptide bonds on the aspartic acid residues of target proteins. This allows caspases to highly selectively cleave certain proteins. They play a significant role in programmed cell death (including apoptosis, pyroptosis, and necroptosis, etc.) and inflammation. Currently, 11 different caspases have been identified in humans. The mammalian Caspase family proteins can be classified into three major categories based on their structure and function.

AKT (PKB or Rac) is a serine/threonine kinase located at the core node of the PI3K/AKT/mTOR signaling pathway (PAM pathway), regulating basic functions such as transcription, translation, proliferation, growth, and apoptosis of cells. AKT has three subtypes: Akt1, Akt2, and Akt3. The PH domain (pleckstrin homology domain) of AKT specifically binds to PIP2 and PIP3, allowing AKT to be localized on the cell membrane. Subsequently, the kinase domain transfers the phosphate group of ATP to the substrate threonine for phosphorylation.