Clone REA424 recognizes the human cellular tumor antigen p53 phosphorylated at serine 37 (pS37). The p53 protein is an important regulator of cell growth and, thus, functions as a tumor suppressor in many tumor types. The p53 tumor suppressor gene is altered or deleted in most solid human tumors. It is tightly regulated and plays a critical role in the cellular response to environmental stress. Upon a cell's exposure to stress, such as hypoxia or genomic damage, the p53 protein is expressed at high levels and is post-translationally modified. These modifications, which include phosphorylation, acetylation, and glycosylation occur rapidly and lead to the activation of p53, resulting in either G1 growth arrest or programmed cell death. Following DNA damage, p53 is phosphorylated on serine residues 15, 20, 33, and 37 within the amino-terminal domain. These phosphorylation events are thought to play a key role in regulating p53 stability and activity. p53 is phosphorylated at S37 in response to both ultraviolet (UV)- and γ-irradiation and may have different functions in response to these two different DNA-damaging treatments. Phosphorylation at this site following UV-irradiation is needed to maintain p53 stability, since mutation of S37 to alanine impaired the accumulation of p53 after exposing cells to UV.
Additional information: Clone REA424 displays negligible binding to Fc receptors.