The overexpression of the c-erbB-2 (HER-2/neu) gene product, a 185 kDa transmembrane receptor protein, is associated with cell transformation and tumorigenesis.
It shares homology with the epidermal growth factor receptor and intrinsic tyrosine kinase activity, HER-2/neu gene is amplified and overexpressed in 25-30% of human breast and ovarian cancers.
Overexpression of the protein, as determined by immunohistochemistry, is associated with poor prognosis.
One of the most important mammalian cell cycle checkpoint proteins is the tumor suppressor protein, p53.
In normal, undamaged cells, p53 is rapidly degraded.
However, when cells are treated with DNA damage-inducing agents, there is a transient accumulation of p53 protein and it is activated as a transcription factor.
In several types of human cancers, p53 is mutated.
Human p53 protein has been shown to be phosphorylated at several N-terminal and C-terminal sites that affect site-specific DNA binding and interaction with other cellular and viral proteins in vitro.
Phosphorylation at serines 6, 9, 15, 20, 33, 37 occur after cells are exposed either to ionizing radiation or to UV light.
Serines 6 and 15 were demonstrated to be one of the strongest and earliest phosphorylated sites in response to DNA damage-induced posttranslational modifications.
With a focus on providing targeted solutions for cancer research, AnaSpec, a leading provider of integrated proteomics solutions, offers a highly specific selection of c-erbB-2 (HER-2/ neu) and p53 polyclonal antibodies.
AnaSpec's collection of p53 antibody products includes both phosphospecific and non-phosphospecific solutions.
