Anaspec has brought out the Z-Fish Anti-p53, a zebrafish-specific p53 antibody.
This antibody was tested in IHC using a 48-hpf zebrafish embryo tail.
Fluorescence detection was carried out with Hilyte Fluor 488 labelled goat anti-rabbit IgG.
Upon addition of the immunising peptide, the signal was abrogated.
Fluorescent western blot analysis using Hilyte Fluor 750 shows an immunoreactive band 53 kD; this band was also abrogated upon addition of the immunising peptide.
One of the most important mammalian cell-cycle checkpoint proteins is the tumour-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 occurs after cells are exposed either to ionising radiation or to UV light.
Serines 6 and 15 were demonstrated to be among the strongest and earliest phosphorylated sites in response to DNA damage-induced post-translational modifications.
Anaspec's collection of p53 antibody products includes both phosphospecific and non-phosphospecific solutions.
