p53 plays a major role in the cellular response to DNA damage and other genomic aberrations. The activation of p53 can lead to either cell cycle arrest and DNA repair, or apoptosis. p53 is phosphorylated at multiple sites in vivo and by several different protein kinases in vitro. p53 can apparently be phosphorylated by ATM, ATR, and DNAPK at Ser15; the phosphorylation impairs the ability of MDM2 to bind p53, promoting both the accumulation and functional activation of p53 in response to DNA damage. Chk2 and Chk1 can phosphorylate p53 at Ser20, enhancing its tetramerization, stability and activity. p53 is phosphorylated at Ser392 in vivo and by CAK in vitro. Phosphorylation of p53 at Ser392 is altered in human tumors and has been reported to influence the growth suppressor function, DNA binding and transcriptional activation of p53.

Cellular tumor antigen p53; Antigen NY-CO-13; Phosphoprotein p53; Tumor suppressor p53; TP53; P53

p04637

Human,Mouse,Rat

WB,IHC,IP

WB 1:500-1:1000
IHC 1:50-1:200
IP 1:50-1:200

~ 53 kDa

Rabbit

This antibody detects endogenous levels of p53 protein only when phosphorylated at Ser15

Synthetic phosphopeptide derived from human p53 around the phosphorylation site of Serine 15.

Polyclonal

Rabbit IgG

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).

PBS with 0.02% sodium azide, 50% glycerol, pH7.2

1mg/ml

Store at 4℃ short term,and store at -20℃ long term. Avoid freeze-thaw cycles.